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:8257 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,257 | train | mutant | 1,016 | 146 | 1,148 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | P56E | P56E | 1 | 1 | 0 | 0 | 56 | P | E | 4 | CONSERVATION | null | false | false | null | null | 1,812 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:P56E | 84.4 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:P... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":8813,"numValue":4.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8258 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,258 | train | mutant | 1,016 | 146 | 1,148 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | P56E | P56E | 1 | 1 | 0 | 0 | 56 | P | E | 4 | CONSERVATION | null | false | false | null | null | 1,824 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:P56E | 88.7 | 1.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S499.csv|PoPMuSiC-2.0_S2648.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|STRUM_Q342... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:P56E","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6766,"numValue":88.7,"references":[],"strValue":n... | [{"id":8813,"numValue":4.0,"position":56,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8259 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,259 | train | mutant | 1,017 | 146 | 1,149 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | R58L | R58L | 1 | 1 | 0 | 0 | 58 | R | L | 5 | CONSERVATION | null | false | false | null | null | 1,813 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:R58L | 82.9 | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:R... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":8815,"numValue":5.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8260 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,260 | train | mutant | 1,017 | 146 | 1,149 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | R58L | R58L | 1 | 1 | 0 | 0 | 58 | R | L | 5 | CONSERVATION | null | false | false | null | null | 1,825 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:R58L | 84 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:R58L","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6769,"numValue":84.0,"references":[],"strValue":null... | [{"id":8815,"numValue":5.0,"position":58,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8261 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,261 | train | mutant | 1,018 | 146 | 1,150 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V61I | V61I | 1 | 1 | 0 | 0 | 61 | V | I | 6 | CONSERVATION | null | false | false | null | null | 1,814 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:V61I | 84.4 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|PoPMuSiC-2.0_S2648.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","PoPMuSiC-2.0_S2648.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_... | [{"id":8818,"numValue":6.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8262 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,262 | train | mutant | 1,018 | 146 | 1,150 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V61I | V61I | 1 | 1 | 0 | 0 | 61 | V | I | 6 | CONSERVATION | null | false | false | null | null | 1,826 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:V61I | 87.2 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V61I","type":"_PD... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6772,"numValue":87.2,"references":[],"strValue":null... | [{"id":8818,"numValue":6.0,"position":61,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8263 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,263 | train | mutant | 131 | 146 | 149 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | S92F | S92F | 1 | 1 | 0 | 0 | 92 | S | F | 2 | CONSERVATION | null | false | false | null | null | 243 | ProTherm | 7 | CD | Thermal | sodium phosphate | null | ammonium sulfate | 1.0-1.5 M | 1OSI_A:S92F | 87 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 21 | ARTICLE | Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures. | 2,001 | 10.1093/protein/14.2.81 | 11297665 | Protein Eng;14;81-4 | 5 | Hirose R|Suzuki T|Moriyama H|Sato T|Yamagishi A | [{"numValue":7.0,"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":"ammonium sulfate","type":"ION"},{"numValue":null,"strValue":"1.0-1.5 M","ty... | [{"datasets":[],"id":996,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":997,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8849,"numValue":2.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8264 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,264 | train | mutant | 131 | 146 | 149 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | S92F | S92F | 1 | 1 | 0 | 0 | 92 | S | F | 2 | CONSERVATION | null | false | false | null | null | 550 | ProTherm | 7 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:S92F | 87 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | M47andM8_S2760.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 57 | ARTICLE | Analysis of the effect of accumulation of amino acid replacements on activity of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,001 | 10.1093/protein/14.8.601 | 11579229 | Protein Eng;14;601-7 | 4 | Suzuki T|Yamagishi A|Yasugi M|Oshima T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:S92F","type":"_PD... | [{"datasets":["M47andM8_S2760.csv"],"id":2186,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["M47andM8_S2760.csv"],"id":2187,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":2188,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8849,"numValue":2.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8265 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,265 | train | mutant | 7,315 | 146 | 7,985 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | S92F|V126M | S92F|V126M | 2 | 2 | 0 | 0 | 92 | S | F | 2 | CONSERVATION | null | false | false | null | null | 15,675 | ProTherm | 7 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:S92F 1OSI_A:V126M | 87 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 57 | ARTICLE | Analysis of the effect of accumulation of amino acid replacements on activity of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,001 | 10.1093/protein/14.8.601 | 11579229 | Protein Eng;14;601-7 | 4 | Suzuki T|Yamagishi A|Yasugi M|Oshima T | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:S92F 1OSI_A:V126M... | [{"datasets":[],"id":57525,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":57526,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":57527,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8849,"numValue":2.0,"position":92,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8266 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,266 | train | mutant | 130 | 146 | 148 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126M | V126M | 1 | 1 | 0 | 0 | 126 | V | M | 6 | CONSERVATION | null | false | false | null | null | 242 | ProTherm | 7 | CD | Thermal | sodium phosphate | null | ammonium sulfate | 1.0-1.5 M | 1OSI_A:V126M | 87 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|ION|ION_CONC|_PDB_CHAIN_MUTATION | 21 | ARTICLE | Crystal structures of mutants of Thermus thermophilus IPMDH adapted to low temperatures. | 2,001 | 10.1093/protein/14.2.81 | 11297665 | Protein Eng;14;81-4 | 5 | Hirose R|Suzuki T|Moriyama H|Sato T|Yamagishi A | [{"numValue":7.0,"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":"ammonium sulfate","type":"ION"},{"numValue":null,"strValue":"1.0-1.5 M","ty... | [{"datasets":[],"id":994,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":995,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8268 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,268 | train | mutant | 130 | 146 | 148 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126M | V126M | 1 | 1 | 0 | 0 | 126 | V | M | 6 | CONSERVATION | null | false | false | null | null | 1,237 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126M | 87 | 0 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126M","type":"_PDB... | [{"datasets":[],"id":4557,"numValue":87.