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:2323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,323 | train | mutant | 1,445 | 41 | 1,632 | 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 | R96N | R96N | 1 | 1 | 0 | 0 | 96 | R | N | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,804 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96N | null | -8 | null | null | null | null | 116 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10234,"numValue":-8.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10235,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10236,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,324 | train | mutant | 1,445 | 41 | 1,632 | 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 | R96N | R96N | 1 | 1 | 0 | 0 | 96 | R | N | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,149 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96N | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25044,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25045,"numValue":3.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25046,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2326 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,326 | train | mutant | 1,446 | 41 | 1,633 | 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 | R96L | R96L | 1 | 1 | 0 | 0 | 96 | R | L | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,785 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96L | null | -8.6 | null | null | null | null | 114 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10177,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10178,"numValue":114.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10179,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,327 | train | mutant | 1,446 | 41 | 1,633 | 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 | R96L | R96L | 1 | 1 | 0 | 0 | 96 | R | L | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,806 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96L | null | -7.2 | null | null | null | null | 88 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10240,"numValue":-7.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10241,"numValue":88.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10242,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,328 | train | mutant | 1,446 | 41 | 1,633 | 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 | R96L | R96L | 1 | 1 | 0 | 0 | 96 | R | L | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,151 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96L | null | null | null | 3.2 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25050,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25051,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25052,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2329 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,329 | train | mutant | 1,446 | 41 | 1,633 | 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 | R96L | R96L | 1 | 1 | 0 | 0 | 96 | R | L | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,985 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:R96L | null | null | null | 3.2 | 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|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27258,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27259,"numValue":3.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27260,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2330 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,330 | train | mutant | 1,447 | 41 | 1,634 | 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 | R96D | R96D | 1 | 1 | 0 | 0 | 96 | R | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,786 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96D | null | -9.5 | null | null | null | null | 124 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10180,"numValue":-9.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10181,"numValue":124.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10182,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,331 | train | mutant | 1,447 | 41 | 1,634 | 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 | R96D | R96D | 1 | 1 | 0 | 0 | 96 | R | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,807 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96D | null | -5.2 | null | null | null | null | 120 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10243,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10244,"numValue":120.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10245,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,332 | train | mutant | 1,447 | 41 | 1,634 | 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 | R96D | R96D | 1 | 1 | 0 | 0 | 96 | R | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,152 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96D | null | null | null | 3.5 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25053,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25054,"numValue":3.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25055,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,333 | train | mutant | 1,447 | 41 | 1,634 | 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 | R96D | R96D | 1 | 1 | 0 | 0 | 96 | R | D | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,986 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:R96D | null | null | null | 2.3 | 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|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27261,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27262,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27263,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,334 | train | mutant | 1,448 | 41 | 1,635 | 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 | R96F | R96F | 1 | 1 | 0 | 0 | 96 | R | F | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,787 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96F | null | -11.5 | null | null | null | null | 108 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10183,"numValue":-11.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10184,"numValue":108.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10185,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,335 | train | mutant | 1,448 | 41 | 1,635 | 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 | R96F | R96F | 1 | 1 | 0 | 0 | 96 | R | F | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,808 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96F | null | -11.2 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10246,"numValue":-11.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10247,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10248,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,336 | train | mutant | 1,448 | 41 | 1,635 | 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 | R96F | R96F | 1 | 1 | 0 | 0 | 96 | R | F | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,153 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96F | null | null | null | 4.2 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25056,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25057,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25058,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,338 | train | mutant | 1,449 | 41 | 1,636 | 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 | R96W | R96W | 1 | 1 | 0 | 0 | 96 | R | W | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,788 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96W | null | -12.8 | null | null | null | null | 95 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10186,"numValue":-12.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10187,"numValue":95.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10188,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,339 | train | mutant | 1,449 | 41 | 1,636 | 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 | R96W | R96W | 1 | 1 | 0 | 0 | 96 | R | W | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,809 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96W | null | -11 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10249,"numValue":-11.