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:9589 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,589 | 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 | 7,409 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52Y | null | null | null | 2.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":25780,"numValue":2.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25781,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9590 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,590 | train | mutant | 355 | 183 | 394 | 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 | A52G | A52G | 1 | 1 | 0 | 0 | 52 | A | G | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 616 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52G | 44.1 | -8.9 | null | null | null | null | 91 | 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:A52G","type":"_... | [{"datasets":[],"id":2451,"numValue":44.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2452,"numValue":-8.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2453,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9592 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,592 | train | mutant | 356 | 183 | 395 | 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 | A52H | A52H | 1 | 1 | 0 | 0 | 52 | A | H | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 617 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52H | 41.2 | -11.8 | null | null | null | null | 84.7 | 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 | 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:A52H","type":"_... | [{"datasets":[],"id":2455,"numValue":41.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2456,"numValue":-11.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2457,"numValue":84.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9594 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,594 | train | mutant | 357 | 183 | 396 | 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 | A52K | A52K | 1 | 1 | 0 | 0 | 52 | A | K | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 618 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52K | 33.5 | -19.5 | 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:A52K","type":"_... | [{"datasets":[],"id":2459,"numValue":33.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2460,"numValue":-19.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2461,"numValue":70.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9595 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,595 | train | mutant | 357 | 183 | 396 | 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 | A52K | A52K | 1 | 1 | 0 | 0 | 52 | A | K | 7 | CONSERVATION | 2RN2 | 76 | null | 52 | A | H | true | false | 0.806226 | 9.926 | 7,412 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52K | null | null | null | 5.9 | 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":25786,"numValue":5.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25787,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9596 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,596 | train | mutant | 6,753 | 183 | 7,395 | 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|V74A | A52V|V74A | 2 | 2 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,525 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52V 2RN2_A:V74A | 51.3 | -1.7 | null | null | null | null | 106.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53695,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53696,"numValue":-1.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53697,"numValue":106.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53698,"numValue":null,"references"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9597 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,597 | train | mutant | 6,753 | 183 | 7,395 | 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|V74A | A52V|V74A | 2 | 2 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,984 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52V 2RN2_A:V74A | 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|_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":[],"id":55149,"numValue":0.52,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55150,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9598 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,598 | train | mutant | 6,754 | 183 | 7,396 | 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|V74A | A52L|V74A | 2 | 2 | 0 | 0 | 52 | A | L | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,526 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52L 2RN2_A:V74A | 54.2 | 1.2 | null | null | null | null | 105.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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:A52L 2RN2_A:V74... | [{"datasets":[],"id":53699,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53700,"numValue":1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53701,"numValue":105.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53702,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9599 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,599 | train | mutant | 6,754 | 183 | 7,396 | 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|V74A | A52L|V74A | 2 | 2 | 0 | 0 | 52 | A | L | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,985 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52L 2RN2_A:V74A | null | null | null | -0.36 | 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 | 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":[],"id":55151,"numValue":-0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55152,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9600 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,600 | train | mutant | 6,755 | 183 | 7,397 | 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|V74A | A52I|V74A | 2 | 2 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,527 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52I 2RN2_A:V74A | 56.9 | 3.9 | null | null | null | null | 101.9 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53703,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53704,"numValue":3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53705,"numValue":101.9,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53706,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9601 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,601 | train | mutant | 6,755 | 183 | 7,397 | 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|V74A | A52I|V74A | 2 | 2 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,986 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52I 2RN2_A:V74A | null | null | null | -1.19 | 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 | 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":[],"id":55153,"numValue":-1.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55154,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9602 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,602 | train | mutant | 6,756 | 183 | 7,398 | 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|V74A | A52F|V74A | 2 | 2 | 0 | 0 | 52 | A | F | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,528 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52F 2RN2_A:V74A | 48.4 | -4.6 | null | null | null | null | 85.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53707,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53708,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53709,"numValue":85.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53710,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9604 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,604 | train | mutant | 6,757 | 183 | 7,399 | 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 | A52G|V74L | A52G|V74L | 2 | 2 | 0 | 0 | 52 | A | G | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,529 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52G 2RN2_A:V74L | 48.4 | -4.6 | null | null | null | null | 97.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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:A52G 2RN2_A:V74... | [{"datasets":[],"id":53711,"numValue":48.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53712,"numValue":-4.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53713,"numValue":97.