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4558,"numValue":0.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4559,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8269 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,269 | train | mutant | 708 | 146 | 772 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126G | V126G | 1 | 1 | 0 | 0 | 126 | V | G | 6 | CONSERVATION | null | false | false | null | null | 1,233 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126G | 82 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126G","type":"_PDB... | [{"datasets":[],"id":4545,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4546,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4547,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8270 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,270 | train | mutant | 709 | 146 | 773 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126A | V126A | 1 | 1 | 0 | 0 | 126 | V | A | 6 | CONSERVATION | null | false | false | null | null | 1,234 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126A | 85 | -2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126A","type":"_PDB... | [{"datasets":[],"id":4548,"numValue":85.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4549,"numValue":-2.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4550,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8271 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,271 | train | mutant | 710 | 146 | 774 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126S | V126S | 1 | 1 | 0 | 0 | 126 | V | S | 6 | CONSERVATION | null | false | false | null | null | 1,235 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126S | 74 | -13 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126S","type":"_PDB... | [{"datasets":[],"id":4551,"numValue":74.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4552,"numValue":-13.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4553,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8272 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,272 | train | mutant | 711 | 146 | 775 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126E | V126E | 1 | 1 | 0 | 0 | 126 | V | E | 6 | CONSERVATION | null | false | false | null | null | 1,236 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126E | 77 | -10 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126E","type":"_PDB... | [{"datasets":[],"id":4554,"numValue":77.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4555,"numValue":-10.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4556,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8273 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,273 | train | mutant | 712 | 146 | 776 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126L | V126L | 1 | 1 | 0 | 0 | 126 | V | L | 6 | CONSERVATION | null | false | false | null | null | 1,238 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126L | 82 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126L","type":"_PDB... | [{"datasets":[],"id":4560,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4561,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4562,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8274 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,274 | train | mutant | 713 | 146 | 777 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126I | V126I | 1 | 1 | 0 | 0 | 126 | V | I | 6 | CONSERVATION | null | false | false | null | null | 1,239 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126I | 82 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126I","type":"_PDB... | [{"datasets":[],"id":4563,"numValue":82.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4564,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4565,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8275 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,275 | train | mutant | 714 | 146 | 778 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V126F | V126F | 1 | 1 | 0 | 0 | 126 | V | F | 6 | CONSERVATION | null | false | false | null | null | 1,240 | ProTherm | 10.4 | CD | Thermal | NaHCO3 | 20 mM | null | 1OSI_A:V126F | 80 | -7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 128 | ARTICLE | Cold-adaptation mechanism of mutant enzymes of 3-isopropylmalate dehydrogenase from Thermus thermophilus. | 2,002 | 10.1093/protein/15.6.471 | 12082165 | Protein Eng;15;471-6 | 5 | Suzuki Toshiharu|Yasugi Masako|Arisaka Fumio|Oshima Tairo|Yamagishi Akihiko | [{"numValue":10.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaHCO3","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V126F","type":"_PDB... | [{"datasets":[],"id":4566,"numValue":80.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":4567,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":4568,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8883,"numValue":6.0,"position":126,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||||
fireprotdb:8276 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,276 | train | mutant | 1,019 | 146 | 1,151 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | L134N | L134N | 1 | 1 | 0 | 0 | 134 | L | N | 9 | CONSERVATION | null | false | false | null | null | 1,815 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:L134N | 87.9 | 3.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q306.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:L... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q306.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6739,"numValue":87.9,"re... | [{"id":8891,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8277 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,277 | train | mutant | 1,019 | 146 | 1,151 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | L134N | L134N | 1 | 1 | 0 | 0 | 134 | L | N | 9 | CONSERVATION | null | false | false | null | null | 1,827 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:L134N | 91.3 | 3.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:L134N","type":"_P... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv"],"id":6775,"numValue":91.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":8891,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8278 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,278 | train | mutant | 7,526 | 146 | 8,211 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | L134N|V181T|P324T|A335E | L134N|V181T|P324T|A335E | 4 | 4 | 0 | 0 | 134 | L | N | 9 | CONSERVATION | null | false | false | null | null | 16,021 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:L134N 1OSI_A:V181T 1OSI_A:P324T 1OSI_A:A335E | 90.2 | 5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 955 | ARTICLE | The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase. | 2,006 | 10.1016/j.febslet.2006.06.012 | 16797545 | FEBS Lett;580;3867-71 | 2 | Yamagishi Akihiko|Watanabe Keiko | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:L... | [{"datasets":[],"id":58793,"numValue":90.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58794,"numValue":5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58795,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8891,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRang... | ||||||||||||||||||