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10250,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10251,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,340 | train | mutant | 1,449 | 41 | 1,636 | 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 | R96W | R96W | 1 | 1 | 0 | 0 | 96 | R | W | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,154 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96W | null | null | null | 4.5 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25059,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25060,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25061,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,341 | train | mutant | 1,449 | 41 | 1,636 | 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 | R96W | R96W | 1 | 1 | 0 | 0 | 96 | R | W | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,988 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:R96W | null | null | null | 4.2 | 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|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27267,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27268,"numValue":4.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27269,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,342 | train | mutant | 1,450 | 41 | 1,637 | 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 | R96Y | R96Y | 1 | 1 | 0 | 0 | 96 | R | Y | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,789 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96Y | null | -13.2 | null | null | null | null | 99 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10189,"numValue":-13.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10190,"numValue":99.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10191,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,343 | train | mutant | 1,450 | 41 | 1,637 | 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 | R96Y | R96Y | 1 | 1 | 0 | 0 | 96 | R | Y | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,810 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96Y | null | -12.3 | null | null | null | null | 73 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10252,"numValue":-12.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10253,"numValue":73.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10254,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2344 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,344 | train | mutant | 1,450 | 41 | 1,637 | 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 | R96Y | R96Y | 1 | 1 | 0 | 0 | 96 | R | Y | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,155 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96Y | null | null | null | 4.7 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25062,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25063,"numValue":4.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25064,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,345 | train | mutant | 1,450 | 41 | 1,637 | 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 | R96Y | R96Y | 1 | 1 | 0 | 0 | 96 | R | Y | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,989 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:R96Y | null | null | null | 4.5 | 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|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27270,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27271,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27272,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,347 | train | mutant | 1,451 | 41 | 1,638 | 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 | R96P | R96P | 1 | 1 | 0 | 0 | 96 | R | P | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 2,811 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | null | 2LZM_A:R96P | null | -16.6 | null | null | null | null | 85 | null | null | null | null | null | null | null | null | null | Unknown | DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM, 1.4 mM, 8.6 mM","type":"BUFFER_CONC"},... | [{"datasets":[],"id":10255,"numValue":-16.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10256,"numValue":85.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":10257,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,348 | train | mutant | 1,451 | 41 | 1,638 | 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 | R96P | R96P | 1 | 1 | 0 | 0 | 96 | R | P | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,156 | ProTherm | 5.35 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 58 | 2LZM_A:R96P | null | null | null | 5.5 | 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 | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":5.35,"strValue":null,"type":"PH"},{"numValue":58.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":25065,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":25066,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25067,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,349 | train | mutant | 1,451 | 41 | 1,638 | 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 | R96P | R96P | 1 | 1 | 0 | 0 | 96 | R | P | 6 | CONSERVATION | 1L63|2LZM | 49|80 | null | 96 | A | H | false | false | 76.733023 | 19.384545 | 7,990 | ProTherm | 3.05 | CD | Thermal | Sodium chloride, Acetic acid, Sodium acetate | 100 mM, 1.4 mM, 8.6 mM | 44 | 2LZM_A:R96P | null | null | null | 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|_PDB_CHAIN_MUTATION | 244 | ARTICLE | Contributions of all 20 amino acids at site 96 to the stability and structure of T4 lysozyme. | 2,009 | 10.1002/pro.94 | 19384988 | Protein Sci;18;871-80 | 4 | Mooers Blaine H M|Baase Walter A|Matthews Brian W|Wray Jonathan W | [{"numValue":3.05,"strValue":null,"type":"PH"},{"numValue":44.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium chloride, Acetic acid, Sodium acetate","type":"BUFFER"},{"numValue":null... | [{"datasets":[],"id":27273,"numValue":1.8,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":27274,"numValue":6.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27275,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6887,"numValue":6.0,"position":96,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,350 | train | mutant | 235 | 41 | 265 | 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 | A98S | A98S | 1 | 1 | 0 | 0 | 98 | A | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 421 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A98S | 44.08 | -7.47 | null | null | null | null | 97 | 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":1735,"numValue":44.08,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1736,"numValue":-7.47,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1737,"numValue":97.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,351 | train | mutant | 235 | 41 | 265 | 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 | A98S | A98S | 1 | 1 | 0 | 0 | 98 | A | S | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 7,590 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.55 | KCl | 25 mM | 2LZM_A:A98S | null | null | null | 2.5 | 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":26237,"numValue":2.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26238,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,352 | train | mutant | 359 | 41 | 398 | 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 | A98V | A98V | 1 | 1 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 621 | ProTherm | 3 | CD | Thermal | HCl | null | 2LZM_A:A98V | 38.6 | -13 | 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|_PDB_CHAIN_MUTATION | 68 | ARTICLE | Structure and thermal stability of phage T4 lysozyme. | 1,987 | 10.1016/0076-6879(87)54093-9 | 3323816 | Methods Enzymol;154;511-33 | 2 | Alber T|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":"HCl","type":"BUFFER"},{"numValue":null,"strValue":"2LZM_A:A98V","type":"_PDB_CHAIN_MUTATION"}] | [{"datasets":[],"id":2469,"numValue":38.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2470,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2471,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,353 | train | mutant | 359 | 41 | 398 | 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 | A98V | A98V | 1 | 1 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 990 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A98V | 39.3 | -14.8 | null | null | null | null | 25.5 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":3709,"numValue":39.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3710,"numValue":-14.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3711,"numValue":25.