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:9475 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,475 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,430 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 10.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77905,"numValue":10.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77906,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9476 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,476 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,431 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77907,"numValue":9.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77908,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9478 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,478 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,433 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 9.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77911,"numValue":9.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77912,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9479 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,479 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,434 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 8.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77913,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77914,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9480 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,480 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,435 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 6.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77915,"numValue":6.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77916,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9481 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,481 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,436 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 8.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77917,"numValue":8.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77918,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9482 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,482 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,437 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 9.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77919,"numValue":9.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77920,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9483 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,483 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,438 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 10.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77921,"numValue":10.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77922,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9484 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,484 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,439 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 8.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77923,"numValue":8.9,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77924,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9485 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,485 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,440 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 10.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77925,"numValue":10.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77926,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9486 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,486 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,441 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 7.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77927,"numValue":7.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77928,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9487 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,487 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,442 | ProTherm | 5.1 | NMR | GdnHCl | Sodium acetate | 100 mM | 25 | null | null | 6.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1479 | ARTICLE | Detection of rare partially folded molecules in equilibrium with the native conformation of RNaseH. | 1,996 | 10.1038/nsb0996-782 | 8784352 | Nat Struct Biol;3;782-7 | 3 | Marqusee S|Handel T M|Chamberlain A K | [{"numValue":5.1,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"NMR","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BU... | [{"datasets":[],"id":77929,"numValue":6.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":77930,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:9489 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,489 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,952 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 10 | null | null | 8.14 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1032 | ARTICLE | -1 | DOI: 10.1016/0040-6031(95)02495-6 | 3 | Kanaya S|Oobatake M.|Yamasaki T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":79529,"numValue":8.14,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79530,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:9490 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,490 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,953 | ProTherm | 4 | CD | Thermal | glycine/HCl | 10 mM | 10 | null | null | 12 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1032 | ARTICLE | -1 | DOI: 10.1016/0040-6031(95)02495-6 | 3 | Kanaya S|Oobatake M.|Yamasaki T | [{"numValue":4.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine/HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":79531,"numValue":12.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79532,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:9491 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,491 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,954 | ProTherm | 2 | CD | Thermal | glycine-HCl | 10 mM | 10 | null | null | 2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC | 1032 | ARTICLE | -1 | DOI: 10.1016/0040-6031(95)02495-6 | 3 | Kanaya S|Oobatake M.|Yamasaki T | [{"numValue":2.0,"strValue":null,"type":"PH"},{"numValue":10.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":79533,"numValue":2.0,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":79534,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||||
fireprotdb:9492 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,492 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,428 | ProTherm | 5.5 | CD | Thermal | NaOAc | 20 mM | null | KCl | 50 mM | 66 | null | null | null | null | 2.7 | null | null | null | null | null | null | null | null | null | null | yes | TM|DCP|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1601 | ARTICLE | Contributions of folding cores to the thermostabilities of two ribonucleases H. | 2,002 | 10.1110/ps.38602 | 11790848 | Protein Sci;11;381-9 | 3 | Marqusee Susan|Robic Srebrenka|Berger James M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaOAc","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KCl","type":"ION"},{"numValu... | [{"datasets":[],"id":80910,"numValue":66.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80911,"numValue":2.7,"references":[],"strValue":null,"type":"DCP"},{"datasets":[],"id":80912,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:9493 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,493 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,714 | ProTherm | 5.5 | CD | GdnHCl | NaOAc | 20 mM | 25 | KCl | 50 mM | null | null | 7.6 | null | null | null | null | null | 4.9 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1601 | ARTICLE | Contributions of folding cores to the thermostabilities of two ribonucleases H. | 2,002 | 10.1110/ps.38602 | 11790848 | Protein Sci;11;381-9 | 3 | Marqusee Susan|Robic Srebrenka|Berger James M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"NaOAc","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"}... | [{"datasets":[],"id":90253,"numValue":7.