fireprotdb:8279 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,279 | train | mutant | 7,526 | 146 | 8,211 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | L134N|V181T|P324T|A335E | L134N|V181T|P324T|A335E | 4 | 4 | 0 | 0 | 134 | L | N | 9 | CONSERVATION | null | false | false | null | null | 16,023 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:L134N 1OSI_A:V181T 1OSI_A:P324T 1OSI_A:A335E | 92.7 | 5.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 955 | ARTICLE | The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase. | 2,006 | 10.1016/j.febslet.2006.06.012 | 16797545 | FEBS Lett;580;3867-71 | 2 | Yamagishi Akihiko|Watanabe Keiko | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:L134N 1OSI_A:V181... | [{"datasets":[],"id":58799,"numValue":92.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58800,"numValue":5.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58801,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8891,"numValue":9.0,"position":134,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRang... | ||||||||||||||||||
fireprotdb:8281 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,281 | train | mutant | 1,020 | 146 | 1,152 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | H179K | H179K | 1 | 1 | 0 | 0 | 179 | H | K | 4 | CONSERVATION | null | false | false | null | null | 1,828 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:H179K | 87.1 | -0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:H179K","type":"_P... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6778,"numValue":87.1,"references":[],"strValue":null,"type... | [{"id":8936,"numValue":4.0,"position":179,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8282 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,282 | train | mutant | 1,021 | 146 | 1,153 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V181T | V181T | 1 | 1 | 0 | 0 | 181 | V | T | 8 | CONSERVATION | null | false | false | null | null | 1,817 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:V181T | 86.1 | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6745,"numValue":8... | [{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8283 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,283 | train | mutant | 1,021 | 146 | 1,153 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V181T | V181T | 1 | 1 | 0 | 0 | 181 | V | T | 8 | CONSERVATION | null | false | false | null | null | 1,829 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:V181T | 89.1 | 1.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V181T","type":"_P... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6781,"numValue":89.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8284 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,284 | train | mutant | 7,525 | 146 | 8,210 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V181T|P324T|A335E | V181T|P324T|A335E | 3 | 3 | 0 | 0 | 181 | V | T | 8 | CONSERVATION | null | false | false | null | null | 16,020 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:V181T 1OSI_A:P324T 1OSI_A:A335E | 88.1 | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 955 | ARTICLE | The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase. | 2,006 | 10.1016/j.febslet.2006.06.012 | 16797545 | FEBS Lett;580;3867-71 | 2 | Yamagishi Akihiko|Watanabe Keiko | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V... | [{"datasets":[],"id":58790,"numValue":88.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58791,"numValue":3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58792,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9092,"numValue":4.0,"position":335,"positionArray":null,"positionRang... | ||||||||||||||||||
fireprotdb:8285 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,285 | train | mutant | 7,525 | 146 | 8,210 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | V181T|P324T|A335E | V181T|P324T|A335E | 3 | 3 | 0 | 0 | 181 | V | T | 8 | CONSERVATION | null | false | false | null | null | 16,022 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:V181T 1OSI_A:P324T 1OSI_A:A335E | 90.9 | 3.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 955 | ARTICLE | The effects of multiple ancestral residues on the Thermus thermophilus 3-isopropylmalate dehydrogenase. | 2,006 | 10.1016/j.febslet.2006.06.012 | 16797545 | FEBS Lett;580;3867-71 | 2 | Yamagishi Akihiko|Watanabe Keiko | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:V181T 1OSI_A:P324... | [{"datasets":[],"id":58796,"numValue":90.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58797,"numValue":3.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58798,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":8938,"numValue":8.0,"position":181,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9092,"numValue":4.0,"position":335,"positionArray":null,"positionRang... | ||||||||||||||||||
fireprotdb:8286 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,286 | train | mutant | 1,022 | 146 | 1,154 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | D184H | D184H | 1 | 1 | 0 | 0 | 184 | D | H | 9 | CONSERVATION | null | false | false | null | null | 1,818 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:D184H | 84.8 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:D... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6748,"numValue":84.8... | [{"id":8941,"numValue":9.0,"position":184,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8287 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,287 | train | mutant | 1,022 | 146 | 1,154 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | D184H | D184H | 1 | 1 | 0 | 0 | 184 | D | H | 9 | CONSERVATION | null | false | false | null | null | 1,830 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:D184H | 88.8 | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | EASE-MM_S1676.csv|HotMuSiC_S1626.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:D184H","type":"_P... | [{"datasets":["EASE-MM_S1676.csv","HotMuSiC_S1626.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6784,"numValue":88.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON... | [{"id":8941,"numValue":9.0,"position":184,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8288 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,288 | train | mutant | 1,023 | 146 | 1,155 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | S261N | S261N | 1 | 1 | 0 | 0 | 261 | S | N | 9 | CONSERVATION | null | false | false | null | null | 1,819 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:S261N | 83.3 | -1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|HotMuSiC_S1626.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:S... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6751,"numValue":83.3,"references":[],"... | [{"id":9018,"numValue":9.0,"position":261,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8289 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,289 | train | mutant | 1,023 | 146 | 1,155 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | S261N | S261N | 1 | 1 | 0 | 0 | 261 | S | N | 9 | CONSERVATION | null | false | false | null | null | 1,831 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:S261N | 85.6 | -1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:S261N","type":"_P... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6787,"numValue":85.