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,354 | train | mutant | 359 | 41 | 398 | 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 | A98V | A98V | 1 | 1 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,778 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98V | 42.5 | -9.2 | null | null | null | null | 67 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.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":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13946,"numValue":42.5,"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":13947,"numValue":-9.2,"references":[],"strValue"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,355 | train | mutant | 359 | 41 | 398 | 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 | A98V | A98V | 1 | 1 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 8,094 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:A98V | null | null | null | 4.9 | null | 2.41 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":27521,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":27522,"numValue":4.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27523,"numValue":null,"references":[],"strValue":"yes","type":"R... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,356 | train | mutant | 359 | 41 | 398 | 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 | A98V | A98V | 1 | 1 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 12,614 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A98V | null | null | null | 5.02 | null | null | null | 3.8 | 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":45745,"numValue":5.02,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45746,"numValue":3.8,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45747,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,357 | train | mutant | 1,960 | 41 | 2,190 | 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 | A98C | A98C | 1 | 1 | 0 | 0 | 98 | A | C | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,777 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98C | 49.1 | -2.6 | null | null | null | null | 105 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.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":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13942,"numValue":49.1,"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":13943,"numValue":-2.6,"references":[],"strValue"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2358 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,358 | train | mutant | 1,961 | 41 | 2,191 | 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 | A98L | A98L | 1 | 1 | 0 | 0 | 98 | A | L | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,779 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98L | 37.8 | -13.9 | null | null | null | null | 49 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q3421.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":[],"id":13950,"numValue":37.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":13951,"numValue":-13.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":13952,"numValue":49.0,"references":[],"strValue":null,"type":"DHV... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,360 | train | mutant | 1,963 | 41 | 2,193 | 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 | A98M | A98M | 1 | 1 | 0 | 0 | 98 | A | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,781 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98M | 42.4 | -9.3 | null | null | null | null | 75 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q3421.csv|AUTOMUTE_S1749.csv|EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1791.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":["STRUM_Q3421.csv"],"id":13958,"numValue":42.4,"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":13959,"numValue":-9.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S5... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,361 | train | mutant | 1,964 | 41 | 2,194 | 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 | A98F | A98F | 1 | 1 | 0 | 0 | 98 | A | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,782 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98F | 31.3 | -20.4 | null | null | null | null | 18 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.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":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13962,"numValue":31.3,"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":13963,"numValue":-20.4,"references":[],"strValue... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,362 | train | mutant | 1,965 | 41 | 2,195 | 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 | A98W | A98W | 1 | 1 | 0 | 0 | 98 | A | W | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 3,783 | ProTherm | 3 | CD | Thermal | phosphoric acid,Potassium phosphate, | 3 mM,17 mM, | null | KCl | 25 mM | 2LZM_A:A98W | 32.4 | -19.3 | null | null | null | null | 20 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.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":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":13966,"numValue":32.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q3421.csv"],"id":13967,"numValue":-19.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,363 | train | mutant | 5,834 | 41 | 6,399 | 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 | A98T | A98T | 1 | 1 | 0 | 0 | 98 | A | T | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98 | A | H | false | false | 0 | 13.585 | 12,613 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A98T | null | null | null | 3.83 | null | null | null | 4.4 | 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":45742,"numValue":3.83,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":45743,"numValue":4.4,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":45744,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:2364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,364 | train | mutant | 6,782 | 41 | 7,424 | 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 | A98V|T152S | A98V|T152S | 2 | 2 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|152 | A | H | false | false | 0.067185 | 14.169643 | 14,577 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:T152S | 40.2 | -13.9 | null | null | null | null | 36.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":53907,"numValue":40.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53908,"numValue":-13.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53909,"numValue":36.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53910,"numValue":null,"references"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2365 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,365 | train | mutant | 6,782 | 41 | 7,424 | 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 | A98V|T152S | A98V|T152S | 2 | 2 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|152 | A | H | false | false | 0.067185 | 14.169643 | 15,113 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:T152S | null | null | null | 4.8 | null | 2.41 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":55452,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55453,"numValue":4.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55454,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2366 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,366 | train | mutant | 6,782 | 41 | 7,424 | 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 | A98V|T152S | A98V|T152S | 2 | 2 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|152 | A | H | false | false | 0.067185 | 14.169643 | 15,489 | ProTherm | 7 | Gel electrophoresis | Urea | imidazole,MOPS, | 0.05 M,0.05 M, | 22 | 2LZM_A:A98V 2LZM_A:T152S | null | null | null | 5.5 | null | null | null | 3.6 | null | null | null | null | null | null | null | null | Unknown | DDG|CM|REVERSIBILITY | 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":[],"id":56871,"numValue":5.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":56872,"numValue":3.6,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":56873,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:2367 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,367 | train | mutant | 6,783 | 41 | 7,425 | 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 | A98V|V149C|T152S | A98V|V149C|T152S | 3 | 3 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|149|152 | A | H | false | false | 0.134371 | 13.697619 | 14,578 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:V149C 2LZM_A:T152S | 42 | -12.1 | null | null | null | null | 74.