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:8704 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,704 | train | mutant | 1,310 | 170 | 1,461 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A | S34A | 1 | 1 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34 | A | S | true | false | 0 | 8.1875 | 2,575 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A | 56 | -1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A","type":"_PDB_... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9516,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9517,"numValue":-1.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9518,"numValue":null,"refe... | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8705 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,705 | train | mutant | 1,310 | 170 | 1,461 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A | S34A | 1 | 1 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34 | A | S | true | false | 0 | 8.1875 | 2,588 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A | 63.8 | 0.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A","type":"_PDB_... | [{"datasets":["STRUM_Q3421.csv"],"id":9555,"numValue":63.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":9556,"numValue":0.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":9557,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBIL... | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8706 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,706 | train | mutant | 7,521 | 170 | 8,206 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A | S34A|I157A | 2 | 2 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|157 | A | S|L | true | false | 14.377691 | 10.212083 | 16,012 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:I132A | 56.8 | -0.7 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:I132A",... | [{"datasets":[],"id":58766,"numValue":56.8,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58767,"numValue":-0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58768,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8707 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,707 | train | mutant | 7,521 | 170 | 8,206 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A | S34A|I157A | 2 | 2 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|157 | A | S|L | true | false | 14.377691 | 10.212083 | 16,016 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:I132A | 66.1 | 2.4 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:I132A",... | [{"datasets":[],"id":58778,"numValue":66.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58779,"numValue":2.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58780,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8708 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,708 | train | mutant | 7,522 | 170 | 8,207 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A|S128A | S34A|I157A|S128A | 3 | 3 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|128|157 | A | S|E|L | true | false | 10.791876 | 10.210139 | 16,013 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:S103A 2DRI_A:I132A | 53.4 | -4.1 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:S103A 2... | [{"datasets":[],"id":58769,"numValue":53.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58770,"numValue":-4.1,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58771,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRa... | ||||||||||||||
fireprotdb:8709 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,709 | train | mutant | 7,522 | 170 | 8,207 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A|S128A | S34A|I157A|S128A | 3 | 3 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|128|157 | A | S|E|L | true | false | 10.791876 | 10.210139 | 16,017 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:S103A 2DRI_A:I132A | 53.7 | -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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:S103A 2... | [{"datasets":[],"id":58781,"numValue":53.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58782,"numValue":-10.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58783,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRa... | ||||||||||||||
fireprotdb:8711 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,711 | train | mutant | 7,523 | 170 | 8,208 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A|S128A|N38A | S34A|I157A|S128A|N38A | 4 | 4 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|38|128|157 | A | S|E|L | true | false | 10.407052 | 9.900786 | 16,018 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:N13A 2DRI_A:S103A 2DRI_A:I132A | 54.7 | -9 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:N13A 2D... | [{"datasets":[],"id":58784,"numValue":54.7,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58785,"numValue":-9.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58786,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12202,"numValue":9.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRan... | ||||||||||||||
fireprotdb:8713 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,713 | train | mutant | 7,524 | 170 | 8,209 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S34A|I157A|S128A|N38A|Q260A | S34A|I157A|S128A|N38A|Q260A | 5 | 5 | 0 | 0 | 34 | S | A | 8 | CONSERVATION | 2DRI | 153 | null | 34|38|128|157|260 | A | S|E|L | true | false | 9.662867 | 9.819129 | 16,019 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S9A 2DRI_A:N13A 2DRI_A:S103A 2DRI_A:I132A 2DRI_A:Q235A | 59 | -4.7 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S9A 2DRI_A:N13A 2D... | [{"datasets":[],"id":58787,"numValue":59.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":58788,"numValue":-4.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":58789,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12198,"numValue":8.0,"position":34,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12202,"numValue":9.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRan... | ||||||||||||||
fireprotdb:8714 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,714 | train | mutant | 1,311 | 170 | 1,462 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | N38A | N38A | 1 | 1 | 0 | 0 | 38 | N | A | 9 | CONSERVATION | 2DRI | 153 | null | 38 | A | S | true | false | 9.252581 | 8.972727 | 2,576 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:N13A | 58.2 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv|EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:N13A","type":"_PDB... | [{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9519,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9520,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":["EASE-MM_S543.csv"... | [{"id":12202,"numValue":9.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8715 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,715 | train | mutant | 1,311 | 170 | 1,462 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | N38A | N38A | 1 | 1 | 0 | 0 | 38 | N | A | 9 | CONSERVATION | 2DRI | 153 | null | 38 | A | S | true | false | 9.252581 | 8.972727 | 2,589 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:N13A | 60.1 | -3.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:N13A","type":"_PDB... | [{"datasets":["STRUM_Q3421.csv"],"id":9558,"numValue":60.1,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9559,"numValue":-3.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9560,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBI... | [{"id":12202,"numValue":9.0,"position":38,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8716 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,716 | train | mutant | 1,312 | 170 | 1,463 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F40A | F40A | 1 | 1 | 0 | 0 | 40 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 40 | A | H | true | false | 6.067613 | 11.813333 | 2,577 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F15A | 52.5 | -5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F15A","type":"_PDB... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9522,"numValue":52.5,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9523,"numValue":-5.0,"references":[],"strValue":null,"type":"DTM"},{"d... | [{"id":12204,"numValue":8.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8717 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,717 | train | mutant | 1,312 | 170 | 1,463 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F40A | F40A | 1 | 1 | 0 | 0 | 40 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 40 | A | H | true | false | 6.067613 | 11.813333 | 2,590 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F15A | 54.2 | -9.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F15A","type":"_PDB... | [{"datasets":[],"id":9561,"numValue":54.