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","... | [{"id":9018,"numValue":9.0,"position":261,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8290 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,290 | train | mutant | 1,024 | 146 | 1,156 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | P324T | P324T | 1 | 1 | 0 | 0 | 324 | P | T | 8 | CONSERVATION | null | false | false | null | null | 1,820 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:P324T | 85.4 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|EASE-MM_S1676.csv|HotMuSiC_S1626.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S168... | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:P... | [{"datasets":["AUTOMUTE_S1925.csv","EASE-MM_S1676.csv","HotMuSiC_S1626.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6754,"numValue":85.4,"references":[],"strValue":nul... | [{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8291 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,291 | train | mutant | 1,024 | 146 | 1,156 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | P324T | P324T | 1 | 1 | 0 | 0 | 324 | P | T | 8 | CONSERVATION | null | false | false | null | null | 1,832 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:P324T | 87.7 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | EASE-MM_S1676.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:P324T","type":"_P... | [{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6790,"numValue":87.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","... | [{"id":9081,"numValue":8.0,"position":324,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8292 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,292 | train | mutant | 1,025 | 146 | 1,157 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | A335E | A335E | 1 | 1 | 0 | 0 | 335 | A | E | 4 | CONSERVATION | null | false | false | null | null | 1,821 | ProTherm | 7.6 | Activity | Thermal | potassium phosphate | 20 mM | null | 1OSI_A:A335E | 85.1 | 0.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S1810.csv|M47andM8_S2760.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|EASE-MM_S1676.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"potassium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:A... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":6757,"numValue":85.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["AU... | [{"id":9092,"numValue":4.0,"position":335,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8293 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,293 | train | mutant | 1,025 | 146 | 1,157 | 345 | 345 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | 18 | 3-isopropylmalate dehydrogenase | Thermus thermophilus | 1 | P61495 | IPR019818|IPR024084|IPR004429 | 1.1.1.85 | A335E | A335E | 1 | 1 | 0 | 0 | 335 | A | E | 4 | CONSERVATION | null | false | false | null | null | 1,833 | ProTherm | 7.6 | CD | Thermal | phosphate | 20 mM | null | 1OSI_A:A335E | 88.3 | 0.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | M47andM8_S1810.csv|M47andM8_S2760.csv|STRUM_Q3421.csv|SVM-WIN31_SVM-3D12_S499.csv|EASE-MM_S1676.csv|PON-TStab_dataset.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 196 | ARTICLE | Designing thermostable proteins: ancestral mutants of 3-isopropylmalate dehydrogenase designed by using a phylogenetic tree. | 2,006 | 10.1016/j.jmb.2005.10.011 | 16309701 | J Mol Biol;355;664-74 | 4 | Yamagishi Akihiko|Ohkuri Takatoshi|Watanabe Keiko|Yokobori Shin-ichi | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"phosphate","type":"BUFFER"},{"numValue":null,"strValue":"20 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1OSI_A:A335E","type":"_P... | [{"datasets":["M47andM8_S1810.csv","M47andM8_S2760.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.csv"],"id":6793,"numValue":88.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S1676.csv","M47andM8_S1810.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","STRUM_Q3421.csv","SVM-WIN31_SVM-3D12_S499.cs... | [{"id":9092,"numValue":4.0,"position":335,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8294 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,294 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,850 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 42.7 | null | null | null | null | null | 120 | null | null | null | null | null | null | null | null | null | yes(85%) | 3.0 | TM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65987,"numValue":42.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65988,"numValue":120.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65989,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":65990,"numValue":null,"references... | ||||||||||||||||||||||||
fireprotdb:8296 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,296 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 17,852 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | null | 43.2 | null | null | null | null | null | 160.6 | null | null | null | null | null | null | null | null | null | yes(75%) | TM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":65995,"numValue":43.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":65996,"numValue":160.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":65997,"numValue":null,"references":[],"strValue":"yes(75%)","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8297 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,297 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,733 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 50 mM | null | 53.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84829,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84830,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8298 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,298 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,734 | ProTherm | 4.75 | Fluorescence | Thermal | Sodium phosphate | 50 mM | null | 53.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.75,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84831,"numValue":53.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84832,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8299 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,299 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,735 | ProTherm | 7 | Fluorescence | Thermal | Sodium phosphate | 50 mM | null | 41.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84833,"numValue":41.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84834,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8300 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,300 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,736 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 50 mM | null | 54 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84835,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84836,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8301 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,301 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,737 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 54 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84837,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84838,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8302 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,302 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,738 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 54.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84839,"numValue":54.