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":90254,"numValue":4.9,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":90255,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:9494 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,494 | train | sequence | 183 | 183 | -1 | 155 | -1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 25,715 | ProTherm | 5.5 | CD | Urea | NaOAc | 20 mM | 25 | KCl | 50 mM | null | null | 9.7 | null | null | null | null | null | 2.1 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1601 | ARTICLE | Contributions of folding cores to the thermostabilities of two ribonucleases H. | 2,002 | 10.1110/ps.38602 | 11790848 | Protein Sci;11;381-9 | 3 | Marqusee Susan|Robic Srebrenka|Berger James M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"NaOAc","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{... | [{"datasets":[],"id":90256,"numValue":9.7,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":90257,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":90258,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:9495 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,495 | train | mutant | 466 | 183 | 515 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10N | D10N | 1 | 1 | 0 | 0 | 10 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 759 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D10N | 53.8 | 6.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10N","type":"... | [{"datasets":[],"id":2903,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2904,"numValue":6.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2905,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9496 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,496 | train | mutant | 466 | 183 | 515 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10N | D10N | 1 | 1 | 0 | 0 | 10 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 772 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D10N | 47.4 | -2.6 | null | null | null | null | 90.5 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10N","type":"_... | [{"datasets":[],"id":2942,"numValue":47.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2943,"numValue":-2.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2944,"numValue":90.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9497 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,497 | train | mutant | 466 | 183 | 515 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10N | D10N | 1 | 1 | 0 | 0 | 10 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,676 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D10N | null | null | null | 0.7 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26423,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26424,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9498 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,498 | train | mutant | 466 | 183 | 515 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10N | D10N | 1 | 1 | 0 | 0 | 10 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,798 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D10N | null | null | null | -2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":26731,"numValue":-2.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26732,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9500 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,500 | train | mutant | 467 | 183 | 516 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10A | D10A | 1 | 1 | 0 | 0 | 10 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 773 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D10A | 58.1 | 8.1 | null | null | null | null | 105.3 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10A","type":"_... | [{"datasets":[],"id":2946,"numValue":58.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2947,"numValue":8.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2948,"numValue":105.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9501 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,501 | train | mutant | 467 | 183 | 516 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10A | D10A | 1 | 1 | 0 | 0 | 10 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 3,962 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 2 mM | null | KF | 5 mM | 2RN2_A:D10A | 62.6 | 14.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KF","type":"ION... | [{"datasets":[],"id":14589,"numValue":62.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14590,"numValue":14.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14591,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9502 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,502 | train | mutant | 467 | 183 | 516 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10A | D10A | 1 | 1 | 0 | 0 | 10 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,677 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D10A | null | null | null | -2.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26425,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26426,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9504 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,504 | train | mutant | 467 | 183 | 516 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10A | D10A | 1 | 1 | 0 | 0 | 10 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 11,062 | ProTherm | 5.5 | CD | Urea | Potassium phosphate | 2 mM | 25 | KF | 5 mM | 2RN2_A:D10A | null | null | 13 | -3.3 | null | null | null | null | 2.1 | null | null | null | null | null | null | null | yes | DG|DDG|M|REVERSIBILITY | potapov_with_uniprot_mapping.csv|SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BU... | [{"datasets":[],"id":38079,"numValue":13.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["potapov_with_uniprot_mapping.csv","SAAFEC_S1262.csv"],"id":38080,"numValue":-3.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38081,"numValue":2.1,"references":[],"strValue":null,"type":"M"},{"data... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9505 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,505 | train | mutant | 468 | 183 | 517 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10E | D10E | 1 | 1 | 0 | 0 | 10 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 761 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D10E | 50.4 | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10E","type":"... | [{"datasets":[],"id":2909,"numValue":50.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2910,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2911,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9506 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,506 | train | mutant | 468 | 183 | 517 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10E | D10E | 1 | 1 | 0 | 0 | 10 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 774 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D10E | 53.8 | 3.8 | null | null | null | null | 97.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10E","type":"_... | [{"datasets":[],"id":2950,"numValue":53.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2951,"numValue":3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPT... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9507 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,507 | train | mutant | 468 | 183 | 517 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10E | D10E | 1 | 1 | 0 | 0 | 10 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,678 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D10E | null | null | null | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26427,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26428,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9508 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,508 | train | mutant | 468 | 183 | 517 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10E | D10E | 1 | 1 | 0 | 0 | 10 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,800 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D10E | null | null | null | -1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26735,"numValue":-1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26736,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9509 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,509 | train | mutant | 469 | 183 | 518 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10S | D10S | 1 | 1 | 0 | 0 | 10 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 762 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D10S | 56.2 | 9.