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53714,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9605 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,605 | train | mutant | 6,757 | 183 | 7,399 | 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 | A52G|V74L | A52G|V74L | 2 | 2 | 0 | 0 | 52 | A | G | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,988 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52G 2RN2_A:V74L | null | null | null | 1.4 | 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 | 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":[],"id":55157,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55158,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9606 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,606 | train | mutant | 6,758 | 183 | 7,400 | 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|V74L | A52V|V74L | 2 | 2 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,530 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52V 2RN2_A:V74L | 61 | 8.07 | null | null | null | null | 125.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53715,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53716,"numValue":8.07,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53717,"numValue":125.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53718,"numValue":null,"references"... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9607 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,607 | train | mutant | 6,758 | 183 | 7,400 | 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|V74L | A52V|V74L | 2 | 2 | 0 | 0 | 52 | A | V | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,989 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52V 2RN2_A:V74L | null | null | null | -2.43 | 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 | 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":[],"id":55159,"numValue":-2.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55160,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9608 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,608 | train | mutant | 6,759 | 183 | 7,401 | 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|V74L | A52L|V74L | 2 | 2 | 0 | 0 | 52 | A | L | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,531 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52L 2RN2_A:V74L | 57.9 | 4.9 | null | null | null | null | 118.1 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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:A52L 2RN2_A:V74... | [{"datasets":[],"id":53719,"numValue":57.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53720,"numValue":4.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53721,"numValue":118.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53722,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9609 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,609 | train | mutant | 6,759 | 183 | 7,401 | 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|V74L | A52L|V74L | 2 | 2 | 0 | 0 | 52 | A | L | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,990 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52L 2RN2_A:V74L | null | null | null | -1.49 | 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 | 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":[],"id":55161,"numValue":-1.49,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55162,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9610 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,610 | train | mutant | 6,760 | 183 | 7,402 | 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|V74L | A52I|V74L | 2 | 2 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,532 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52I 2RN2_A:V74L | 56.9 | 3.9 | null | null | null | null | 122.3 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53723,"numValue":56.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53724,"numValue":3.9,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53725,"numValue":122.3,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53726,"numValue":null,"references":... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9611 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,611 | train | mutant | 6,760 | 183 | 7,402 | 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|V74L | A52I|V74L | 2 | 2 | 0 | 0 | 52 | A | I | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,991 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52I 2RN2_A:V74L | null | null | null | -1.19 | 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 | 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":[],"id":55163,"numValue":-1.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55164,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9612 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,612 | train | mutant | 6,761 | 183 | 7,403 | 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|V74L | A52F|V74L | 2 | 2 | 0 | 0 | 52 | A | F | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,533 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:A52F 2RN2_A:V74L | 53.1 | 0.1 | null | null | null | null | 99.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | 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 2RN2_A:V74... | [{"datasets":[],"id":53727,"numValue":53.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53728,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53729,"numValue":99.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53730,"numValue":null,"references":[... | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9613 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,613 | train | mutant | 6,761 | 183 | 7,403 | 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|V74L | A52F|V74L | 2 | 2 | 0 | 0 | 52 | A | F | 7 | CONSERVATION | 2RN2 | 76 | null | 52|74 | A | H | true | false | 1.679637 | 11.623714 | 14,992 | ProTherm | 3.2 | CD | Thermal | glycine-HCl | 10 mM | 53 | 2RN2_A:A52F 2RN2_A:V74L | null | null | null | -0.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":[],"id":55165,"numValue":-0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55166,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16561,"numValue":7.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9614 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,614 | train | mutant | 2,041 | 183 | 2,280 | 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 | I53A | I53A | 1 | 1 | 0 | 0 | 53 | I | A | 8 | CONSERVATION | 2RN2 | 76 | null | 53 | A | H | false | false | 0 | 10.25 | 3,960 | ProTherm | 5.5 | CD | Thermal | Potassium phosphate | 2 mM | null | KF | 5 mM | 2RN2_A:I53A | 35.7 | -12.1 | 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|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":14583,"numValue":35.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14584,"numValue":-12.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14585,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16562,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9617 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,617 | train | mutant | 3,942 | 183 | 4,444 | 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 | I53L | I53L | 1 | 1 | 0 | 0 | 53 | I | L | 8 | CONSERVATION | 2RN2 | 76 | null | 53 | A | H | false | false | 0 | 10.25 | 9,119 | ProTherm | 5.5 | CD | Urea | sodium acetate | 20 mM | 25 | KCl | 50 mM | 2RN2_A:I53L | null | null | 8.3 | 1.4 | null | null | null | null | 2.3 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 622 | ARTICLE | Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. | 2,004 | 10.1016/j.jmb.2003.10.052 | 14672667 | J Mol Biol;335;609-18 | 3 | Spudich Giulietta M|Miller Erik J|Marqusee Susan | [{"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":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":31034,"numValue":8.3,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31035,"numValue":1.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31036,"numValue":2.3,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31037,"numValue":null,"... | [{"id":16562,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9618 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,618 | train | mutant | 3,943 | 183 | 4,445 | 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 | I53F | I53F | 1 | 1 | 0 | 0 | 53 | I | F | 8 | CONSERVATION | 2RN2 | 76 | null | 53 | A | H | false | false | 0 | 10.25 | 9,120 | ProTherm | 5.5 | CD | Urea | sodium acetate | 20 mM | 25 | KCl | 50 mM | 2RN2_A:I53F | null | null | 5.8 | 3.9 | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 622 | ARTICLE | Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. | 2,004 | 10.1016/j.jmb.2003.10.052 | 14672667 | J Mol Biol;335;609-18 | 3 | Spudich Giulietta M|Miller Erik J|Marqusee Susan | [{"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":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":31038,"numValue":5.8,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":31039,"numValue":3.