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":9562,"numValue":-9.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":9563,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12204,"numValue":8.0,"position":40,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8718 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,718 | train | mutant | 1,313 | 170 | 1,464 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F41A | F41A | 1 | 1 | 0 | 0 | 41 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 41 | A | H | true | false | 6.525103 | 10.058333 | 2,578 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F16A | 58.9 | 1.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F16A","type":"_PDB... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9525,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9526,"numValue":1.4,"references":[],"strValue":nu... | [{"id":12205,"numValue":8.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8719 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,719 | train | mutant | 1,313 | 170 | 1,464 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F41A | F41A | 1 | 1 | 0 | 0 | 41 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 41 | A | H | true | false | 6.525103 | 10.058333 | 2,591 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F16A | 57.4 | -6.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | STRUM_Q3421.csv | BUFFER|PH|MEASURE|METHOD|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"numValue":null,"strValue":"Phosphate","type":"BUFFER"},{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F16A","type":"_PDB... | [{"datasets":["STRUM_Q3421.csv"],"id":9564,"numValue":57.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":9565,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":9566,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBI... | [{"id":12205,"numValue":8.0,"position":41,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8720 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,720 | train | mutant | 4,606 | 170 | 5,133 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | A52T | A52T | 1 | 1 | 0 | 0 | 52 | A | T | 9 | CONSERVATION | 2DRI | 153 | null | 52 | A | H | false | false | 0 | 20.241666 | 10,819 | ProTherm | 7.7 | Fluorescence | GdnHCl | HEPES | 10 mM | 25 | 2DRI_A:A27T | null | null | 1.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 720 | ARTICLE | Mutations that affect the folding of ribose-binding protein selected as suppressors of a defect in export in Escherichia coli. | 1,991 | 1904869 | J Biol Chem;266;11789-96 | 6 | Kim J|Park S|Song T|Park C|Teschke C M|Randall L L | [{"numValue":7.7,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"GdnHCl","type":"METHOD"},{"numValue":null,"strValue":"HEPES","type":"BUFFER"},{"numValue":null,"strValue":"10 mM","type":"BUF... | [{"datasets":[],"id":37230,"numValue":1.8,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":37231,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":12216,"numValue":9.0,"position":52,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:8722 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,722 | train | mutant | 146 | 170 | 171 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | L87C | L87C | 1 | 1 | 0 | 0 | 87 | L | C | 6 | CONSERVATION | 2DRI | 153 | null | 87 | A | E | true | false | 0 | 11.78 | 275 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 2DRI_A:L62C | 54 | -8.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"Potassium chloride","ty... | [{"datasets":[],"id":1117,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1118,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1119,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12251,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8723 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,723 | train | mutant | 146 | 170 | 171 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | L87C | L87C | 1 | 1 | 0 | 0 | 87 | L | C | 6 | CONSERVATION | 2DRI | 153 | null | 87 | A | E | true | false | 0 | 11.78 | 2,896 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 2DRI_A:L62C | 54 | -8.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":... | [{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":10518,"numValue":54.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":10519,"numValue":-8.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":10520,"numValue":null,... | [{"id":12251,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8724 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,724 | train | mutant | 146 | 170 | 171 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | L87C | L87C | 1 | 1 | 0 | 0 | 87 | L | C | 6 | CONSERVATION | 2DRI | 153 | null | 87 | A | E | true | false | 0 | 11.78 | 8,647 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | 25 | Potassium chloride | 100 mM | 2DRI_A:L62C | null | null | 3.2 | 2.7 | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | DHVH|DG|DDG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_... | [{"datasets":[],"id":29344,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":29345,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":29346,"numValue":2.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":29347,"numValue":null,"references":[]... | [{"id":12251,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8725 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,725 | train | mutant | 146 | 170 | 171 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | L87C | L87C | 1 | 1 | 0 | 0 | 87 | L | C | 6 | CONSERVATION | 2DRI | 153 | null | 87 | A | E | true | false | 0 | 11.78 | 10,503 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | 25 | Potassium chloride | 100 mM | 2DRI_A:L62C | null | null | 3.2 | null | null | null | 81 | null | null | null | null | null | null | null | null | null | Unknown | DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue"... | [{"datasets":[],"id":36056,"numValue":81.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":36057,"numValue":3.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36058,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12251,"numValue":6.0,"position":87,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8726 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,726 | train | mutant | 1,314 | 170 | 1,465 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | N89A | N89A | 1 | 1 | 0 | 0 | 89 | N | A | 8 | CONSERVATION | 2DRI | 153 | null | 89 | A | L | true | false | 0 | 8.344545 | 2,579 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:N64A | 52.9 | -4.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:N64A","type":"_PDB... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9528,"numValue":52.9,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9529,"numValue":-4.6,"references":[],"strValue":n... | [{"id":12253,"numValue":8.0,"position":89,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8728 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,728 | train | mutant | 1,315 | 170 | 1,466 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | D114A | D114A | 1 | 1 | 0 | 0 | 114 | D | A | 9 | CONSERVATION | 2DRI | 153 | null | 114 | A | S | true | false | 6.430785 | 9.814444 | 2,580 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:D89A | 58.2 | 0.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:D89A","type":"_PDB... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9531,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9532,"numValue":0.7,"references":[],"strValue":nu... | [{"id":12278,"numValue":9.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8729 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,729 | train | mutant | 1,315 | 170 | 1,466 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | D114A | D114A | 1 | 1 | 0 | 0 | 114 | D | A | 9 | CONSERVATION | 2DRI | 153 | null | 114 | A | S | true | false | 6.430785 | 9.814444 | 2,593 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:D89A | 57.2 | -6.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:D89A","type":"_PDB... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":9570,"numValue":57.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9571,"numValue":-6.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9572,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12278,"numValue":9.0,"position":114,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8730 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,730 | train | mutant | 1,316 | 170 | 1,467 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S128A | S128A | 1 | 1 | 0 | 0 | 128 | S | A | 9 | CONSERVATION | 2DRI | 153 | null | 128 | A | E | false | false | 3.620246 | 10.20625 | 2,581 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S103A | 57.8 | 0.