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|HotMuSiC_S1626.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10S","type":"... | [{"datasets":[],"id":2912,"numValue":56.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","HotMuSiC_S1626.csv","Saraboji_S1791.csv"],"id":2913,"numValue":9.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["HotMuSiC_S1626.csv"],"id":2914,"numValue":null,"references":[],"strValu... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9510 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,510 | train | mutant | 469 | 183 | 518 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10S | D10S | 1 | 1 | 0 | 0 | 10 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 775 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D10S | 52.4 | 2.4 | null | null | null | null | 120.7 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10S","type":"_... | [{"datasets":[],"id":2954,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2955,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2956,"numValue":120.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9511 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,511 | train | mutant | 469 | 183 | 518 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10S | D10S | 1 | 1 | 0 | 0 | 10 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,679 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D10S | null | null | null | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26429,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26430,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9512 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,512 | train | mutant | 469 | 183 | 518 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10S | D10S | 1 | 1 | 0 | 0 | 10 | D | S | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,801 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D10S | null | null | null | -2.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":26737,"numValue":-2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26738,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9514 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,514 | train | mutant | 470 | 183 | 519 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10H | D10H | 1 | 1 | 0 | 0 | 10 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 776 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D10H | 51.5 | 1.5 | null | null | null | null | 114.6 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:D10H","type":"_... | [{"datasets":[],"id":2958,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2959,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2960,"numValue":114.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9515 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,515 | train | mutant | 470 | 183 | 519 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10H | D10H | 1 | 1 | 0 | 0 | 10 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,680 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D10H | null | null | null | -0.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26431,"numValue":-0.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26432,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9516 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,516 | train | mutant | 470 | 183 | 519 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | D10H | D10H | 1 | 1 | 0 | 0 | 10 | D | H | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 10 | A | E | true | true | 20.744928 | 13.77 | 7,802 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D10H | null | null | null | -2.4 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv"],"id":26739,"numValue":-2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26740,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":81,"numValue":null,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16519,"numValue":9.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9517 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,517 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 3,924 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:G23A | 53.2 | 2.3 | null | null | null | null | 99.3 | 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 | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":14445,"numValue":53.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14446,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14447,"numValue":99.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9518 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,518 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 3,928 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.1 M | 2RN2_A:G23A | 54.3 | 1.8 | null | null | null | null | 91.8 | 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 | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":5.5,"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":14461,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14462,"numValue":1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14463,"numValue":91.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9519 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,519 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 4,080 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:G23A | 54.5 | 1.8 | null | null | null | null | 91.8 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15068,"numValue":54.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15069,"numValue":1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15070,"numValue":91.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9520 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,520 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 4,093 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:G23A | 52.4 | 2.3 | null | null | null | null | 99.3 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15120,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15121,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15122,"numValue":99.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9522 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,522 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 7,455 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | 52.5 | NaCl | 0.1 M | 2RN2_A:G23A | null | null | null | -0.5 | 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 | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.5,"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25903,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25904,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9523 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,523 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 7,619 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.9 | NaCl | 0.1 M | 2RN2_A:G23A | null | null | null | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 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 | 362 | ARTICLE | High resistance of Escherichia coli ribonuclease HI variant with quintuple thermostabilizing mutations to thermal denaturation, acid denaturation, and proteolytic degradation. | 1,995 | 10.1021/bi00025a018 | 7794925 | Biochemistry;34;8115-22 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.9,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26303,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26304,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9524 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,524 | train | mutant | 2,025 | 183 | 2,261 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | G23A | G23A | 1 | 1 | 0 | 0 | 23 | G | A | 8 | CONSERVATION | 2RN2 | 76 | null | 23 | A | E | false | false | 0 | 10.0425 | 7,654 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:G23A | null | null | null | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26373,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26374,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16532,"numValue":8.0,"position":23,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9525 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,525 | train | mutant | 2,071 | 183 | 2,312 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A24V | A24V | 1 | 1 | 0 | 0 | 24 | A | V | 6 | CONSERVATION | 2RN2 | 76 | null | 24 | A | E | false | false | 0 | 11.018 | 4,081 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:A24V | 55.9 | 3.2 | null | null | null | null | 101.2 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15072,"numValue":55.