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31040,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31041,"numValue":null,"... | [{"id":16562,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9619 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,619 | train | mutant | 3,944 | 183 | 4,446 | 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 | I53D | I53D | 1 | 1 | 0 | 0 | 53 | I | D | 8 | CONSERVATION | 2RN2 | 76 | null | 53 | A | H | false | false | 0 | 10.25 | 9,121 | ProTherm | 5.5 | CD | Urea | sodium acetate | 20 mM | 25 | KCl | 50 mM | 2RN2_A:I53D | null | null | 5.6 | 4.1 | null | null | null | null | 2 | null | null | null | null | null | null | null | Unknown | DG|DDG|M|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 622 | ARTICLE | Destabilization of the Escherichia coli RNase H kinetic intermediate: switching between a two-state and three-state folding mechanism. | 2,004 | 10.1016/j.jmb.2003.10.052 | 14672667 | J Mol Biol;335;609-18 | 3 | Spudich Giulietta M|Miller Erik J|Marqusee Susan | [{"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":"sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER... | [{"datasets":[],"id":31042,"numValue":5.6,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":31043,"numValue":4.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":31044,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":31045,"numValue":null,"references":[],"st... | [{"id":16562,"numValue":8.0,"position":53,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9621 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,621 | train | mutant | 6,933 | 183 | 7,575 | 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|K60R | E119V|K60R | 2 | 2 | 0 | 0 | 119 | E | V | 5 | CONSERVATION | 2RN2 | 76 | null | 60|119 | A | L|E | true | false | 112.206976 | 26.272222 | 14,786 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:K60R 2RN2_A:E119V | 55 | 2.3 | null | null | null | null | 98.6 | 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":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":54628,"numValue":55.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54629,"numValue":2.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54630,"numValue":98.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54631,"numValue":null,"references":[... | [{"id":16569,"numValue":5.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9622 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,622 | train | mutant | 6,933 | 183 | 7,575 | 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|K60R | E119V|K60R | 2 | 2 | 0 | 0 | 119 | E | V | 5 | CONSERVATION | 2RN2 | 76 | null | 60|119 | A | L|E | true | false | 112.206976 | 26.272222 | 14,790 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:K60R 2RN2_A:E119V | 49.9 | -0.2 | null | null | null | null | 108.7 | 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":54644,"numValue":49.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54645,"numValue":-0.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54646,"numValue":108.7,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":54647,"numValue":null,"references"... | [{"id":16569,"numValue":5.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9623 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,623 | train | mutant | 6,933 | 183 | 7,575 | 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|K60R | E119V|K60R | 2 | 2 | 0 | 0 | 119 | E | V | 5 | CONSERVATION | 2RN2 | 76 | null | 60|119 | A | L|E | true | false | 112.206976 | 26.272222 | 14,994 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:K60R 2RN2_A:E119V | null | null | null | -0.63 | 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":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":[],"id":55169,"numValue":-0.63,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55170,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16569,"numValue":5.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9624 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,624 | train | mutant | 6,933 | 183 | 7,575 | 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|K60R | E119V|K60R | 2 | 2 | 0 | 0 | 119 | E | V | 5 | CONSERVATION | 2RN2 | 76 | null | 60|119 | A | L|E | true | false | 112.206976 | 26.272222 | 15,049 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:K60R 2RN2_A:E119V | null | null | null | 0.06 | 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":55287,"numValue":0.06,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55288,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16569,"numValue":5.0,"position":60,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16628,"numValue":3.0,"position":119,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9625 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,625 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 2,885 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H62P | 53.2 | 3.4 | null | null | null | null | 109.5 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | STRUM_Q306.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | 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:H62P","type":"_... | [{"datasets":["STRUM_Q306.csv","STRUM_Q3421.csv"],"id":10481,"numValue":53.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv","STRUM_Q306.csv","STRUM_Q3421.csv"],"id":10482,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q306.csv","STRU... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9626 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,626 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 2,887 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | 2RN2_A:H62P | 56.1 | 4.1 | 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|_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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H62P","type"... | [{"datasets":[],"id":10489,"numValue":56.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":10490,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10491,"numValue":102.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9627 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,627 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 3,925 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:H62P | 54.3 | 3.4 | null | null | null | null | 109.5 | 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 | 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":14449,"numValue":54.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14450,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14451,"numValue":109.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9628 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,628 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 3,929 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.1 M | 2RN2_A:H62P | 56.6 | 4.1 | 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 | 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":14465,"numValue":56.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14466,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14467,"numValue":102.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9629 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,629 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,084 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:H62P | 56.8 | 4.1 | 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":15084,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15085,"numValue":4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15086,"numValue":102.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9630 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,630 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,097 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:H62P | 53.5 | 3.4 | null | null | null | null | 109.5 | 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":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":15136,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15137,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15138,"numValue":109.