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S103A","type":"_PD... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9534,"numValue":57.8,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9535,"numValue":0.3,"references":[],"strValue":nu... | [{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8731 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,731 | train | mutant | 1,316 | 170 | 1,467 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | S128A | S128A | 1 | 1 | 0 | 0 | 128 | S | A | 9 | CONSERVATION | 2DRI | 153 | null | 128 | A | E | false | false | 3.620246 | 10.20625 | 2,594 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:S103A | 60.7 | -3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:S103A","type":"_PD... | [{"datasets":[],"id":9573,"numValue":60.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv"],"id":9574,"numValue":-3.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":9575,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12292,"numValue":9.0,"position":128,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8732 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,732 | train | mutant | 1,317 | 170 | 1,468 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | I157A | I157A | 1 | 1 | 0 | 0 | 157 | I | A | 5 | CONSERVATION | 2DRI | 153 | null | 157 | A | L | true | false | 28.755382 | 12.236667 | 2,582 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:I132A | 57.3 | -0.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:I132A","type":"_PD... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9537,"numValue":57.3,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9538,"numValue":-0.2,"references":[],"strValue":n... | [{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8733 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,733 | train | mutant | 1,317 | 170 | 1,468 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | I157A | I157A | 1 | 1 | 0 | 0 | 157 | I | A | 5 | CONSERVATION | 2DRI | 153 | null | 157 | A | L | true | false | 28.755382 | 12.236667 | 2,595 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:I132A | 61.2 | -2.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:I132A","type":"_PD... | [{"datasets":[],"id":9576,"numValue":61.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9577,"numValue":-2.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv"],"id":9578,"numValue":null,"references":[],"strValue":"... | [{"id":12321,"numValue":5.0,"position":157,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8734 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,734 | train | mutant | 1,318 | 170 | 1,469 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F189A | F189A | 1 | 1 | 0 | 0 | 189 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 189 | A | T | true | false | 16.996334 | 9.119167 | 2,583 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F164A | 51.7 | -5.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F164A","type":"_PD... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9540,"numValue":51.7,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9541,"numValue":-5.8,"references":[],"strValue":n... | [{"id":12353,"numValue":8.0,"position":189,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8735 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,735 | train | mutant | 1,318 | 170 | 1,469 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F189A | F189A | 1 | 1 | 0 | 0 | 189 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 189 | A | T | true | false | 16.996334 | 9.119167 | 2,596 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F164A | 53.3 | -10.4 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F164A","type":"_PD... | [{"datasets":[],"id":9579,"numValue":53.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9580,"numValue":-10.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9581,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12353,"numValue":8.0,"position":189,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8736 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,736 | train | mutant | 147 | 170 | 172 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | A213C | A213C | 1 | 1 | 0 | 0 | 213 | A | C | 8 | CONSERVATION | 2DRI | 153 | null | 213 | A | E | false | false | 0 | 8.608333 | 276 | ProTherm | 7.6 | Activity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 2DRI_A:A188C | 56 | -6.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Activity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"Potassium chloride","ty... | [{"datasets":[],"id":1120,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1121,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1122,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12377,"numValue":8.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8737 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,737 | train | mutant | 147 | 170 | 172 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | A213C | A213C | 1 | 1 | 0 | 0 | 213 | A | C | 8 | CONSERVATION | 2DRI | 153 | null | 213 | A | E | false | false | 0 | 8.608333 | 2,897 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | null | Potassium chloride | 100 mM | 2DRI_A:A188C | 56 | -6.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue":"25 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":10521,"numValue":56.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv"],"id":10522,"numValue":-6.6,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":10523,"numValue":null,"references":[],"str... | [{"id":12377,"numValue":8.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8739 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,739 | train | mutant | 147 | 170 | 172 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | A213C | A213C | 1 | 1 | 0 | 0 | 213 | A | C | 8 | CONSERVATION | 2DRI | 153 | null | 213 | A | E | false | false | 0 | 8.608333 | 10,504 | ProTherm | 7.6 | Quantitative cysteine reactivity | Thermal | MOPS | 25 mM | 25 | Potassium chloride | 100 mM | 2DRI_A:A188C | null | null | 4.1 | null | null | null | 91 | null | null | null | null | null | null | null | null | null | Unknown | DHVH|DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 29 | ARTICLE | Picomole-scale characterization of protein stability and function by quantitative cysteine reactivity. | 2,010 | 10.1073/pnas.0910421107 | 20194783 | Proc Natl Acad Sci U S A;107;4908-13 | 4 | Isom Daniel G|Vardy Eyal|Oas Terrence G|Hellinga Homme W | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Quantitative cysteine reactivity","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"MOPS","type":"BUFFER"},{"numValue":null,"strValue"... | [{"datasets":[],"id":36059,"numValue":91.0,"references":[],"strValue":null,"type":"DHVH"},{"datasets":[],"id":36060,"numValue":4.1,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":36061,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12377,"numValue":8.0,"position":213,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8740 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,740 | train | mutant | 1,319 | 170 | 1,470 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | N215A | N215A | 1 | 1 | 0 | 0 | 215 | N | A | 9 | CONSERVATION | 2DRI | 153 | null | 215 | A | S | true | false | 3.067652 | 7.475455 | 2,584 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:N190A | 49.4 | -8.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | EASE-MM_S543.csv|HotMuSiC_S1626.csv|PoPMuSiC-2.0_S2648.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:N190A","type":"_PD... | [{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9543,"numValue":49.4,"references":[],"strValue":null,"type":"TM"},{"datasets":["EASE-MM_S543.csv","HotMuSiC_S1626.csv","PoPMuSiC-2.0_S2648.csv","STRUM_Q3421.csv"],"id":9544,"numValue":-8.1,"references":[],"strValue":n... | [{"id":12379,"numValue":9.0,"position":215,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8741 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,741 | train | mutant | 1,319 | 170 | 1,470 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | N215A | N215A | 1 | 1 | 0 | 0 | 215 | N | A | 9 | CONSERVATION | 2DRI | 153 | null | 215 | A | S | true | false | 3.067652 | 7.475455 | 2,597 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:N190A | 51.5 | -12.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:N190A","type":"_PD... | [{"datasets":["Broom_S605.csv"],"id":9582,"numValue":51.