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15073,"numValue":3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15074,"numValue":101.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16533,"numValue":6.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9526 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,526 | train | mutant | 2,071 | 183 | 2,312 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A24V | A24V | 1 | 1 | 0 | 0 | 24 | A | V | 6 | CONSERVATION | 2RN2 | 76 | null | 24 | A | E | false | false | 0 | 11.018 | 4,094 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:A24V | 52.5 | 2.4 | null | null | null | null | 108.7 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15124,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15125,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15126,"numValue":108.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16533,"numValue":6.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9528 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,528 | train | mutant | 2,071 | 183 | 2,312 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A24V | A24V | 1 | 1 | 0 | 0 | 24 | A | V | 6 | CONSERVATION | 2RN2 | 76 | null | 24 | A | E | false | false | 0 | 11.018 | 7,655 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:A24V | null | null | null | -0.73 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26375,"numValue":-0.73,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26376,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16533,"numValue":6.0,"position":24,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9529 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,529 | train | mutant | 2,043 | 183 | 2,282 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | R27A | R27A | 1 | 1 | 0 | 0 | 27 | R | A | 4 | CONSERVATION | 2RN2 | 76 | null | 27 | A | E | true | false | 61.97757 | 25.050909 | 3,963 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 2 mM | null | KF | 5 mM | 2RN2_A:R27A | 42.2 | -5.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"KF","type":"ION... | [{"datasets":[],"id":14592,"numValue":42.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14593,"numValue":-5.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14594,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16536,"numValue":4.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9530 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,530 | train | mutant | 2,043 | 183 | 2,282 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | R27A | R27A | 1 | 1 | 0 | 0 | 27 | R | A | 4 | CONSERVATION | 2RN2 | 76 | null | 27 | A | E | true | false | 61.97757 | 25.050909 | 11,063 | ProTherm | 5.5 | CD | Urea | Potassium phosphate | 2 mM | 25 | KF | 5 mM | 2RN2_A:R27A | null | null | 7.5 | 2.2 | null | null | null | null | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 369 | ARTICLE | Confirmation of the hierarchical folding of RNase H: a protein engineering study. | 1,999 | 10.1038/12277 | 10467093 | Nat Struct Biol;6;825-31 | 3 | Kho J|Marqusee S|Raschke T M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"2 mM","type":"BU... | [{"datasets":[],"id":38083,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":38084,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38085,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":38086,"numValue":null,"... | [{"id":16536,"numValue":4.0,"position":27,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9531 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,531 | train | mutant | 6,841 | 183 | 7,483 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Y28F|R29H|G30A|R31H | Y28F|R29H|G30A|R31H | 4 | 4 | 0 | 0 | 28 | Y | F | 3 | CONSERVATION | 2RN2 | 76 | null | 28|29|30|31 | A | E|T | true | false | 109.620624 | 33.677747 | 14,667 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:Y28F 2RN2_A:R29H 2RN2_A:G30A 2RN2_A:R31H | 47.5 | -2.3 | null | null | null | null | 92.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:Y28F 2RN2_A:R29... | [{"datasets":[],"id":54237,"numValue":47.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54238,"numValue":-2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54239,"numValue":92.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54240,"numValue":null,"references":... | [{"id":16537,"numValue":3.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16538,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16539,"numValue":1.0,"position":30,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9532 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,532 | train | mutant | 6,841 | 183 | 7,483 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Y28F|R29H|G30A|R31H | Y28F|R29H|G30A|R31H | 4 | 4 | 0 | 0 | 28 | Y | F | 3 | CONSERVATION | 2RN2 | 76 | null | 28|29|30|31 | A | E|T | true | false | 109.620624 | 33.677747 | 14,668 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:Y28F 2RN2_A:R29H 2RN2_A:G30A 2RN2_A:R31H | 48.8 | -3.2 | null | null | null | null | 80.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:Y28F 2RN2_A:R29... | [{"datasets":[],"id":54241,"numValue":48.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54242,"numValue":-3.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54243,"numValue":80.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54244,"numValue":null,"references":... | [{"id":16537,"numValue":3.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16538,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16539,"numValue":1.0,"position":30,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9533 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,533 | train | mutant | 6,841 | 183 | 7,483 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Y28F|R29H|G30A|R31H | Y28F|R29H|G30A|R31H | 4 | 4 | 0 | 0 | 28 | Y | F | 3 | CONSERVATION | 2RN2 | 76 | null | 28|29|30|31 | A | E|T | true | false | 109.620624 | 33.677747 | 14,997 | ProTherm | 5.5 | CD | Thermal | glycine-HCl | 10 mM | 52 | 2RN2_A:Y28F 2RN2_A:R29H 2RN2_A:G30A 2RN2_A:R31H | null | null | null | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55176,"numValue":0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55177,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16537,"numValue":3.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16538,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16539,"numValue":1.0,"position":30,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9534 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,534 | train | mutant | 6,841 | 183 | 7,483 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | Y28F|R29H|G30A|R31H | Y28F|R29H|G30A|R31H | 4 | 4 | 0 | 0 | 28 | Y | F | 3 | CONSERVATION | 2RN2 | 76 | null | 28|29|30|31 | A | E|T | true | false | 109.620624 | 33.677747 | 15,058 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:Y28F 2RN2_A:R29H 2RN2_A:G30A 2RN2_A:R31H | null | null | null | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 250 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by strategic replacement of amino acid residues with those from the thermophilic counterpart. | 1,992 | 1328237 | J Biol Chem;267;21535-42 | 5 | Oobatake M|Kanaya S|Nakamura H|Kimura S|Hashimoto T | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":49.8,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55307,"numValue":0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55308,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16537,"numValue":3.0,"position":28,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16538,"numValue":3.0,"position":29,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16539,"numValue":1.0,"position":30,"positionArray":null,"positionRang... | ||||||||||||||