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84840,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8303 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,303 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,739 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 57.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84841,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84842,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8304 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,304 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,740 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 60 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84843,"numValue":60.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84844,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8305 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,305 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,741 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 64.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84845,"numValue":64.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84846,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8306 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,306 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,742 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 66.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84847,"numValue":66.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84848,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8307 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,307 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,743 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 67.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84849,"numValue":67.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84850,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8308 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,308 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,744 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 68 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84851,"numValue":68.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84852,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8309 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,309 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,745 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 69.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84853,"numValue":69.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84854,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8310 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,310 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,746 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 54.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84855,"numValue":54.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84856,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8311 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,311 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,747 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 55.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84857,"numValue":55.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84858,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8312 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,312 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,748 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 56.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84859,"numValue":56.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84860,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8313 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,313 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,749 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 58.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84861,"numValue":58.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84862,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8314 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,314 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,750 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 60.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84863,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84864,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8315 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,315 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,751 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 61.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84865,"numValue":61.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84866,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8316 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,316 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,752 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 62.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84867,"numValue":62.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84868,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8317 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,317 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,753 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 65.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84869,"numValue":65.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84870,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8318 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,318 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,754 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 66.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84871,"numValue":66.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84872,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8319 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,319 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,755 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 150 mM | null | 44.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"150 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84873,"numValue":44.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84874,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8320 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,320 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,756 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 52.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84875,"numValue":52.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84876,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8321 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,321 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,757 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 58.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84877,"numValue":58.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84878,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8322 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,322 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,758 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 58.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84879,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84880,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8323 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,323 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,759 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 57.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84881,"numValue":57.