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9583,"numValue":-12.2,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9584,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBI... | [{"id":12379,"numValue":9.0,"position":215,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8742 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,742 | train | mutant | 1,320 | 170 | 1,471 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F239A | F239A | 1 | 1 | 0 | 0 | 239 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 239 | A | E | false | false | 0 | 10.619167 | 2,585 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F214A | 48 | -9.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | AUTOMUTE_S1962.csv|Saraboji_S2204.csv|STRUM_Q3421.csv|Broom_S605.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F214A","type":"_PD... | [{"datasets":["AUTOMUTE_S1962.csv","Saraboji_S2204.csv","STRUM_Q3421.csv"],"id":9546,"numValue":48.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9547,"numValue":-9.5,"references":[],"strValue":null,"type":"DTM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id"... | [{"id":12403,"numValue":8.0,"position":239,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8743 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,743 | train | mutant | 1,320 | 170 | 1,471 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | F239A | F239A | 1 | 1 | 0 | 0 | 239 | F | A | 8 | CONSERVATION | 2DRI | 153 | null | 239 | A | E | false | false | 0 | 10.619167 | 2,598 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:F214A | 46 | -17.7 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:F214A","type":"_PD... | [{"datasets":["Broom_S605.csv"],"id":9585,"numValue":46.0,"references":[],"strValue":null,"type":"TM"},{"datasets":["STRUM_Q3421.csv"],"id":9586,"numValue":-17.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9587,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12403,"numValue":8.0,"position":239,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8744 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,744 | train | mutant | 1,321 | 170 | 1,472 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | D240A | D240A | 1 | 1 | 0 | 0 | 240 | D | A | 9 | CONSERVATION | 2DRI | 153 | null | 240 | A | E | true | false | 5.839663 | 10.255555 | 2,586 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:D215A | 51.2 | -6.3 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | Broom_S605.csv|STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:D215A","type":"_PD... | [{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9549,"numValue":51.2,"references":[],"strValue":null,"type":"TM"},{"datasets":["Broom_S605.csv","STRUM_Q3421.csv"],"id":9550,"numValue":-6.3,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9551,"numValue":null,"references":[],"strValue":"Unknown",... | [{"id":12404,"numValue":9.0,"position":240,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8745 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,745 | train | mutant | 1,321 | 170 | 1,472 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | D240A | D240A | 1 | 1 | 0 | 0 | 240 | D | A | 9 | CONSERVATION | 2DRI | 153 | null | 240 | A | E | true | false | 5.839663 | 10.255555 | 2,599 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:D215A | 51.3 | -12.4 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:D215A","type":"_PD... | [{"datasets":[],"id":9588,"numValue":51.3,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9589,"numValue":-12.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9590,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12404,"numValue":9.0,"position":240,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8746 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,746 | train | mutant | 1,322 | 170 | 1,473 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | Q260A | Q260A | 1 | 1 | 0 | 0 | 260 | Q | A | 9 | CONSERVATION | 2DRI | 153 | null | 260 | A | L | true | false | 6.686126 | 9.4925 | 2,587 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:Q235A | 58.2 | 0.7 | 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 | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:Q235A","type":"_PD... | [{"datasets":[],"id":9552,"numValue":58.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9553,"numValue":0.7,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":9554,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12424,"numValue":9.0,"position":260,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||
fireprotdb:8747 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,747 | train | mutant | 1,322 | 170 | 1,473 | 296 | 296 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | 25 | Ribose import binding protein RbsB | Escherichia coli (strain K12) | 1 | P02925 | IPR028082|IPR025997 | Q260A | Q260A | 1 | 1 | 0 | 0 | 260 | Q | A | 9 | CONSERVATION | 2DRI | 153 | null | 260 | A | L | true | false | 6.686126 | 9.4925 | 2,600 | ProTherm | 7 | CD | Thermal | Phosphate | 5 mM | null | 2DRI_A:Q235A | 58.9 | -4.8 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | STRUM_Q3421.csv | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|_PDB_CHAIN_MUTATION | 227 | ARTICLE | Analysis of ligand binding to a ribose biosensor using site-directed mutagenesis and fluorescence spectroscopy. | 2,007 | 10.1110/ps.062595707 | 17242374 | Protein Sci;16;362-8 | 5 | Vercillo Natalie C|Herald Kaitlin J|Fox John M|Der Bryan S|Dattelbaum Jonathan D | [{"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":"5 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"2DRI_A:Q235A","type":"_PD... | [{"datasets":[],"id":9591,"numValue":58.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":9592,"numValue":-4.8,"references":[],"strValue":null,"type":"DTM"},{"datasets":["STRUM_Q3421.csv"],"id":9593,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12424,"numValue":9.0,"position":260,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8748 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,748 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,727 | ProTherm | 7.6 | CD | Urea | Sodium phosphate | 0.05 M | 20 | NaCl | 0.15 M | null | null | 1.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1529 | ARTICLE | Minimum folding unit of dystrophin rod domain. | 1,995 | 10.1021/bi00025a017 | 7794924 | Biochemistry;34;8110-4 | 2 | Kahana E|Gratzer W B | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUF... | [{"datasets":[],"id":78830,"numValue":1.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78831,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8749 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,749 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 21,728 | ProTherm | 7.6 | CD | Urea | Sodium phosphate | 0.05 M | 20 | NaCl | 0.15 M | null | null | 3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | DG|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 1529 | ARTICLE | Minimum folding unit of dystrophin rod domain. | 1,995 | 10.1021/bi00025a017 | 7794924 | Biochemistry;34;8110-4 | 2 | Kahana E|Gratzer W B | [{"numValue":7.6,"strValue":null,"type":"PH"},{"numValue":20.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"Sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.05 M","type":"BUF... | [{"datasets":[],"id":78832,"numValue":3.4,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":78833,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8750 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,750 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 22,232 | ProTherm | 7 | CD | Thermal | Phosphate | 100 mM | null | NaCl | 150 mM | 58 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 30 | ARTICLE | Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates. | 2,010 | 10.1073/pnas.1008818107 | 20696926 | Proc Natl Acad Sci U S A;107;15069-74 | 4 | Singh Surinder M|Kongari Narsimulu|Cabello-Villegas Javier|Mallela Krishna M G | [{"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":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":80386,"numValue":58.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":80387,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||
fireprotdb:8751 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,751 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,222 | ProTherm | 7.5 | CD | Thermal | Tris-HCl | 20000.0 | null | NaCl | 150000.0 | 53.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 424 | ARTICLE | Novel mutation in spectrin-like repeat 1 of dystrophin central domain causes protein misfolding and mild Becker muscular dystrophy. | 2,012 | 10.1074/jbc.M111.284521 | 22453924 | J Biol Chem;287;18153-62 | 9 | Acsadi Gyula|Moore Steven A|Ch?ron Ang?lique|Delalande Olivier|Bennett Lindsey|Kupsky William|El-Baba Mohammad|Le Rumeur Elisabeth|Hubert Jean-Fran?ois | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":86131,"numValue":53.4,"references":[],"strValue":null,"type":"TM"}] | |||||||||||||||||||||||||