fireprotdb:9535 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,535 | train | mutant | 6,931 | 183 | 7,573 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H62P|T40A|K122R | H62P|T40A|K122R | 3 | 3 | 0 | 0 | 62 | H | P | 2 | CONSERVATION | 2RN2 | 76 | null | 40|62|122 | A | E|L | true | true | 118.827895 | 25.111212 | 14,784 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:T40A 2RN2_A:H62P 2RN2_A:K122R | 55.8 | 3.1 | null | null | null | null | 96.9 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":54620,"numValue":55.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54621,"numValue":3.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54622,"numValue":96.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54623,"numValue":null,"references":[... | [{"id":16549,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16631,"numValue":7.0,"position":122,"positionArray":null,"positionRan... | ||||||||||||
fireprotdb:9536 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,536 | train | mutant | 6,931 | 183 | 7,573 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H62P|T40A|K122R | H62P|T40A|K122R | 3 | 3 | 0 | 0 | 62 | H | P | 2 | CONSERVATION | 2RN2 | 76 | null | 40|62|122 | A | E|L | true | true | 118.827895 | 25.111212 | 14,788 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:T40A 2RN2_A:H62P 2RN2_A:K122R | 51.8 | 1.7 | null | null | null | null | 108.6 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":54636,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54637,"numValue":1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54638,"numValue":108.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54639,"numValue":null,"references":... | [{"id":16549,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16631,"numValue":7.0,"position":122,"positionArray":null,"positionRan... | ||||||||||||
fireprotdb:9538 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,538 | train | mutant | 6,931 | 183 | 7,573 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | H62P|T40A|K122R | H62P|T40A|K122R | 3 | 3 | 0 | 0 | 62 | H | P | 2 | CONSERVATION | 2RN2 | 76 | null | 40|62|122 | A | E|L | true | true | 118.827895 | 25.111212 | 15,047 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:T40A 2RN2_A:H62P 2RN2_A:K122R | null | null | null | -0.52 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55283,"numValue":-0.52,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55284,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16549,"numValue":2.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16631,"numValue":7.0,"position":122,"positionArray":null,"positionRan... | ||||||||||||
fireprotdb:9539 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,539 | train | mutant | 2,078 | 183 | 2,319 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | R41C | R41C | 1 | 1 | 0 | 0 | 41 | R | C | 1 | CONSERVATION | 2RN2 | 76 | null | 41 | A | E | false | false | 120.667532 | 19.741818 | 4,090 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:R41C | 54.3 | 1.6 | null | null | null | null | 102 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15108,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15109,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15110,"numValue":102.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9541 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,541 | train | mutant | 2,078 | 183 | 2,319 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | R41C | R41C | 1 | 1 | 0 | 0 | 41 | R | C | 1 | CONSERVATION | 2RN2 | 76 | null | 41 | A | E | false | false | 120.667532 | 19.741818 | 7,427 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:R41C | null | null | null | -0.44 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":52.7,"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":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv"],"id":25823,"numValue":-0.44,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25824,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9542 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,542 | train | mutant | 2,078 | 183 | 2,319 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | R41C | R41C | 1 | 1 | 0 | 0 | 41 | R | C | 1 | CONSERVATION | 2RN2 | 76 | null | 41 | A | E | false | false | 120.667532 | 19.741818 | 7,664 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:R41C | null | null | null | -0.12 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv"],"id":26393,"numValue":-0.12,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26394,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9543 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,543 | train | mutant | 6,934 | 183 | 7,576 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V|R41C | E119V|R41C | 2 | 2 | 0 | 0 | 119 | E | V | 1 | CONSERVATION | 2RN2 | 76 | null | 41|119 | A | E | true | false | 88.168765 | 21.084242 | 14,787 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:R41C 2RN2_A:E119V | 56.9 | 4.2 | null | null | null | null | 107.2 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":54632,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54633,"numValue":4.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54634,"numValue":107.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54635,"numValue":null,"references":... | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9544 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,544 | train | mutant | 6,934 | 183 | 7,576 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V|R41C | E119V|R41C | 2 | 2 | 0 | 0 | 119 | E | V | 1 | CONSERVATION | 2RN2 | 76 | null | 41|119 | A | E | true | false | 88.168765 | 21.084242 | 14,791 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:R41C 2RN2_A:E119V | 50.4 | 0.3 | null | null | null | null | 101.3 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":54648,"numValue":50.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54649,"numValue":0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54650,"numValue":101.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54651,"numValue":null,"references":... | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9546 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,546 | train | mutant | 6,934 | 183 | 7,576 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E119V|R41C | E119V|R41C | 2 | 2 | 0 | 0 | 119 | E | V | 1 | CONSERVATION | 2RN2 | 76 | null | 41|119 | A | E | true | false | 88.168765 | 21.084242 | 15,050 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:R41C 2RN2_A:E119V | null | null | null | -0.09 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":55289,"numValue":-0.09,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55290,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16550,"numValue":1.