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84882,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8324 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,324 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,760 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 55.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84883,"numValue":55.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84884,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8325 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,325 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,761 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 59.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84885,"numValue":59.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84886,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8327 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,327 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,763 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 58.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84889,"numValue":58.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84890,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8328 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,328 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,764 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 58.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84891,"numValue":58.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84892,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8331 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,331 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,767 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 59.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84897,"numValue":59.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84898,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8332 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,332 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,768 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 54.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84899,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84900,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8333 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,333 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,769 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 55.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84901,"numValue":55.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84902,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8334 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,334 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,770 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 55.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84903,"numValue":55.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84904,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8335 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,335 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,771 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 56.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84905,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84906,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8336 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,336 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,772 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 53.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84907,"numValue":53.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84908,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8337 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,337 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,773 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 47.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84909,"numValue":47.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84910,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8338 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,338 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,774 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 51.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84911,"numValue":51.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84912,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8339 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,339 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,775 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 70.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84913,"numValue":70.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84914,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8340 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,340 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,776 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 68.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84915,"numValue":68.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84916,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8341 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,341 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,777 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 67.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84917,"numValue":67.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84918,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8342 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,342 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,778 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 69.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84919,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84920,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8343 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,343 | train | sequence | 154 | 154 | -1 | 278 | -1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 23,779 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 66.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"}] | [{"datasets":[],"id":84921,"numValue":66.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":84922,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | |||||||||||||||||||||||||
fireprotdb:8345 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,345 | train | mutant | 136 | 154 | 155 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F | W68F | 1 | 1 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68 | A | G | true | false | 27.352152 | 8.620714 | 257 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W28F | 45.2 | -7 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | yes(77%) | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:W28F","typ... | [{"datasets":[],"id":1053,"numValue":45.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1054,"numValue":-7.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1055,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8346 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,346 | train | mutant | 136 | 154 | 155 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F | W68F | 1 | 1 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68 | A | G | true | false | 27.352152 | 8.620714 | 260 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W28F | 36.2 | -7 | null | null | null | null | 196.5 | null | null | null | null | null | null | null | null | null | yes(75%) | TM|DTM|DHVH|REVERSIBILITY | AUTOMUTE_S1925.csv|I_Mutant2.0_S1948.csv|I_Mutant2.0_S2087.csv|iPTREE-STAB_S1859.csv|M47andM8_S2760.csv|PON-TStab_dataset.csv|Saraboji_S1396.csv|SVM-WIN31_SVM-3D12_S1634.csv|SVM-WIN31_SVM-3D12_S1681.csv|AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:... | [{"datasets":["AUTOMUTE_S1925.csv","I_Mutant2.0_S1948.csv","I_Mutant2.0_S2087.csv","iPTREE-STAB_S1859.csv","M47andM8_S2760.csv","PON-TStab_dataset.csv","Saraboji_S1396.csv","SVM-WIN31_SVM-3D12_S1634.csv","SVM-WIN31_SVM-3D12_S1681.csv"],"id":1068,"numValue":36.