fireprotdb:8752 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,752 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,237 | ProTherm | 7.5 | CD | Thermal | PBS | null | 46.1 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 1734 | ARTICLE | Internal deletion compromises the stability of dystrophin. | 2,011 | 10.1093/hmg/ddr199 | 21558423 | Hum Mol Genet;20;2955-63 | 5 | Belanto Joseph J|Ervasti James M|Henderson Davin M|Li Bin|Heun-Johnson Hanke | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86159,"numValue":46.1,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86160,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8753 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,753 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,238 | ProTherm | 7.5 | CD | Thermal | PBS | null | 50.9 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 1734 | ARTICLE | Internal deletion compromises the stability of dystrophin. | 2,011 | 10.1093/hmg/ddr199 | 21558423 | Hum Mol Genet;20;2955-63 | 5 | Belanto Joseph J|Ervasti James M|Henderson Davin M|Li Bin|Heun-Johnson Hanke | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86161,"numValue":50.9,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86162,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8754 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,754 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,239 | ProTherm | 7.5 | CD | Thermal | PBS | null | 65.5 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 1734 | ARTICLE | Internal deletion compromises the stability of dystrophin. | 2,011 | 10.1093/hmg/ddr199 | 21558423 | Hum Mol Genet;20;2955-63 | 5 | Belanto Joseph J|Ervasti James M|Henderson Davin M|Li Bin|Heun-Johnson Hanke | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86163,"numValue":65.5,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86164,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8755 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,755 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,240 | ProTherm | 7.5 | CD | Thermal | PBS | null | 50.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 1734 | ARTICLE | Internal deletion compromises the stability of dystrophin. | 2,011 | 10.1093/hmg/ddr199 | 21558423 | Hum Mol Genet;20;2955-63 | 5 | Belanto Joseph J|Ervasti James M|Henderson Davin M|Li Bin|Heun-Johnson Hanke | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86165,"numValue":50.2,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86166,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8756 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,756 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,241 | ProTherm | 7.5 | CD | Thermal | PBS | null | 69.6 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 1734 | ARTICLE | Internal deletion compromises the stability of dystrophin. | 2,011 | 10.1093/hmg/ddr199 | 21558423 | Hum Mol Genet;20;2955-63 | 5 | Belanto Joseph J|Ervasti James M|Henderson Davin M|Li Bin|Heun-Johnson Hanke | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86167,"numValue":69.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86168,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8757 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,757 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,246 | ProTherm | 7.4 | CD | Thermal | PBS | null | 60 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER | 1735 | ARTICLE | Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. | 2,010 | 10.1002/cm.20489 | 20886611 | Cytoskeleton (Hoboken);67;796-807 | 7 | Discher Dennis E|Krieger Christine Carag|Bhasin Nishant|Tewari Manorama|Brown Andre E X|Safer Daniel|Sweeney H Lee | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86185,"numValue":60.0,"references":[],"strValue":null,"type":"TM"}] | ||||||||||||||||||||||||||||
fireprotdb:8758 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,758 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,247 | ProTherm | 7.4 | CD | Thermal | PBS | null | 65 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER | 1735 | ARTICLE | Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. | 2,010 | 10.1002/cm.20489 | 20886611 | Cytoskeleton (Hoboken);67;796-807 | 7 | Discher Dennis E|Krieger Christine Carag|Bhasin Nishant|Tewari Manorama|Brown Andre E X|Safer Daniel|Sweeney H Lee | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86186,"numValue":65.0,"references":[],"strValue":null,"type":"TM"}] | ||||||||||||||||||||||||||||
fireprotdb:8759 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,759 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,248 | ProTherm | 7.4 | CD | Thermal | PBS | null | 55 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER | 1735 | ARTICLE | Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. | 2,010 | 10.1002/cm.20489 | 20886611 | Cytoskeleton (Hoboken);67;796-807 | 7 | Discher Dennis E|Krieger Christine Carag|Bhasin Nishant|Tewari Manorama|Brown Andre E X|Safer Daniel|Sweeney H Lee | [{"numValue":7.4,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86187,"numValue":55.0,"references":[],"strValue":null,"type":"TM"}] | ||||||||||||||||||||||||||||
fireprotdb:8760 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,760 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,249 | ProTherm | 7.5 | Fluorescence | Thermal | PBS | null | 55 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER | 1735 | ARTICLE | Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. | 2,010 | 10.1002/cm.20489 | 20886611 | Cytoskeleton (Hoboken);67;796-807 | 7 | Discher Dennis E|Krieger Christine Carag|Bhasin Nishant|Tewari Manorama|Brown Andre E X|Safer Daniel|Sweeney H Lee | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86188,"numValue":55.0,"references":[],"strValue":null,"type":"TM"}] | ||||||||||||||||||||||||||||
fireprotdb:8762 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,762 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,251 | ProTherm | 7.5 | Fluorescence | Thermal | PBS | null | 35 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM | PH|MEASURE|METHOD|BUFFER | 1735 | ARTICLE | Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. | 2,010 | 10.1002/cm.20489 | 20886611 | Cytoskeleton (Hoboken);67;796-807 | 7 | Discher Dennis E|Krieger Christine Carag|Bhasin Nishant|Tewari Manorama|Brown Andre E X|Safer Daniel|Sweeney H Lee | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":86190,"numValue":35.0,"references":[],"strValue":null,"type":"TM"}] | ||||||||||||||||||||||||||||
fireprotdb:8763 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,763 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,380 | ProTherm | 7 | CD | Thermal | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | 61 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":86580,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":86581,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":86582,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:8764 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,764 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,381 | ProTherm | 7 | CD | Urea | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | null | null | 11.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},... | [{"datasets":[],"id":86583,"numValue":11.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":86584,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":86585,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:8765 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,765 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,382 | ProTherm | 7 | Fluorescence | Urea | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | null | null | 11.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","typ... | [{"datasets":[],"id":86586,"numValue":11.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":86587,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":86588,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | |||||||||||||||||||||||
fireprotdb:8767 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,767 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 24,658 | ProTherm | 7.5 | Differential Scanning Fluorimetry | Thermal | PBS | null | 43.36 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|STATE | PH|MEASURE|METHOD|BUFFER | 512 | ARTICLE | Disease-proportional proteasomal degradation of missense dystrophins. | 2,015 | 10.1073/pnas.1508755112 | 26392559 | Proc Natl Acad Sci U S A;112;12414-9 | 3 | Talsness Dana M|Belanto Joseph J|Ervasti James M | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Differential Scanning Fluorimetry","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":87279,"numValue":43.36,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":87280,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | |||||||||||||||||||||||||||