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9631 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,631 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,423 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:H62P | 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|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","potapov_with_uniprot_mapping.csv"],"id":25815,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25816,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9632 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,632 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,456 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | 52.5 | NaCl | 0.1 M | 2RN2_A:H62P | 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|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","potapov_with_uniprot_mapping.csv"],"id":25905,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25906,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9633 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,633 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,464 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52 | 2RN2_A:H62P | 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 | 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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":25924,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25925,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9634 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,634 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,620 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.9 | NaCl | 0.1 M | 2RN2_A:H62P | null | null | null | -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|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":26305,"numValue":-1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26306,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9635 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,635 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,658 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:H62P | null | null | null | -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|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":26381,"numValue":-1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26382,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9636 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,636 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,732 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:H62P | null | null | null | -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 | 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":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26573,"numValue":-1.0,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26574,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9637 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,637 | train | mutant | 1,524 | 183 | 1,716 | 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 | H62P | 1 | 1 | 0 | 0 | 62 | H | P | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 10,454 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 25 | 2RN2_A:H62P | null | null | 9.89 | -0.74 | null | null | null | 1.98 | 4.98 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | 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":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":35819,"numValue":9.89,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":35820,"numValue":-0.74,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":35821,"numValue":4.98,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":35822,"numValue":1.... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9638 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,638 | train | mutant | 2,044 | 183 | 2,283 | 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 | H62A | H62A | 1 | 1 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 3,964 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H62A | 50.7 | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara 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":"2RN2_A:H62A","type":"_... | [{"datasets":[],"id":14595,"numValue":50.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14596,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14597,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9639 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,639 | train | mutant | 2,044 | 183 | 2,283 | 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 | H62A | H62A | 1 | 1 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 3,971 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H62A | 51.2 | 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 | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H62A","typ... | [{"datasets":[],"id":14616,"numValue":51.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14617,"numValue":1.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14618,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9640 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,640 | train | mutant | 2,044 | 183 | 2,283 | 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 | H62A | H62A | 1 | 1 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 10,727 | ProTherm | 5.5 | Fluorescence | GdnHCl | Sodium acetate | 20 mM | 25 | NaCl | 0.1 M | 2RN2_A:H62A | null | null | 9.64 | -0.38 | null | null | null | 1.86 | 5.19 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 701 | ARTICLE | Effect of mutagenesis at each of five histidine residues on enzymatic activity and stability of ribonuclease H from Escherichia coli. | 1,991 | 10.1111/j.1432-1033.1991.tb16033.x | 1645658 | Eur J Biochem;198;437-40 | 5 | Kanaya S|Katayanagi K|Morikawa K|Inoue H|Ohtsuka E | [{"numValue":5.5,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","t... | [{"datasets":[],"id":36869,"numValue":9.64,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36870,"numValue":-0.38,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36871,"numValue":5.19,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9641 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,641 | train | mutant | 2,044 | 183 | 2,283 | 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 | H62A | H62A | 1 | 1 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 11,064 | ProTherm | 5.5 | CD | GdnHCl | Sodium acetate | 20 mM | 25 | 2RN2_A:H62A | null | null | 9.57 | -0.36 | null | null | null | 1.86 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara 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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFF... | [{"datasets":[],"id":38087,"numValue":9.57,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":38088,"numValue":-0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38089,"numValue":1.86,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9642 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,642 | train | mutant | 2,044 | 183 | 2,283 | 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 | H62A | H62A | 1 | 1 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 11,068 | ProTherm | 8.2 | CD | GdnHCl | Tris-HCl | 20 mM | 25 | 2RN2_A:H62A | null | null | 9.07 | -0.58 | null | null | null | 1.76 | null | null | null | null | null | null | null | null | yes | DG|DDG|CM|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":8.2,"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":"Tris-HCl","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CON... | [{"datasets":[],"id":38103,"numValue":9.07,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":38104,"numValue":-0.58,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":38105,"numValue":1.76,"references":[],"strValue":null,"type":"CM"},{"datasets":[],"id":38106,"numValue":null,"references":[... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9643 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,643 | train | mutant | 2,072 | 183 | 2,313 | 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 | H62R | H62R | 1 | 1 | 0 | 0 | 62 | H | R | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,083 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:H62R | 54 | 1.3 | null | null | null | null | 97.1 | 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":15080,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15081,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15082,"numValue":97.