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[... | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8347 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,347 | train | mutant | 136 | 154 | 155 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F | W68F | 1 | 1 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68 | A | G | true | false | 27.352152 | 8.620714 | 7,459 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 52.2 | 1CHK_A:W28F | null | null | null | 1.76 | null | null | null | null | null | null | null | null | null | null | null | null | yes(77%) | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":52.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":25911,"numValue":1.76,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25912,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":25913,"numValue":null,"references":[],"strValue":"yes(77%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8348 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,348 | train | mutant | 136 | 154 | 155 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F | W68F | 1 | 1 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68 | A | G | true | false | 27.352152 | 8.620714 | 8,008 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | 43.2 | 1CHK_A:W28F | null | null | null | 4.43 | null | null | null | null | null | null | null | null | null | null | null | null | yes(75%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM"... | [{"datasets":[],"id":27326,"numValue":4.43,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27327,"numValue":null,"references":[],"strValue":"yes(75%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8349 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,349 | train | mutant | 136 | 154 | 155 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F | W68F | 1 | 1 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68 | A | G | true | false | 27.352152 | 8.620714 | 8,010 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 42.7 | 1CHK_A:W28F | null | null | null | 3.56 | null | null | null | null | null | null | null | null | null | null | null | null | yes(77%) | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":42.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":27330,"numValue":3.56,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27331,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27332,"numValue":null,"references":[],"strValue":"yes(77%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8350 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,350 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 14,468 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W28F 1CHK_A:W101F | 31.3 | -11.4 | null | null | null | null | 155 | null | null | null | null | null | null | null | null | null | yes(68%) | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:W28F 1CHK_... | [{"datasets":[],"id":53487,"numValue":31.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53488,"numValue":-11.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53489,"numValue":155.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53490,"numValue":3.0,"references"... | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8351 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,351 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 14,469 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W28F 1CHK_A:W101F | 44.2 | -8 | null | null | null | null | 60 | null | null | null | null | null | null | null | null | null | yes(68%) | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:W28F 1CHK_... | [{"datasets":[],"id":53492,"numValue":44.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53493,"numValue":-8.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53494,"numValue":60.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53495,"numValue":3.0,"references":[... | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8352 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,352 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 14,470 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W28F 1CHK_A:W101F | 31.2 | -12 | null | null | null | null | 203.6 | null | null | null | null | null | null | null | null | null | yes(80%) | TM|DTM|DHVH|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:... | [{"datasets":[],"id":53497,"numValue":31.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":53498,"numValue":-12.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":53499,"numValue":203.6,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":53500,"numValue":null,"references... | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8353 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,353 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 14,996 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 52.2 | 1CHK_A:W28F 1CHK_A:W101F | null | null | null | 1.51 | null | null | null | null | null | null | null | null | null | null | null | null | yes(68%) | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":52.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":55173,"numValue":1.51,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55174,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":55175,"numValue":null,"references":[],"strValue":"yes(68%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8354 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,354 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 15,095 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | 43.2 | 1CHK_A:W28F 1CHK_A:W101F | null | null | null | 8.03 | null | null | null | null | null | null | null | null | null | null | null | null | yes(80%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM"... | [{"datasets":[],"id":55404,"numValue":8.03,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55405,"numValue":null,"references":[],"strValue":"yes(80%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8355 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,355 | train | mutant | 6,714 | 154 | 7,356 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W68F|W141F | W68F|W141F | 2 | 2 | 0 | 0 | 68 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 68|141 | A | G|H | true | false | 13.676076 | 10.473929 | 15,096 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 42.7 | 1CHK_A:W28F 1CHK_A:W101F | null | null | null | 5.8 | null | null | null | null | null | null | null | null | null | null | null | null | yes(68%) | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":42.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":55406,"numValue":5.8,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":55407,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":55408,"numValue":null,"references":[],"strValue":"yes(68%)","type":"REVERSIBILITY"}] | [{"id":9170,"numValue":9.0,"position":68,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8356 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,356 | train | mutant | 137 | 154 | 156 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 141 | A | H | false | false | 0 | 12.327143 | 255 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W101F | 35.6 | -7.1 | null | null | null | null | 170 | null | null | null | null | null | null | null | null | null | yes(79%) | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:W101F","ty... | [{"datasets":[],"id":1043,"numValue":35.6,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1044,"numValue":-7.