fireprotdb:8768 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,768 | train | sequence | 175 | 175 | -1 | 3,685 | -1 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | 0 | 0 | 0 | 0 | -1 | null | null | false | false | null | null | 26,626 | ProTherm | 7 | Fluorescence | Urea | PBS | 25 | null | null | 11.2 | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":93402,"numValue":11.2,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":93403,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":93404,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | ||||||||||||||||||||||||||
fireprotdb:8769 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,769 | train | mutant | 7,653 | 175 | 8,356 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | C10S|C188S | C10S|C188S | 2 | 2 | 0 | 0 | 10 | C | S | 1 | CONSERVATION | 1DXX | 238 | null | 10|188 | A|B | L|T | true | false | 78.396811 | 62.669583 | 16,210 | ProTherm | 7 | CD | Urea | NaH2PO4 | 100000.0 | null | NaCl | 150000.0 | null | null | 9.81 | null | null | null | null | null | -1.68 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 964 | ARTICLE | Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. | 2,012 | 10.1002/prot.24033 | 22275054 | Proteins;80;1377-92 | 7 | Singh Surinder M|Kongari Narsimulu|Mallela Krishna M G|Bandi Swati|Molas Justine F|Armstrong Geoffrey S|Winder Steve J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":100000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"numVal... | [{"datasets":[],"id":59366,"numValue":9.81,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":59367,"numValue":-1.68,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":59368,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":12470,"numValue":1.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12648,"numValue":1.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8770 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,770 | train | mutant | 7,653 | 175 | 8,356 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | C10S|C188S | C10S|C188S | 2 | 2 | 0 | 0 | 10 | C | S | 1 | CONSERVATION | 1DXX | 238 | null | 10|188 | A|B | L|T | true | false | 78.396811 | 62.669583 | 16,211 | ProTherm | 7 | Fluorescence | Urea | NaH2PO4 | 100000.0 | null | NaCl | 150000.0 | null | null | 12.84 | null | null | null | null | null | -2.23 | null | null | null | null | null | null | null | yes | DG|M|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 964 | ARTICLE | Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. | 2,012 | 10.1002/prot.24033 | 22275054 | Proteins;80;1377-92 | 7 | Singh Surinder M|Kongari Narsimulu|Mallela Krishna M G|Bandi Swati|Molas Justine F|Armstrong Geoffrey S|Winder Steve J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":100000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"... | [{"datasets":[],"id":59369,"numValue":12.84,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":59370,"numValue":-2.23,"references":[],"strValue":null,"type":"M"},{"datasets":[],"id":59371,"numValue":null,"references":[],"strValue":"yes","type":"REVERSIBILITY"}] | [{"id":12470,"numValue":1.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12648,"numValue":1.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8771 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,771 | train | mutant | 7,653 | 175 | 8,356 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | C10S|C188S | C10S|C188S | 2 | 2 | 0 | 0 | 10 | C | S | 1 | CONSERVATION | 1DXX | 238 | null | 10|188 | A|B | L|T | true | false | 78.396811 | 62.669583 | 16,212 | ProTherm | 7 | CD | Thermal | NaH2PO4 | 100000.0 | null | NaCl | 150000.0 | 61 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 964 | ARTICLE | Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. | 2,012 | 10.1002/prot.24033 | 22275054 | Proteins;80;1377-92 | 7 | Singh Surinder M|Kongari Narsimulu|Mallela Krishna M G|Bandi Swati|Molas Justine F|Armstrong Geoffrey S|Winder Steve J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":100000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":59372,"numValue":61.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59373,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":12470,"numValue":1.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12648,"numValue":1.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8772 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,772 | train | mutant | 7,653 | 175 | 8,356 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | C10S|C188S | C10S|C188S | 2 | 2 | 0 | 0 | 10 | C | S | 1 | CONSERVATION | 1DXX | 238 | null | 10|188 | A|B | L|T | true | false | 78.396811 | 62.669583 | 16,213 | ProTherm | 7 | Fluorescence | Thermal | NaH2PO4 | 100000.0 | null | NaCl | 150000.0 | 62.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | TM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 964 | ARTICLE | Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin. | 2,012 | 10.1002/prot.24033 | 22275054 | Proteins;80;1377-92 | 7 | Singh Surinder M|Kongari Narsimulu|Mallela Krishna M G|Bandi Swati|Molas Justine F|Armstrong Geoffrey S|Winder Steve J | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"NaH2PO4","type":"BUFFER"},{"numValue":100000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"I... | [{"datasets":[],"id":59374,"numValue":62.4,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":59375,"numValue":null,"references":[],"strValue":"no","type":"REVERSIBILITY"}] | [{"id":12470,"numValue":1.0,"position":10,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"},{"id":12648,"numValue":1.0,"position":188,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||
fireprotdb:8773 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,773 | train | mutant | 2,353 | 175 | 2,685 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | K18N | K18N | 1 | 1 | 0 | 0 | 18 | K | N | 8 | CONSERVATION | 1DXX | 238 | null | 18 | A|B | H | true | false | 70.054441 | 28.796667 | 4,647 | ProTherm | 7 | CD | Thermal | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | 1DXX_A:K18N | 57.6 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | TM|DTM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"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":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION... | [{"datasets":[],"id":17183,"numValue":57.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17184,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17185,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":17186,"numValue":null,"references":... | [{"id":12478,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8774 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,774 | train | mutant | 2,353 | 175 | 2,685 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | K18N | K18N | 1 | 1 | 0 | 0 | 18 | K | N | 8 | CONSERVATION | 1DXX | 238 | null | 18 | A|B | H | true | false | 70.054441 | 28.796667 | 4,648 | ProTherm | 7 | CD | Urea | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | 1DXX_A:K18N | null | null | 7.5 | 3.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},... | [{"datasets":[],"id":17187,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":17188,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17189,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":17190,"numValue":null,"references":[]... | [{"id":12478,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8775 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,775 | train | mutant | 2,353 | 175 | 2,685 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | K18N | K18N | 1 | 1 | 0 | 0 | 18 | K | N | 8 | CONSERVATION | 1DXX | 238 | null | 18 | A|B | H | true | false | 70.054441 | 28.796667 | 4,649 | ProTherm | 7 | Fluorescence | Urea | sodium phosphate | 0.1 M | null | NaCl | 0.15 M | 1DXX_A:K18N | null | null | 7.5 | 3.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"sodium phosphate","type":"BUFFER"},{"numValue":null,"strValue":"0.1 M","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","typ... | [{"datasets":[],"id":17191,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":17192,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":17193,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":17194,"numValue":null,"references":[]... | [{"id":12478,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||