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9644 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,644 | train | mutant | 2,072 | 183 | 2,313 | 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 | H62R | H62R | 1 | 1 | 0 | 0 | 62 | H | R | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,096 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:H62R | 50 | -0.1 | null | null | null | null | 114.5 | 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":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":15132,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15133,"numValue":-0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15134,"numValue":114.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9645 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,645 | train | mutant | 2,072 | 183 | 2,313 | 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 | H62R | H62R | 1 | 1 | 0 | 0 | 62 | H | R | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,422 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52.7 | NaCl | 0.1 M | 2RN2_A:H62R | null | null | null | -0.36 | 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":25813,"numValue":-0.36,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25814,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9646 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,646 | train | mutant | 2,072 | 183 | 2,313 | 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 | H62R | H62R | 1 | 1 | 0 | 0 | 62 | H | R | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,657 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:H62R | null | null | null | 0.03 | 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":26379,"numValue":0.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26380,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9647 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,647 | train | mutant | 2,073 | 183 | 2,314 | 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 | H62D | H62D | 1 | 1 | 0 | 0 | 62 | H | D | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,085 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:H62D | 52.1 | -0.6 | null | null | null | null | 97.8 | 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":15088,"numValue":52.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15089,"numValue":-0.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15090,"numValue":97.8,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9648 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,648 | train | mutant | 2,073 | 183 | 2,314 | 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 | H62D | H62D | 1 | 1 | 0 | 0 | 62 | H | D | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 4,098 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:H62D | 52.3 | 2.2 | null | null | null | null | 118.4 | 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":15140,"numValue":52.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15141,"numValue":2.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15142,"numValue":118.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9650 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,650 | train | mutant | 2,073 | 183 | 2,314 | 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 | H62D | H62D | 1 | 1 | 0 | 0 | 62 | H | D | 3 | CONSERVATION | 2RN2 | 76 | null | 62 | A | L | true | false | 136.962166 | 26.803 | 7,659 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.1 | NaCl | 0.1 M | 2RN2_A:H62D | null | null | null | -0.67 | 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":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"],"id":26383,"numValue":-0.67,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26384,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9652 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,652 | train | mutant | 6,928 | 183 | 7,570 | 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 | H62A|H83A | H62A|H83A | 2 | 2 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62|83 | A | L|H | true | false | 128.631432 | 28.5645 | 14,781 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H62A 2RN2_A:H83A | 51.5 | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H62A 2RN2_... | [{"datasets":[],"id":54611,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54612,"numValue":1.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54613,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:9653 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,653 | train | mutant | 6,930 | 183 | 7,572 | 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 | H62A|H83A|H124A|H127A | H62A|H83A|H124A|H127A | 4 | 4 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62|83|124|127 | A | L|H|T | true | true | 121.961866 | 27.986 | 14,779 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:H62A 2RN2_A:H83A 2RN2_A:H124A 2RN2_A:H127A | 54.9 | 5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara 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":"2RN2_A:H62A 2RN2_A:H83... | [{"datasets":[],"id":54605,"numValue":54.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54606,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54607,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRan... | |||||||||||||
fireprotdb:9654 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,654 | train | mutant | 6,930 | 183 | 7,572 | 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 | H62A|H83A|H124A|H127A | H62A|H83A|H124A|H127A | 4 | 4 | 0 | 0 | 62 | H | A | 3 | CONSERVATION | 2RN2 | 76 | null | 62|83|124|127 | A | L|H|T | true | true | 121.961866 | 27.986 | 14,783 | ProTherm | 7.8 | CD | Thermal | Sodium phosphate | 20 mM | null | 2RN2_A:H62A 2RN2_A:H83A 2RN2_A:H124A 2RN2_A:H127A | 51.7 | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 370 | ARTICLE | pH-dependent thermostabilization of Escherichia coli ribonuclease HI by histidine to alanine substitutions. | 1,993 | 10.1016/0168-1656(93)90129-b | 7764048 | J Biotechnol;28;117-36 | 4 | Oobatake M|Kanaya S|Nakamura H|Ikehara M | [{"numValue":7.8,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2RN2_A:H62A 2RN2_... | [{"datasets":[],"id":54617,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":54618,"numValue":1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":54619,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16571,"numValue":3.0,"position":62,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16592,"numValue":1.0,"position":83,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":16633,"numValue":9.0,"position":124,"positionArray":null,"positionRan... | |||||||||||||
fireprotdb:9655 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,655 | train | mutant | 1,793 | 183 | 2,007 | 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 | S68G | S68G | 1 | 1 | 0 | 0 | 68 | S | G | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 3,446 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:S68G | 41.8 | -8 | null | null | null | null | 84.7 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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:S68G","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12736,"numValue":41.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12737,"numValue":-8.0,"references":[],"strValue":nul... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9656 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,656 | train | mutant | 1,793 | 183 | 2,007 | 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 | S68G | S68G | 1 | 1 | 0 | 0 | 68 | S | G | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 7,726 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:S68G | 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|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26561,"numValue":2.4,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26562,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9657 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,657 | train | mutant | 1,793 | 183 | 2,007 | 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 | S68G | S68G | 1 | 1 | 0 | 0 | 68 | S | G | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 10,736 | ProTherm | 5.5 | CD | Urea | Sodium acetate | 10 mM | 25 | NaCl | 0.1 M | 2RN2_A:S68G | null | null | 7.61 | 2.2 | null | null | null | 4 | 2 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":36914,"numValue":7.61,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36915,"numValue":2.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36916,"numValue":2.0,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36917,"numValue":4.0,"... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9658 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,658 | train | mutant | 1,794 | 183 | 2,008 | 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 | S68A | S68A | 1 | 1 | 0 | 0 | 68 | S | A | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 3,447 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:S68A | 48.3 | -1.5 | null | null | null | null | 89 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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:S68A","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12740,"numValue":48.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12741,"numValue":-... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9659 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,659 | train | mutant | 1,794 | 183 | 2,008 | 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 | S68A | S68A | 1 | 1 | 0 | 0 | 68 | S | A | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 7,727 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:S68A | 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 | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26563,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26564,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9660 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,660 | train | mutant | 1,794 | 183 | 2,008 | 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 | S68A | S68A | 1 | 1 | 0 | 0 | 68 | S | A | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 10,737 | ProTherm | 5.5 | CD | Urea | Sodium acetate | 10 mM | 25 | NaCl | 0.1 M | 2RN2_A:S68A | null | null | 10 | -0.19 | null | null | null | 4.8 | 2.06 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":36919,"numValue":10.0,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36920,"numValue":-0.19,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36921,"numValue":2.06,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":3... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9661 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,661 | train | mutant | 1,795 | 183 | 2,009 | 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 | S68T | S68T | 1 | 1 | 0 | 0 | 68 | S | T | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 3,448 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:S68T | 49.1 | -0.7 | null | null | null | null | 106.2 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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:S68T","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12744,"numValue":49.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12745,"numValue":-0.7,"references":... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9662 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,662 | train | mutant | 1,795 | 183 | 2,009 | 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 | S68T | S68T | 1 | 1 | 0 | 0 | 68 | S | T | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 7,728 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:S68T | 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 | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26565,"numValue":0.2,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26566,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9663 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,663 | train | mutant | 1,795 | 183 | 2,009 | 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 | S68T | S68T | 1 | 1 | 0 | 0 | 68 | S | T | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 10,738 | ProTherm | 5.5 | CD | Urea | Sodium acetate | 10 mM | 25 | NaCl | 0.1 M | 2RN2_A:S68T | null | null | 9.91 | -0.1 | null | null | null | 5 | 1.95 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv|SAAFEC_S983.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":36924,"numValue":9.91,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv","SAAFEC_S983.csv"],"id":36925,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36926,"numValue":1.95,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9664 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,664 | train | mutant | 1,796 | 183 | 2,010 | 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 | S68V | S68V | 1 | 1 | 0 | 0 | 68 | S | V | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 3,449 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:S68V | 51.7 | 1.9 | null | null | null | null | 98.8 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Broom_S605.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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:S68V","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12748,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12749,"numValue":1.9,"references":[... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9665 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,665 | train | mutant | 1,796 | 183 | 2,010 | 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 | S68V | S68V | 1 | 1 | 0 | 0 | 68 | S | V | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 7,729 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:S68V | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26567,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26568,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9666 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,666 | train | mutant | 1,796 | 183 | 2,010 | 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 | S68V | S68V | 1 | 1 | 0 | 0 | 68 | S | V | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 10,739 | ProTherm | 5.5 | CD | Urea | Sodium acetate | 10 mM | 25 | NaCl | 0.1 M | 2RN2_A:S68V | null | null | 11.1 | -1.29 | null | null | null | 5.1 | 2.13 | null | null | null | null | null | null | null | yes | DG|DDG|M|CM|REVERSIBILITY | SAAFEC_S1262.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER... | [{"datasets":[],"id":36929,"numValue":11.1,"references":[],"strValue":null,"type":"DG"},{"datasets":["SAAFEC_S1262.csv"],"id":36930,"numValue":-1.29,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":36931,"numValue":2.13,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":36932,"numValue":5.... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9667 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,667 | train | mutant | 1,797 | 183 | 2,011 | 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 | S68L | S68L | 1 | 1 | 0 | 0 | 68 | S | L | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 3,450 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:S68L | 48.2 | -1.6 | null | null | null | null | 84 | null | null | null | null | null | null | null | null | null | yes | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|AUTOMUTE_S1749.csv|Broom_S605.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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:S68L","type":"_... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12752,"numValue":48.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","AUTOMUTE_S1962.csv","Broom_S605.csv","Saraboji_S1791.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":12753,"numValue":-1.6,"references":... | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9668 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,668 | train | mutant | 1,797 | 183 | 2,011 | 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 | S68L | S68L | 1 | 1 | 0 | 0 | 68 | S | L | 4 | CONSERVATION | 2RN2 | 76 | null | 68 | A | E | true | false | 1.881193 | 13.965 | 7,730 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | 2RN2_A:S68L | 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 | 308 | ARTICLE | Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI. | 1,992 | 10.1111/j.1432-1033.1992.tb16932.x | 1317795 | Eur J Biochem;206;337-43 | 5 | Kimura S|Oda Y|Nakai T|Katayanagi K|Kitakuni E | [{"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":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":26569,"numValue":0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26570,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16577,"numValue":4.