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9547 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,547 | train | mutant | 471 | 183 | 520 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48Q | E48Q | 1 | 1 | 0 | 0 | 48 | E | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 764 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:E48Q | 48 | 1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48Q","type":"... | [{"datasets":[],"id":2918,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2919,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2920,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9548 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,548 | train | mutant | 471 | 183 | 520 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48Q | E48Q | 1 | 1 | 0 | 0 | 48 | E | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 777 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:E48Q | 49.8 | -0.2 | null | null | null | null | 99.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Saraboji_S1396.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48Q","type":"_... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":2962,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749... | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9549 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,549 | train | mutant | 471 | 183 | 520 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48Q | E48Q | 1 | 1 | 0 | 0 | 48 | E | Q | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 7,681 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:E48Q | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26433,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26434,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9551 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,551 | train | mutant | 472 | 183 | 521 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48A | E48A | 1 | 1 | 0 | 0 | 48 | E | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 765 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:E48A | 46 | -1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48A","type":"... | [{"datasets":[],"id":2921,"numValue":46.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2922,"numValue":-1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2923,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9552 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,552 | train | mutant | 472 | 183 | 521 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48A | E48A | 1 | 1 | 0 | 0 | 48 | E | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 778 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:E48A | 49.8 | -0.2 | null | null | null | null | 91.6 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48A","type":"_... | [{"datasets":[],"id":2966,"numValue":49.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2967,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2968,"numValue":91.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9553 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,553 | train | mutant | 472 | 183 | 521 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48A | E48A | 1 | 1 | 0 | 0 | 48 | E | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 7,682 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:E48A | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26435,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26436,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9554 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,554 | train | mutant | 472 | 183 | 521 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48A | E48A | 1 | 1 | 0 | 0 | 48 | E | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 7,804 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:E48A | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26743,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26744,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9555 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,555 | train | mutant | 473 | 183 | 522 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48D | E48D | 1 | 1 | 0 | 0 | 48 | E | D | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 766 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:E48D | 46.2 | -0.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48D","type":"... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":2924,"numValue":46.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","potapov_with_uniprot_mapping.csv","Saraboji_S1791.csv"],"id":2925,"numValue":-0.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["potapov_with_uniprot_m... | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9556 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,556 | train | mutant | 473 | 183 | 522 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48D | E48D | 1 | 1 | 0 | 0 | 48 | E | D | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 779 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:E48D | 50.8 | 0.8 | null | null | null | null | 103.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | potapov_with_uniprot_mapping.csv|AUTOMUTE_S1749.csv|AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|Saraboji_S1791.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:E48D","type":"_... | [{"datasets":["potapov_with_uniprot_mapping.csv"],"id":2970,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","potapo... | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9557 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,557 | train | mutant | 473 | 183 | 522 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48D | E48D | 1 | 1 | 0 | 0 | 48 | E | D | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 7,683 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:E48D | null | null | null | -0.2 | 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|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26437,"numValue":-0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":26438,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9558 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,558 | train | mutant | 473 | 183 | 522 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | E48D | E48D | 1 | 1 | 0 | 0 | 48 | E | D | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 48 | A | H | true | false | 20.528799 | 17.881111 | 7,805 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:E48D | null | null | null | 0.2 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 85 | ARTICLE | Thermal stability of Escherichia coli ribonuclease HI and its active site mutants in the presence and absence of the Mg2+ ion. Proposal of a novel catalytic role for Glu48. | 1,996 | 10.1074/jbc.271.51.32729 | 8955106 | J Biol Chem;271;32729-36 | 3 | Oobatake M|Kanaya S|Liu Y | [{"numValue":9.0,"strValue":null,"type":"PH"},{"numValue":47.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-NaOH","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFE... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26745,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":["potapov_with_uniprot_mapping.csv"],"id":26746,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":82,"numValue":null,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16557,"numValue":9.0,"position":48,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9559 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,559 | train | mutant | 341 | 183 | 380 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52I | A52I | 1 | 1 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 602 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52I | 59.2 | 6.2 | null | null | null | null | 84.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52I","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":2395,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2396,"numValue":6.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2397,"numValue":84.8,"references":[],"strValu... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9560 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,560 | train | mutant | 341 | 183 | 380 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52I | A52I | 1 | 1 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,396 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52I | null | null | null | -1.