fireprotdb:8776 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,776 | train | mutant | 2,353 | 175 | 2,685 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | K18N | K18N | 1 | 1 | 0 | 0 | 18 | K | N | 8 | CONSERVATION | 1DXX | 238 | null | 18 | A|B | H | true | false | 70.054441 | 28.796667 | 4,650 | ProTherm | 7 | CD | Thermal | PBS | null | 57.6 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | no | 2.0 | TM|DTM|STATE|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":17195,"numValue":57.6,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":17196,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":17197,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":17198,"numValue":null,"references":... | [{"id":12478,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:8777 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,777 | train | mutant | 2,353 | 175 | 2,685 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | K18N | K18N | 1 | 1 | 0 | 0 | 18 | K | N | 8 | CONSERVATION | 1DXX | 238 | null | 18 | A|B | H | true | false | 70.054441 | 28.796667 | 11,527 | ProTherm | 7 | Fluorescence | Urea | PBS | 25 | null | null | 7.5 | 3.7 | null | null | null | null | null | null | null | null | null | null | null | null | yes | 2.0 | DG|DDG|STATE|REVERSIBILITY | PH|EXP_TEMPERATURE|MEASURE|METHOD|BUFFER | 454 | ARTICLE | Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function. | 2,014 | 10.1371/journal.pone.0110439 | 25340340 | PLoS One;9;e110439 | 5 | Singh Surinder M|Mallela Krishna M G|Bandi Swati|Shah Dinen D|Armstrong Geoffrey | [{"numValue":7.0,"strValue":null,"type":"PH"},{"numValue":25.0,"strValue":null,"type":"EXP_TEMPERATURE"},{"numValue":null,"strValue":"Fluorescence","type":"MEASURE"},{"numValue":null,"strValue":"Urea","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":39807,"numValue":7.5,"references":[],"strValue":null,"type":"DG"},{"datasets":[],"id":39808,"numValue":3.7,"references":[],"strValue":null,"type":"DDG"},{"datasets":[],"id":39809,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"},{"datasets":[],"id":39810,"numValue":null,"references":[]... | [{"id":12478,"numValue":8.0,"position":18,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||
fireprotdb:8779 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,779 | train | mutant | 2,826 | 175 | 3,205 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | L172H | L172H | 1 | 1 | 0 | 0 | 172 | L | H | 7 | CONSERVATION | 1DXX | 238 | null | 172 | A|B | H | false | false | 0 | 35.41375 | 5,217 | ProTherm | 7.5 | Differential Scanning Fluorimetry | Thermal | PBS | null | 42.08 | -1.28 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 2.0 | TM|DTM|STATE | PH|MEASURE|METHOD|BUFFER | 512 | ARTICLE | Disease-proportional proteasomal degradation of missense dystrophins. | 2,015 | 10.1073/pnas.1508755112 | 26392559 | Proc Natl Acad Sci U S A;112;12414-9 | 3 | Talsness Dana M|Belanto Joseph J|Ervasti James M | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"Differential Scanning Fluorimetry","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"PBS","type":"BUFFER"}] | [{"datasets":[],"id":19033,"numValue":42.08,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":19034,"numValue":-1.28,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":19035,"numValue":2.0,"references":[],"strValue":null,"type":"STATE"}] | [{"id":12632,"numValue":7.0,"position":172,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||||||
fireprotdb:8780 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,780 | train | mutant | 150 | 175 | 176 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Y231N | Y231N | 1 | 1 | 0 | 0 | 231 | Y | N | 9 | CONSERVATION | 1DXX | 238 | null | 231 | A|B | H | true | false | 0.775194 | 23.305 | 279 | ProTherm | 7 | CD | Thermal | Phosphate | 100 mM | null | NaCl | 150 mM | 1DXX_A:Y231N | 43 | -15 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | Unknown | TM|DTM|REVERSIBILITY | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC|_PDB_CHAIN_MUTATION | 30 | ARTICLE | Missense mutations in dystrophin that trigger muscular dystrophy decrease protein stability and lead to cross-beta aggregates. | 2,010 | 10.1073/pnas.1008818107 | 20696926 | Proc Natl Acad Sci U S A;107;15069-74 | 4 | Singh Surinder M|Kongari Narsimulu|Cabello-Villegas Javier|Mallela Krishna M G | [{"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":"100 mM","type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"n... | [{"datasets":[],"id":1129,"numValue":43.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":1130,"numValue":-15.0,"references":[],"strValue":null,"type":"DTM"},{"datasets":[],"id":1131,"numValue":null,"references":[],"strValue":"Unknown","type":"REVERSIBILITY"}] | [{"id":12691,"numValue":9.0,"position":231,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | ||||||||||||
fireprotdb:8781 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,781 | train | mutant | 2,229 | 175 | 2,533 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | L427P | L427P | 1 | 1 | 0 | 0 | 427 | L | P | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 4,423 | ProTherm | 7.5 | CD | Thermal | Tris-HCl | 20000.0 | null | NaCl | 150000.0 | 50 | -3.4 | null | null | null | null | null | null | null | null | null | null | null | null | null | null | TM|DTM | PH|MEASURE|METHOD|BUFFER|BUFFER_CONC|ION|ION_CONC | 424 | ARTICLE | Novel mutation in spectrin-like repeat 1 of dystrophin central domain causes protein misfolding and mild Becker muscular dystrophy. | 2,012 | 10.1074/jbc.M111.284521 | 22453924 | J Biol Chem;287;18153-62 | 9 | Acsadi Gyula|Moore Steven A|Ch?ron Ang?lique|Delalande Olivier|Bennett Lindsey|Kupsky William|El-Baba Mohammad|Le Rumeur Elisabeth|Hubert Jean-Fran?ois | [{"numValue":7.5,"strValue":null,"type":"PH"},{"numValue":null,"strValue":"CD","type":"MEASURE"},{"numValue":null,"strValue":"Thermal","type":"METHOD"},{"numValue":null,"strValue":"Tris-HCl","type":"BUFFER"},{"numValue":20000.0,"strValue":null,"type":"BUFFER_CONC"},{"numValue":null,"strValue":"NaCl","type":"ION"},{"num... | [{"datasets":[],"id":16376,"numValue":50.0,"references":[],"strValue":null,"type":"TM"},{"datasets":[],"id":16377,"numValue":-3.4,"references":[],"strValue":null,"type":"DTM"}] | [{"id":12887,"numValue":9.0,"position":427,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||
fireprotdb:8782 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,782 | train | mutant | 3,775,242 | 175 | 3,779,155 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057C | V3057C | 1 | 1 | 0 | 0 | 3,057 | V | C | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,454 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.045728 | 0.228396 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649590,"numValue":0.0457282820383199,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649591,"numValue":0.228396183410903,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8783 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,783 | train | mutant | 3,775,243 | 175 | 3,779,156 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057G | V3057G | 1 | 1 | 0 | 0 | 3,057 | V | G | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,455 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.236674 | 0.13673 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649592,"numValue":0.236673578912972,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649593,"numValue":0.136730198983126,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8784 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,784 | train | mutant | 3,775,244 | 175 | 3,779,157 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057H | V3057H | 1 | 1 | 0 | 0 | 3,057 | V | H | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,456 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.136895 | 0.276082 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649594,"numValue":0.136895046968617,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649595,"numValue":0.276081604153791,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8785 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,785 | train | mutant | 3,775,245 | 175 | 3,779,158 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057I | V3057I | 1 | 1 | 0 | 0 | 3,057 | V | I | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,457 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.76332 | 0.514177 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649596,"numValue":0.763319934969492,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649597,"numValue":0.514177290217888,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8786 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,786 | train | mutant | 3,775,246 | 175 | 3,779,159 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057K | V3057K | 1 | 1 | 0 | 0 | 3,057 | V | K | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,458 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 1.968242 | 1.563677 