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9670 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,670 | train | mutant | 474 | 183 | 523 | 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 | D70N | D70N | 1 | 1 | 0 | 0 | 70 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 767 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D70N | 52.5 | 5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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:D70N","type":"... | [{"datasets":[],"id":2927,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2928,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2929,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9671 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,671 | train | mutant | 474 | 183 | 523 | 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 | D70N | D70N | 1 | 1 | 0 | 0 | 70 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 780 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D70N | 48.8 | -1.2 | null | null | null | null | 110.1 | 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:D70N","type":"_... | [{"datasets":[],"id":2974,"numValue":48.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2975,"numValue":-1.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2976,"numValue":110.1,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9672 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,672 | train | mutant | 474 | 183 | 523 | 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 | D70N | D70N | 1 | 1 | 0 | 0 | 70 | D | N | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 7,684 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D70N | null | null | null | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | 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":26439,"numValue":0.3,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26440,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9674 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,674 | train | mutant | 475 | 183 | 524 | 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 | D70A | D70A | 1 | 1 | 0 | 0 | 70 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 768 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | null | 2RN2_A:D70A | 50.8 | 3.8 | 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:D70A","type":"... | [{"datasets":[],"id":2930,"numValue":50.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2931,"numValue":3.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2932,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9675 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,675 | train | mutant | 475 | 183 | 524 | 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 | D70A | D70A | 1 | 1 | 0 | 0 | 70 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 781 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D70A | 49.7 | -0.3 | null | null | null | null | 85.5 | 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:D70A","type":"_... | [{"datasets":[],"id":2978,"numValue":49.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2979,"numValue":-0.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2980,"numValue":85.5,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9676 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,676 | train | mutant | 475 | 183 | 524 | 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 | D70A | D70A | 1 | 1 | 0 | 0 | 70 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 7,685 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D70A | null | null | null | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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":26441,"numValue":0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26442,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9677 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,677 | train | mutant | 475 | 183 | 524 | 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 | D70A | D70A | 1 | 1 | 0 | 0 | 70 | D | A | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 7,807 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D70A | null | null | null | -1.1 | 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":26749,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26750,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9679 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,679 | train | mutant | 476 | 183 | 525 | 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 | D70E | D70E | 1 | 1 | 0 | 0 | 70 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 782 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | 2RN2_A:D70E | 51.8 | 1.8 | null | null | null | null | 90.4 | 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:D70E","type":"_... | [{"datasets":[],"id":2982,"numValue":51.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":2983,"numValue":1.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2984,"numValue":90.4,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id... | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9680 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,680 | train | mutant | 476 | 183 | 525 | 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 | D70E | D70E | 1 | 1 | 0 | 0 | 70 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 7,686 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50 | 2RN2_A:D70E | null | null | null | -0.5 | 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":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"],"id":26443,"numValue":-0.5,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26444,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9681 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,681 | train | mutant | 476 | 183 | 525 | 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 | D70E | D70E | 1 | 1 | 0 | 0 | 70 | D | E | 9 | BINDING_SITE|CONSERVATION | 2RN2 | 76 | null | 70 | A | L | true | true | 55.843327 | 18.195 | 7,808 | ProTherm | 9 | CD | Thermal | glycine-NaOH | 50 mM | 47 | 2RN2_A:D70E | null | null | null | -0.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_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"],"id":26751,"numValue":-0.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26752,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":83,"numValue":null,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"BINDING_SITE"},{"id":16579,"numValue":9.0,"position":70,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:9682 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,682 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 3,926 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | 54.6 | 3.7 | null | null | null | null | 118.6 | 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|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":14453,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14454,"numValue":3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14455,"numValue":118.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[]... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9683 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,683 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 3,930 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | 55.8 | 3.3 | null | null | null | null | 91.2 | 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 | 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":14469,"numValue":55.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":14470,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":14471,"numValue":91.2,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9684 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,684 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,074 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | 53.5 | 3.7 | 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 | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15050,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15051,"numValue":3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15052,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9685 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,685 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,077 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | 55.3 | 3.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | TM|DTM|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15059,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15060,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15061,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9686 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,686 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,663 | ProTherm | 3 | CD | Thermal | Gly-HCl buffer | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | null | 3.7 | null | -1.1 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl buffer","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17244,"numValue":3.