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25754,"numValue":-1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25755,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9561 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,561 | train | mutant | 342 | 183 | 381 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52V | A52V | 1 | 1 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 603 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52V | 58.5 | 5.5 | null | null | null | null | 128 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52V","type":"_... | [{"datasets":[],"id":2399,"numValue":58.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2400,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2401,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9562 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,562 | train | mutant | 342 | 183 | 381 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52V | A52V | 1 | 1 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 4,082 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:A52V | 60.5 | 7.8 | null | null | null | null | 87.5 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":5.5,"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":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":[],"id":15076,"numValue":60.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15077,"numValue":7.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15078,"numValue":87.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9563 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,563 | train | mutant | 342 | 183 | 381 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52V | A52V | 1 | 1 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 4,095 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:A52V | 55.6 | 5.5 | null | null | null | null | 128 | 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 | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"... | [{"datasets":[],"id":15128,"numValue":55.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15129,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15130,"numValue":128.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9564 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,564 | train | mutant | 342 | 183 | 381 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52V | A52V | 1 | 1 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,397 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52V | null | null | null | -1.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|HotMuSiC_S1626.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","HotMuSiC_S1626.csv","potapov_with_uniprot_mapping.csv"],"id":25756,"numValue":-1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25757,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9565 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,565 | train | mutant | 342 | 183 | 381 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52V | A52V | 1 | 1 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,656 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:A52V | null | null | null | -1.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|HotMuSiC_S1626.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 378 | ARTICLE | A novel strategy for stabilization of Escherichia coli ribonuclease HI involving a screen for an intragenic suppressor of carboxyl-terminal deletions. | 1,994 | 7929430 | J Biol Chem;269;26904-11 | 6 | Akasako A|Haruki M|Oobatake M|Kanaya S|Noguchi E|Itaya M | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":50.1,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","HotMuSiC_S1626.csv","potapov_with_uniprot_mapping.csv"],"id":26377,"numValue":-1.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26378,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9567 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,567 | train | mutant | 343 | 183 | 382 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52L | A52L | 1 | 1 | 0 | 0 | 52 | A | L | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,398 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52L | null | null | null | -1.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25758,"numValue":-1.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25759,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9568 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,568 | train | mutant | 344 | 183 | 383 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52C | A52C | 1 | 1 | 0 | 0 | 52 | A | C | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 605 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52C | 55.5 | 2.5 | null | null | null | null | 128.3 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52C","type":"_... | [{"datasets":[],"id":2407,"numValue":55.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2408,"numValue":2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2409,"numValue":128.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9569 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,569 | train | mutant | 344 | 183 | 383 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52C | A52C | 1 | 1 | 0 | 0 | 52 | A | C | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,399 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52C | null | null | null | -0.8 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25760,"numValue":-0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25761,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9570 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,570 | train | mutant | 345 | 183 | 384 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52M | A52M | 1 | 1 | 0 | 0 | 52 | A | M | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 606 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52M | 54.6 | 1.6 | null | null | null | null | 111.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|AUTOMUTE_S1962.csv|Saraboji_S1791.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52M","type":"_... | [{"datasets":[],"id":2411,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":2412,"numValue":1.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2413,"numValue":111.9,"ref... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9571 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,571 | train | mutant | 345 | 183 | 384 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52M | A52M | 1 | 1 | 0 | 0 | 52 | A | M | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,400 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52M | null | null | null | -0.5 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25762,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25763,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9572 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,572 | train | mutant | 346 | 183 | 385 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52F | A52F | 1 | 1 | 0 | 0 | 52 | A | F | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 607 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52F | 51.5 | -1.5 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52F","type":"_... | [{"datasets":[],"id":2415,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2416,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2417,"numValue":89.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9573 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,573 | train | mutant | 346 | 183 | 385 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52F | A52F | 1 | 1 | 0 | 0 | 52 | A | F | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,401 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52F | null | null | null | -0.5 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25764,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25765,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9574 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,574 | train | mutant | 347 | 183 | 386 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52T | A52T | 1 | 1 | 0 | 0 | 52 | A | T | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 608 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52T | 50.3 | -2.7 | null | null | null | null | 107.9 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52T","type":"_... | [{"datasets":[],"id":2419,"numValue":50.