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1045,"numValue":170.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"... | [{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8357 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,357 | train | mutant | 137 | 154 | 156 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 141 | A | H | false | false | 0 | 12.327143 | 258 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | null | 1CHK_A:W101F | 44.7 | -7.5 | null | null | null | null | 80 | null | null | null | null | null | null | null | null | null | yes(79%) | 3.0 | TM|DTM|DHVH|STATE|REVERSIBILITY | AUTOMUTE_S1749.csv|Saraboji_S1791.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"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":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:W101F","ty... | [{"datasets":[],"id":1058,"numValue":44.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1749.csv","Saraboji_S1791.csv"],"id":1059,"numValue":-7.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1060,"numValue":80.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"i... | [{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8359 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,359 | train | mutant | 137 | 154 | 156 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 141 | A | H | false | false | 0 | 12.327143 | 7,460 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 52.2 | 1CHK_A:W101F | null | null | null | 1.89 | null | null | null | null | null | null | null | null | null | null | null | null | yes(79%) | 3.0 | DDG|STATE|REVERSIBILITY | khan_protherm_data_mapped.csv | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":52.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":["khan_protherm_data_mapped.csv"],"id":25914,"numValue":1.89,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":25915,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":25916,"numValue":null,"references":[],"strValue":"yes(79%)","type":"REVERSIBILITY"}] | [{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8360 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,360 | train | mutant | 137 | 154 | 156 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 141 | A | H | false | false | 0 | 12.327143 | 8,007 | ProTherm | 7 | Fluorescence | Thermal | sodium phosphate | 50 mM | 43.2 | 1CHK_A:W101F | null | null | null | 4.27 | null | null | null | null | null | null | null | null | null | null | null | null | yes(77%) | DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":43.2,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM"... | [{"datasets":[],"id":27324,"numValue":4.27,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27325,"numValue":null,"references":[],"strValue":"yes(77%)","type":"REVERSIBILITY"}] | [{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8361 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,361 | train | mutant | 137 | 154 | 156 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | W141F | W141F | 1 | 1 | 0 | 0 | 141 | W | F | 9 | CONSERVATION | 1CHK | 154 | null | 141 | A | H | false | false | 0 | 12.327143 | 8,011 | ProTherm | 7 | CD | Thermal | sodium phosphate | 50 mM | 42.7 | 1CHK_A:W101F | null | null | null | 3.91 | null | null | null | null | null | null | null | null | null | null | null | null | yes(79%) | 3.0 | DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 23 | ARTICLE | Thermal unfolding of chitosanase from Streptomyces sp. N174: role of tryptophan residues in the protein structure stabilization. | 1,999 | 10.1016/s0167-4838(98)00243-x | 9989221 | Biochim Biophys Acta;1429;365-76 | 6 | Honda Y|Fukamizo T|Okajima T|Goto S|Boucher I|Brzezinski R | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":42.7,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"B... | [{"datasets":[],"id":27333,"numValue":3.91,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":27334,"numValue":3.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":27335,"numValue":null,"references":[],"strValue":"yes(79%)","type":"REVERSIBILITY"}] | [{"id":9243,"numValue":9.0,"position":141,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8362 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,362 | train | mutant | 1,344 | 154 | 1,517 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | A144L | A144L | 1 | 1 | 0 | 0 | 144 | A | L | 9 | CONSERVATION | 1CHK | 154 | null | 144 | A | H | false | false | 3.090532 | 8.858 | 2,644 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 50 mM | null | 1CHK_A:A104L | 48 | -5.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"50 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:A1... | [{"datasets":[],"id":9700,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9701,"numValue":-5.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9702,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":9246,"numValue":9.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8363 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,363 | train | mutant | 1,344 | 154 | 1,517 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | A144L | A144L | 1 | 1 | 0 | 0 | 144 | A | L | 9 | CONSERVATION | 1CHK | 154 | null | 144 | A | H | false | false | 3.090532 | 8.858 | 2,645 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 1CHK_A:A104L | 48.7 | -5.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:A... | [{"datasets":[],"id":9703,"numValue":48.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9704,"numValue":-5.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9705,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":9246,"numValue":9.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8364 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,364 | train | mutant | 1,344 | 154 | 1,517 | 278 | 278 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | 19 | Chitosanase | Streptomyces sp. (strain N174) | 1 | P33665 | IPR000400|IPR023099|IPR023346 | 3.2.1.132 | A144L | A144L | 1 | 1 | 0 | 0 | 144 | A | L | 9 | CONSERVATION | 1CHK | 154 | null | 144 | A | H | false | false | 3.090532 | 8.858 | 2,646 | ProTherm | 4.5 | Fluorescence | Thermal | Sodium acetate | 100 mM | null | 1CHK_A:A104L | 50.2 | -5.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | No | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 233 | ARTICLE | Quantitative fluorometric analysis of the protective effect of chitosan on thermal unfolding of catalytically active native and genetically-engineered chitosanases. | 2,007 | 10.1016/j.bbapap.2007.05.016 | 17644457 | Biochim Biophys Acta;1774;975-84 | 7 | Roy S?bastien|Fortin M?lanie|Gagnon Julie|Ghinet Mariana Gabriela|Lehoux Jean-Guy|Dupuis Gilles|Brzezinski Ryszard | [{"numValue":4.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Sodium acetate","type":"BUFFER"},{"numValue":null,"strValue":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"1CHK_A:A... | [{"datasets":[],"id":9706,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9707,"numValue":-5.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9708,"numValue":null,"references":[],"strValue":"No","type":"REVERSIBILITY"}] | [{"id":9246,"numValue":9.0,"position":144,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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