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":53911,"numValue":42.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53912,"numValue":-12.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53913,"numValue":74.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53914,"numValue":null,"references"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2368 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,368 | train | mutant | 6,783 | 41 | 7,425 | 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 | A98V|V149C|T152S | A98V|V149C|T152S | 3 | 3 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|149|152 | A | H | false | false | 0.134371 | 13.697619 | 15,114 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:V149C 2LZM_A:T152S | null | null | null | 4.4 | null | 2.41 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":55455,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55456,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55457,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2369 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,369 | train | mutant | 6,784 | 41 | 7,426 | 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 | A98V|V149I|T152S | A98V|V149I|T152S | 3 | 3 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|149|152 | A | H | false | false | 0.134371 | 13.697619 | 14,579 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:V149I 2LZM_A:T152S | 42.1 | -12 | null | null | null | null | 69.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"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":53915,"numValue":42.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53916,"numValue":-12.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53917,"numValue":69.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53918,"numValue":null,"references"... | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2370 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,370 | train | mutant | 6,784 | 41 | 7,426 | 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 | A98V|V149I|T152S | A98V|V149I|T152S | 3 | 3 | 0 | 0 | 98 | A | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 98|149|152 | A | H | false | false | 0.134371 | 13.697619 | 15,115 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 40 | KCl | 25 mM | 2LZM_A:A98V 2LZM_A:V149I 2LZM_A:T152S | null | null | null | 4.4 | null | 2.41 | 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 | 102 | ARTICLE | Structural and thermodynamic analysis of the packing of two alpha-helices in bacteriophage T4 lysozyme. | 1,991 | 10.1016/0022-2836(91)80079-a | 1920439 | J Mol Biol;221;647-67 | 5 | Alber T|Daopin S|Baase W A|Matthews B W|Wozniak J A | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":40.0,"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":"20 mM","type"... | [{"datasets":[],"id":55458,"numValue":2.41,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55459,"numValue":4.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55460,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6889,"numValue":8.0,"position":98,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6940,"numValue":8.0,"position":149,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6943,"numValue":7.0,"position":152,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2371 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,371 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 41 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L99A | 36.1 | -15.7 | null | null | null | 2.5 | 79.6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"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":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":136,"numValue":36.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":137,"numValue":-15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":138,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":1... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2372 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,372 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 958 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99A | 36.06 | -15.7 | null | null | null | null | 80 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3593,"numValue":36.06,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3594,"numValue":-15.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3595,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2373 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,373 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 968 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99A | 53.48 | -11.4 | null | null | null | null | 110 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3633,"numValue":53.48,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3634,"numValue":-11.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3635,"numValue":110.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2374 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,374 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 2,026 | ProTherm | 5.4 | CD, Fluorescence | Thermal | acetic acid, sodium acetate | 1.4 mM, 8.6 mM | null | Sodium Chloride | 0.10 M | 1L63_A:L99A | 53.6 | -11.7 | null | null | null | null | 104 | null | null | null | null | null | null | null | null | null | Yes(80%) | 2.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|EASE-MM_S1676.csv|SVM-WIN31_SVM-3D12_S499.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","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","STRUM_Q3421.csv"],"id":7572,"numValue":53.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mut... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2375 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,375 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 3,824 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99A | 36.1 | -15.6 | null | null | null | null | 76 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q306.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J 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":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":14086,"numValue":36.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv"],"id":14087,"numValue":-15.6,"references":[],"strValue":nul... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2376 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,376 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 3,827 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:L99A | 53.7 | -11.5 | null | null | null | null | 101 | null | null | null | null | null | null | null | null | null | yes(>80%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":14098,"numValue":53.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14099,"numValue":-11.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14100,"numValue":101.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2377 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,377 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,793 | 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:L99A | null | null | null | 4.1 | 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":24081,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24082,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":24083,"numValue":null,"references":[],"strValue":"Yes(80%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||