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2420,"numValue":-2.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2421,"numValue":107.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9575 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,575 | train | mutant | 347 | 183 | 386 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52T | A52T | 1 | 1 | 0 | 0 | 52 | A | T | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,402 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52T | null | null | null | 0.8 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25766,"numValue":0.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25767,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9576 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,576 | train | mutant | 348 | 183 | 387 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52Q | A52Q | 1 | 1 | 0 | 0 | 52 | A | Q | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 609 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52Q | 49.1 | -3.9 | null | null | null | null | 90.3 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52Q","type":"_... | [{"datasets":[],"id":2423,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2424,"numValue":-3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2425,"numValue":90.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9577 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,577 | train | mutant | 348 | 183 | 387 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52Q | A52Q | 1 | 1 | 0 | 0 | 52 | A | Q | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,403 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52Q | null | null | null | 1.2 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25768,"numValue":1.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25769,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9579 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,579 | train | mutant | 349 | 183 | 388 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52E | A52E | 1 | 1 | 0 | 0 | 52 | A | E | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,404 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52E | null | null | null | 1.5 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25770,"numValue":1.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25771,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9580 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,580 | train | mutant | 350 | 183 | 389 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52P | A52P | 1 | 1 | 0 | 0 | 52 | A | P | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 611 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52P | 47.6 | -5.4 | null | null | null | null | 93 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52P","type":"_... | [{"datasets":[],"id":2431,"numValue":47.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2432,"numValue":-5.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2433,"numValue":93.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9581 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,581 | train | mutant | 350 | 183 | 389 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52P | A52P | 1 | 1 | 0 | 0 | 52 | A | P | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,405 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52P | null | null | null | 1.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25772,"numValue":1.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25773,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9582 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,582 | train | mutant | 351 | 183 | 390 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52S | A52S | 1 | 1 | 0 | 0 | 52 | A | S | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 612 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52S | 47.2 | -5.8 | null | null | null | null | 117.6 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52S","type":"_... | [{"datasets":[],"id":2435,"numValue":47.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2436,"numValue":-5.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2437,"numValue":117.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9583 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,583 | train | mutant | 351 | 183 | 390 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52S | A52S | 1 | 1 | 0 | 0 | 52 | A | S | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,406 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52S | null | null | null | 1.8 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25774,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25775,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9584 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,584 | train | mutant | 352 | 183 | 391 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52N | A52N | 1 | 1 | 0 | 0 | 52 | A | N | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 613 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52N | 47.1 | -5.9 | null | null | null | null | 95.6 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52N","type":"_... | [{"datasets":[],"id":2439,"numValue":47.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2440,"numValue":-5.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2441,"numValue":95.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9585 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,585 | train | mutant | 352 | 183 | 391 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52N | A52N | 1 | 1 | 0 | 0 | 52 | A | N | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,407 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52N | null | null | null | 1.8 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25776,"numValue":1.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25777,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9587 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,587 | train | mutant | 353 | 183 | 392 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52D | A52D | 1 | 1 | 0 | 0 | 52 | A | D | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,408 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52D | null | null | null | 1.9 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":53.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25778,"numValue":1.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25779,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9588 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,588 | train | mutant | 354 | 183 | 393 | 155 | 155 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | 28 | Ribonuclease HI | Escherichia coli (strain K12) | 1 | P0A7Y4 | IPR050092|IPR012337|IPR002156|IPR036397|IPR022892 | 3.1.26.4 | A52Y | A52Y | 1 | 1 | 0 | 0 | 52 | A | Y | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 615 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52Y | 45.4 | -7.6 | null | null | null | null | 70.8 | 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|_PDB_CHAIN_MUTATION | 66 | ARTICLE | Conformational stabilities of Escherichia coli RNase HI variants with a series of amino acid substitutions at a cavity within the hydrophobic core. | 1,997 | 10.1074/jbc.272.30.18686 | 9228039 | J Biol Chem;272;18686-93 | 4 | Akasako A|Haruki M|Oobatake M|Kanaya S | [{"numValue":3.2,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"glycine-HCl","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:A52Y","type":"_... | [{"datasets":[],"id":2447,"numValue":45.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2448,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2449,"numValue":70.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.