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":17245,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17246,"numValue":null,"... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9687 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,687 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,666 | ProTherm | 5.5 | CD | Thermal | sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74L | null | 3.3 | null | -0.9 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"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":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17253,"numValue":3.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":17254,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets"... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9688 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,688 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,457 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 10 mM | 52.5 | NaCl | 0.1 M | 2RN2_A:V74L | null | null | null | -0.9 | 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|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":25907,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25908,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9689 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,689 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,467 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52 | NaCl | 0.1 M | 2RN2_A:V74L | null | null | null | -0.9 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25930,"numValue":-0.9,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25931,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9690 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,690 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,621 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 50.9 | NaCl | 0.1 M | 2RN2_A:V74L | 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|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":26307,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26308,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9691 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,691 | train | mutant | 2,026 | 183 | 2,262 | 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 | V74L | V74L | 1 | 1 | 0 | 0 | 74 | V | L | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,735 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | NaCl | 0.1 M | 2RN2_A:V74L | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26579,"numValue":-1.1,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26580,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9692 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,692 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,075 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74I | 52.2 | 2.4 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15053,"numValue":52.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15054,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15055,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9693 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,693 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,078 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74I | 54.1 | 2.1 | 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|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15062,"numValue":54.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15063,"numValue":2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15064,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9694 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,694 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,664 | ProTherm | 3 | CD | Thermal | Gly-HCl buffer | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74I | null | 2.4 | null | -0.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv|potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"numValue":3.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Gly-HCl buffer","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"}... | [{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17247,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":17248,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17249,"numValue":null,"... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9695 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,695 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,667 | ProTherm | 5.5 | CD | Thermal | sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74I | null | 2.1 | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DTM|DDG|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv|capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 458 | ARTICLE | Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core. | 1,993 | 8390295 | Biochemistry;32;6171-8 | 4 | Kanaya S|Nakamura H|Ishikawa K|Morikawa K | [{"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":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":17256,"numValue":2.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":17257,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets"... | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:9696 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,696 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,468 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | 52 | NaCl | 0.1 M | 2RN2_A:V74I | null | null | null | -0.6 | null | null | null | null | null | null | null | null | null | null | null | null | yes | DDG|REVERSIBILITY | capriotti_S1615_map.csv|khan_protherm_data_mapped.csv|potapov_with_uniprot_mapping.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUF... | [{"datasets":["capriotti_S1615_map.csv","khan_protherm_data_mapped.csv","potapov_with_uniprot_mapping.csv"],"id":25932,"numValue":-0.6,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25933,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9697 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,697 | train | mutant | 2,069 | 183 | 2,310 | 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 | V74I | V74I | 1 | 1 | 0 | 0 | 74 | V | I | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 7,736 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | 49.8 | NaCl | 0.1 M | 2RN2_A:V74I | 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 | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":["capriotti_S1615_map.csv","potapov_with_uniprot_mapping.csv"],"id":26581,"numValue":-0.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":26582,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9698 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,698 | train | mutant | 2,070 | 183 | 2,311 | 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 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,076 | ProTherm | 3 | CD | Thermal | glycine-HCl | 10 mM | null | NaCl | 0.1 M | 2RN2_A:V74A | 42.2 | -7.6 | 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 | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15056,"numValue":42.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15057,"numValue":-7.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15058,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||
fireprotdb:9699 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 9,699 | train | mutant | 2,070 | 183 | 2,311 | 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 | V74A | V74A | 1 | 1 | 0 | 0 | 74 | V | A | 8 | CONSERVATION | 2RN2 | 76 | null | 74 | A | H | true | false | 2.553048 | 13.321429 | 4,079 | ProTherm | 5.5 | CD | Thermal | Sodium acetate | 20 mM | null | NaCl | 0.1 M | 2RN2_A:V74A | 39.3 | -12.7 | 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 | 377 | ARTICLE | Antithrombin III Utah: proline-407 to leucine mutation in a highly conserved region near the inhibitor reactive site. | 1,988 | 10.1021/bi00416a052 | 3191114 | Biochemistry;27;6171-8 | 3 | Bock S C|Marrinan J A|Radziejewska E | [{"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":15065,"numValue":39.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":15066,"numValue":-12.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":15067,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":16583,"numValue":8.0,"position":74,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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