fireprotdb:2378 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,378 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,816 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.2 | NaCl | 0.10 M | 2LZM_A:L99A | null | null | null | 4 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>80%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.2,"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":"BUF... | [{"datasets":[],"id":24149,"numValue":4.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24150,"numValue":null,"references":[],"strValue":"yes(>80%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2379 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,379 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,971 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:L99A | null | null | null | 4.5 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24576,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24577,"numValue":4.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24578,"numValue":null,"references":[],"strV... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2380 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,380 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,502 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | 51.8 | KCl | 0.025 M | 2LZM_A:L99A | null | null | null | 5 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.020 M","ty... | [{"datasets":[],"id":26003,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26004,"numValue":5.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26005,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2382 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,382 | train | mutant | 41 | 41 | 45 | 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 | L99A | L99A | 1 | 1 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,521 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 25 mM | 2LZM_A:L99A | null | null | null | 4.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":26054,"numValue":4.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26055,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2383 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,383 | train | mutant | 163 | 41 | 191 | 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 | L99M | L99M | 1 | 1 | 0 | 0 | 99 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 300 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate, | 1.4 mM,8.6 mM, | null | NaCl | 0.1 M | 2LZM_A:L99M | 64 | -1.3 | null | null | null | 2.5 | 134 | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|DCP|DHVH|REVERSIBILITY | HotMuSiC_S1626.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"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,"strValu... | [{"datasets":["HotMuSiC_S1626.csv"],"id":1225,"numValue":64.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":1226,"numValue":-1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1227,"numValue":2.5,"references":[],"strValu... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2384 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,384 | train | mutant | 163 | 41 | 191 | 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 | L99M | L99M | 1 | 1 | 0 | 0 | 99 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 961 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99M | 49.76 | -2 | null | null | null | null | 116 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3605,"numValue":49.76,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3606,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3607,"numValue":116.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2385 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,385 | train | mutant | 163 | 41 | 191 | 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 | L99M | L99M | 1 | 1 | 0 | 0 | 99 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 971 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99M | 63.38 | -1.5 | null | null | null | null | 140 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3645,"numValue":63.38,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3646,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3647,"numValue":140.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2386 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,386 | train | mutant | 163 | 41 | 191 | 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 | L99M | L99M | 1 | 1 | 0 | 0 | 99 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,771 | ProTherm | 5.42 | CD | Thermal | Acetic acid,Sodium acetate | 1.4 mM,8.6 mM | 65.3 | NaCl | 0.1 M | 2LZM_A:L99M | null | null | null | 0.4 | 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 | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 33 | ARTICLE | A test of the "jigsaw puzzle" model for protein folding by multiple methionine substitutions within the core of T4 lysozyme. | 1,996 | 10.1073/pnas.93.22.12155 | 8901549 | Proc Natl Acad Sci U S A;93;12155-8 | 3 | Baase W A|Matthews B W|Gassner N C | [{"numValue":5.42,"strValue":null,"type":"PH"},{"numValue":65.3,"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 m... | [{"datasets":[],"id":24015,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":24016,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24017,"numValue":null,"references":[],"strValue":"Unknown","type":"R... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2387 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,387 | train | mutant | 163 | 41 | 191 | 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 | L99M | L99M | 1 | 1 | 0 | 0 | 99 | L | M | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,974 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:L99M | null | null | null | 0.6 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24585,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24586,"numValue":0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24587,"numValue":null,"references":[],"strValue":"yes","type":"RE... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2389 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,389 | train | mutant | 573 | 41 | 624 | 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 | L99V | L99V | 1 | 1 | 0 | 0 | 99 | L | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 959 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99V | 45.16 | -6.6 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3597,"numValue":45.16,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3598,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3599,"numValue":101.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2390 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,390 | train | mutant | 573 | 41 | 624 | 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 | L99V | L99V | 1 | 1 | 0 | 0 | 99 | L | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 969 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99V | 59.68 | -5.2 | null | null | null | null | 121 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3637,"numValue":59.68,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3638,"numValue":-5.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3639,"numValue":121.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2392 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,392 | train | mutant | 573 | 41 | 624 | 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 | L99V | L99V | 1 | 1 | 0 | 0 | 99 | L | V | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,510 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99V | null | null | null | 2.3 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | DCP|DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26023,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv"],"id":26024,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26025,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2393 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,393 | train | mutant | 574 | 41 | 625 | 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 | L99I | L99I | 1 | 1 | 0 | 0 | 99 | L | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 960 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99I | 47.76 | -4 | null | null | null | null | 107 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3601,"numValue":47.76,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3602,"numValue":-4.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3603,"numValue":107.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2394 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,394 | train | mutant | 574 | 41 | 625 | 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 | L99I | L99I | 1 | 1 | 0 | 0 | 99 | L | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 970 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99I | 61.18 | -3.7 | null | null | null | null | 127 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3641,"numValue":61.18,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3642,"numValue":-3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3643,"numValue":127.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2395 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,395 | train | mutant | 574 | 41 | 625 | 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 | L99I | L99I | 1 | 1 | 0 | 0 | 99 | L | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,973 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:L99I | null | null | null | 1.5 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24582,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24583,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24584,"numValue":null,"references":[],"strValue":"yes","type":"RE... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2396 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,396 | train | mutant | 574 | 41 | 625 | 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 | L99I | L99I | 1 | 1 | 0 | 0 | 99 | L | I | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,511 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99I | null | null | null | 1.4 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26026,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26027,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26028,"numValue":null,"references... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2397 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,397 | train | mutant | 575 | 41 | 626 | 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 | L99F | L99F | 1 | 1 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 962 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F | 50.66 | -1.1 | null | null | null | null | 109 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":3609,"numValue":50.66,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3610,"numValue":-1.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3611,"numValue":109.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2398 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,398 | train | mutant | 575 | 41 | 626 | 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 | L99F | L99F | 1 | 1 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 972 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99F | 64.18 | -0.7 | null | null | null | null | 126 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":3649,"numValue":64.18,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":3650,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":3651,"numValue":126.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2399 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,399 | train | mutant | 575 | 41 | 626 | 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 | L99F | L99F | 1 | 1 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,975 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:L99F | null | null | null | 0.3 | null | 3.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":24588,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":24589,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24590,"numValue":null,"references":[],"strValue":"yes","type":"RE... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2400 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,400 | train | mutant | 575 | 41 | 626 | 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 | L99F | L99F | 1 | 1 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,513 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F | null | null | null | 0.4 | null | 2.5 | null | null | null | null | null | null | null | null | null | null | yes | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER_CO... | [{"datasets":[],"id":26032,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26033,"numValue":0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26034,"numValue":null,"references":[],"strValue":"yes","type":"RE... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2401 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,401 | train | mutant | 1,989 | 41 | 2,225 | 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 | L99G | L99G | 1 | 1 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 3,825 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99G | 22.5 | -29.2 | null | null | null | null | 48 | null | null | null | null | null | null | null | null | null | yes(>95%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J 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":14090,"numValue":22.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14091,"numValue":-29.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14092,"numValue":48.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2402 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,402 | train | mutant | 1,989 | 41 | 2,225 | 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 | L99G | L99G | 1 | 1 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 3,828 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.10 M | 2LZM_A:L99G | 44.9 | -20.3 | null | null | null | null | 74 | null | null | null | null | null | null | null | null | null | yes(>80%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":14102,"numValue":44.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14103,"numValue":-20.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14104,"numValue":74.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2403 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,403 | train | mutant | 1,989 | 41 | 2,225 | 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 | L99G | L99G | 1 | 1 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 6,817 | ProTherm | 5.4 | CD | Thermal | Sodium acetate | 10 mM | 65.2 | NaCl | 0.10 M | 2LZM_A:L99G | null | null | null | 6.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>80%) | DDG|REVERSIBILITY | guerios_625_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"numValue":5.4,"strValue":null,"type":"PH"},{"numValue":65.2,"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":"BUF... | [{"datasets":["guerios_625_map.csv","potapov_with_uniprot_mapping.csv"],"id":24151,"numValue":6.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":24152,"numValue":null,"references":[],"strValue":"yes(>80%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:2404 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,404 | train | mutant | 1,989 | 41 | 2,225 | 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 | L99G | L99G | 1 | 1 | 0 | 0 | 99 | L | G | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99 | A | H | false | false | 0.201556 | 12.825 | 7,522 | ProTherm | 3 | CD | Thermal | Potassium phosphate | 20 mM | 51.7 | KCl | 25 mM | 2LZM_A:L99G | null | null | null | 7.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes(>95%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 358 | ARTICLE | Structural analysis of a non-contiguous second-site revertant in T4 lysozyme shows that increasing the rigidity of a protein can enhance its stability. | 1,999 | 10.1006/jmbi.1999.3102 | 10512706 | J Mol Biol;292;1111-20 | 5 | Baase W A|Lindstrom J D|Poteete A R|Weaver L H|Wray J W | [{"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":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type"... | [{"datasets":[],"id":26056,"numValue":7.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26057,"numValue":null,"references":[],"strValue":"yes(>95%)","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2405 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,405 | train | mutant | 6,699 | 41 | 7,341 | 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 | L99A|F153A | L99A|F153A | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,440 | ProTherm | 3.01 | CD | Thermal | Potassium phosphate | 0.020 M | null | KCl | 0.025 M | 2LZM_A:L99A 2LZM_A:F153A | 10 | -41.8 | null | null | null | 2.5 | 6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DCP|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 5 | ARTICLE | Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect. | 1,992 | 10.1126/science.1553543 | 1553543 | Science;255;178-83 | 5 | Blaber M|Eriksson A E|Baase W A|Zhang X J|Heinz D W | [{"numValue":3.01,"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":"0.020 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type"... | [{"datasets":[],"id":53386,"numValue":10.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53387,"numValue":-41.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53388,"numValue":2.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":53389,"numValue":6.0,"references":[]... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2406 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,406 | train | mutant | 6,699 | 41 | 7,341 | 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 | L99A|F153A | L99A|F153A | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,575 | ProTherm | 3.01 | CD | Thermal | KH2PO4 | 20 mM | null | KCl | 25 mM | 2LZM_A:L99A 2LZM_A:F153A | 9.86 | -41.8 | null | null | null | null | 6 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVa... | [{"datasets":[],"id":53899,"numValue":9.86,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53900,"numValue":-41.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53901,"numValue":6.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53902,"numValue":null,"references":... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2407 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,407 | train | mutant | 6,699 | 41 | 7,341 | 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 | L99A|F153A | L99A|F153A | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,576 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | null | KCl | 20 mM | 2LZM_A:L99A 2LZM_A:F153A | 42.08 | -22.8 | null | null | null | null | 56 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"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":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numVal... | [{"datasets":[],"id":53903,"numValue":42.08,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53904,"numValue":-22.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53905,"numValue":56.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53906,"numValue":null,"references... | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2408 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,408 | train | mutant | 6,699 | 41 | 7,341 | 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 | L99A|F153A | L99A|F153A | 2 | 2 | 0 | 0 | 99 | L | A | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,928 | ProTherm | 5.7 | CD | Thermal | KH2PO4 | 10 mM | 64.88 | KCl | 20 mM | 2LZM_A:L99A 2LZM_A:F153A | null | null | null | 6.9 | null | 3.5 | 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 | 100 | ARTICLE | Similar hydrophobic replacements of Leu99 and Phe153 within the core of T4 lysozyme have different structural and thermodynamic consequences. | 1,993 | 10.1006/jmbi.1993.1077 | 8433369 | J Mol Biol;229;747-69 | 3 | Eriksson A E|Baase W A|Matthews B W | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.88,"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":"10 mM","type":"BUFFER_CON... | [{"datasets":[],"id":55010,"numValue":3.5,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":55011,"numValue":6.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55012,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2410 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,410 | train | mutant | 6,734 | 41 | 7,376 | 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 | L99F|M102L | L99F|M102L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102 | A | H | false | false | 1.400244 | 14.201875 | 14,493 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L | 49.42 | -2.34 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53578,"numValue":49.42,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53579,"numValue":-2.34,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53580,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2411 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,411 | train | mutant | 6,734 | 41 | 7,376 | 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 | L99F|M102L | L99F|M102L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102 | A | H | false | false | 1.400244 | 14.201875 | 14,502 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:M102L | 62.68 | -2.21 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53605,"numValue":62.68,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53606,"numValue":-2.21,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53607,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2414 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,414 | train | mutant | 6,735 | 41 | 7,377 | 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 | L99F|V111I | L99F|V111I | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111 | A | H | false | false | 0.201556 | 16.1125 | 14,494 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:V111I | 49.06 | -2.7 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53581,"numValue":49.06,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53582,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53583,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2415 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,415 | train | mutant | 6,735 | 41 | 7,377 | 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 | L99F|V111I | L99F|V111I | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111 | A | H | false | false | 0.201556 | 16.1125 | 14,503 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:V111I | 62.38 | -2.51 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53608,"numValue":62.38,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53609,"numValue":-2.51,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53610,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2416 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,416 | train | mutant | 6,735 | 41 | 7,377 | 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 | L99F|V111I | L99F|V111I | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111 | A | H | false | false | 0.201556 | 16.1125 | 14,920 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:V111I | null | null | null | 0.93 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"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_... | [{"datasets":[],"id":54994,"numValue":0.93,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54995,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2417 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,417 | train | mutant | 6,735 | 41 | 7,377 | 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 | L99F|V111I | L99F|V111I | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111 | A | H | false | false | 0.201556 | 16.1125 | 15,000 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:V111I | null | null | null | 0.82 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55182,"numValue":0.82,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55183,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2418 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,418 | train | mutant | 6,736 | 41 | 7,378 | 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 | L99F|F153L | L99F|F153L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,495 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:F153L | 51.85 | 0.09 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53584,"numValue":51.85,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53585,"numValue":0.09,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53586,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2419 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,419 | train | mutant | 6,736 | 41 | 7,378 | 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 | L99F|F153L | L99F|F153L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,504 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:F153L | 65.47 | 0.58 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53611,"numValue":65.47,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53612,"numValue":0.58,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53613,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2420 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,420 | train | mutant | 6,736 | 41 | 7,378 | 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 | L99F|F153L | L99F|F153L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 14,921 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:F153L | null | null | null | -0.21 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"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_... | [{"datasets":[],"id":54996,"numValue":-0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":54997,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2421 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,421 | train | mutant | 6,736 | 41 | 7,378 | 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 | L99F|F153L | L99F|F153L | 2 | 2 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|153 | A | H | true | false | 0.465854 | 14.907045 | 15,001 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:F153L | null | null | null | -0.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55184,"numValue":-0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55185,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:2422 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,422 | train | mutant | 6,739 | 41 | 7,381 | 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 | L99F|M102L|V111I | L99F|M102L|V111I | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111 | A | H | false | false | 1.000681 | 15.934583 | 14,498 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I | 47.24 | -4.02 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53593,"numValue":47.24,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53594,"numValue":-4.02,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53595,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2424 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,424 | train | mutant | 6,739 | 41 | 7,381 | 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 | L99F|M102L|V111I | L99F|M102L|V111I | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111 | A | H | false | false | 1.000681 | 15.934583 | 14,924 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I | null | null | null | 1.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"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_... | [{"datasets":[],"id":55002,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55003,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2426 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,426 | train | mutant | 6,740 | 41 | 7,382 | 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 | L99F|M102L|F153L | L99F|M102L|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|153 | A | H | true | false | 1.17688 | 15.130947 | 14,499 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:F153L | 51.08 | -0.68 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53596,"numValue":51.08,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53597,"numValue":-0.68,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53598,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2427 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,427 | train | mutant | 6,740 | 41 | 7,382 | 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 | L99F|M102L|F153L | L99F|M102L|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|153 | A | H | true | false | 1.17688 | 15.130947 | 14,508 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:F153L | 64.15 | -0.74 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53623,"numValue":64.15,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53624,"numValue":-0.74,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53625,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2429 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,429 | train | mutant | 6,740 | 41 | 7,382 | 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 | L99F|M102L|F153L | L99F|M102L|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|153 | A | H | true | false | 1.17688 | 15.130947 | 15,005 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:F153L | null | null | null | 0.21 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55192,"numValue":0.21,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55193,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2430 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,430 | train | mutant | 6,741 | 41 | 7,383 | 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 | L99F|V111I|F153L | L99F|V111I|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111|153 | A | H | true | false | 0.377755 | 16.404697 | 14,500 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:V111I 2LZM_A:F153L | 50.08 | -1.73 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53599,"numValue":50.08,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53600,"numValue":-1.73,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53601,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2431 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,431 | train | mutant | 6,741 | 41 | 7,383 | 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 | L99F|V111I|F153L | L99F|V111I|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111|153 | A | H | true | false | 0.377755 | 16.404697 | 14,509 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:V111I 2LZM_A:F153L | 63.64 | -1.25 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53626,"numValue":63.64,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53627,"numValue":-1.25,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53628,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2432 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,432 | train | mutant | 6,741 | 41 | 7,383 | 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 | L99F|V111I|F153L | L99F|V111I|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111|153 | A | H | true | false | 0.377755 | 16.404697 | 14,926 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | 64.89 | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:V111I 2LZM_A:F153L | null | null | null | 0.43 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"strValue":null,"type":"PH"},{"numValue":64.89,"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_... | [{"datasets":[],"id":55006,"numValue":0.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55007,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2433 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,433 | train | mutant | 6,741 | 41 | 7,383 | 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 | L99F|V111I|F153L | L99F|V111I|F153L | 3 | 3 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|111|153 | A | H | true | false | 0.377755 | 16.404697 | 15,006 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | 51.76 | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:V111I 2LZM_A:F153L | null | null | null | 0.55 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"strValue":null,"type":"PH"},{"numValue":51.76,"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":"20 mM","type":"BUFFER... | [{"datasets":[],"id":55194,"numValue":0.55,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55195,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6944,"numValue":7.0,"position":153,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2434 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,434 | train | mutant | 6,742 | 41 | 7,384 | 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 | L99F|M102L|V111I|F153L | L99F|M102L|V111I|F153L | 4 | 4 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111|153 | A | H | true | false | 0.933049 | 16.19821 | 14,501 | ProTherm | 3.01 | CD | Thermal | phosphate | 20 mM | null | KCl | 25 mM | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I 2LZM_A:F153L | 49.94 | -1.82 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":3.01,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"nu... | [{"datasets":[],"id":53602,"numValue":49.94,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53603,"numValue":-1.82,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53604,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... | |||||||||||
fireprotdb:2435 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 2,435 | train | mutant | 6,742 | 41 | 7,384 | 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 | L99F|M102L|V111I|F153L | L99F|M102L|V111I|F153L | 4 | 4 | 0 | 0 | 99 | L | F | 8 | CONSERVATION | 1L63|2LZM | 49|80 | null | 99|102|111|153 | A | H | true | false | 0.933049 | 16.19821 | 14,510 | ProTherm | 5.7 | CD | Thermal | phosphate | 10 mM | null | KCl | 0.2 M | 2LZM_A:L99F 2LZM_A:M102L 2LZM_A:V111I 2LZM_A:F153L | 62.82 | -2.07 | 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 | 53 | ARTICLE | Design and structural analysis of alternative hydrophobic core packing arrangements in bacteriophage T4 lysozyme. | 1,992 | 10.1016/0022-2836(92)90475-y | 1569571 | J Mol Biol;224;1143-59 | 3 | Baase W A|Matthews B W|Hurley J H | [{"numValue":5.7,"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":53629,"numValue":62.82,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53630,"numValue":-2.07,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53631,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":6890,"numValue":8.0,"position":99,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6893,"numValue":9.0,"position":102,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":6902,"numValue":8.0,"position":111,"positionArray":null,"positionRange... |
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