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649598,"numValue":1.96824184851721,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649599,"numValue":1.56367713144867,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8787 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,787 | train | mutant | 3,775,247 | 175 | 3,779,160 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057L | V3057L | 1 | 1 | 0 | 0 | 3,057 | V | L | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,459 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.196842 | 0.036709 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649600,"numValue":0.196842256858595,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649601,"numValue":0.0367086052980008,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8788 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,788 | train | mutant | 3,775,248 | 175 | 3,779,161 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057M | V3057M | 1 | 1 | 0 | 0 | 3,057 | V | M | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,460 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.704176 | 0.53065 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649602,"numValue":0.704175522784618,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649603,"numValue":0.530650307078843,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8789 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,789 | train | mutant | 3,775,249 | 175 | 3,779,162 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057P | V3057P | 1 | 1 | 0 | 0 | 3,057 | V | P | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,461 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.290393 | 0.216579 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649604,"numValue":-0.290393485811664,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649605,"numValue":0.216579307718221,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8790 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,790 | train | mutant | 3,775,250 | 175 | 3,779,163 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057R | V3057R | 1 | 1 | 0 | 0 | 3,057 | V | R | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,462 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.112675 | 0.188125 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649606,"numValue":-0.112674506747359,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649607,"numValue":0.188124606563914,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8791 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,791 | train | mutant | 3,775,251 | 175 | 3,779,164 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057T | V3057T | 1 | 1 | 0 | 0 | 3,057 | V | T | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,463 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.070824 | 0.0706 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649608,"numValue":-0.0708237448264857,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649609,"numValue":0.0705996451895659,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8792 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,792 | train | mutant | 3,775,252 | 175 | 3,779,165 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057A | V3057A | 1 | 1 | 0 | 0 | 3,057 | V | A | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,464 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.392555 | 0.122659 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649610,"numValue":-0.392554867001091,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649611,"numValue":0.122659031730634,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8793 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,793 | train | mutant | 3,775,253 | 175 | 3,779,166 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057D | V3057D | 1 | 1 | 0 | 0 | 3,057 | V | D | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,465 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.389156 | 0.154328 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649612,"numValue":-0.389156193175368,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649613,"numValue":0.154327601873247,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8794 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,794 | train | mutant | 3,775,254 | 175 | 3,779,167 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057E | V3057E | 1 | 1 | 0 | 0 | 3,057 | V | E | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,466 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | -0.324016 | 0.148202 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649614,"numValue":-0.324015666904079,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649615,"numValue":0.14820161914964,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8796 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,796 | train | mutant | 3,775,256 | 175 | 3,779,169 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057Q | V3057Q | 1 | 1 | 0 | 0 | 3,057 | V | Q | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,468 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.267778 | 0.651335 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649618,"numValue":0.267778282186069,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649619,"numValue":0.651334988937715,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8798 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,798 | train | mutant | 3,775,258 | 175 | 3,779,171 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057Y | V3057Y | 1 | 1 | 0 | 0 | 3,057 | V | Y | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,470 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.391483 | 0.337495 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649622,"numValue":0.39148276713627,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649623,"numValue":0.33749509971232,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8799 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,799 | train | mutant | 3,775,259 | 175 | 3,779,172 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | V3057F | V3057F | 1 | 1 | 0 | 0 | 3,057 | V | F | 9 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,471 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.22841 | 0.28806 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9649624,"numValue":0.228410429463644,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9649625,"numValue":0.28805964253791,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15517,"numValue":9.0,"position":3057,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8801 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,801 | train | mutant | 3,775,463 | 175 | 3,779,383 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058C | Q3058C | 1 | 1 | 0 | 0 | 3,058 | Q | C | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,675 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 1.543761 | 0.603731 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650032,"numValue":1.5437607896267,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650033,"numValue":0.603731342338011,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8802 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,802 | train | mutant | 3,775,464 | 175 | 3,779,384 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058D | Q3058D | 1 | 1 | 0 | 0 | 3,058 | Q | D | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,676 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.137024 | 0.232738 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650034,"numValue":0.137024352965496,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650035,"numValue":0.232737977435949,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8803 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,803 | train | mutant | 3,775,465 | 175 | 3,779,385 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058E | Q3058E | 1 | 1 | 0 | 0 | 3,058 | Q | E | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,677 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.317739 | 0.234013 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650036,"numValue":0.317738626509068,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650037,"numValue":0.234012762847353,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8804 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,804 | train | mutant | 3,775,466 | 175 | 3,779,386 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058F | Q3058F | 1 | 1 | 0 | 0 | 3,058 | Q | F | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,678 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.895428 | 1.053437 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650038,"numValue":0.895427599290278,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650039,"numValue":1.05343656798843,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8805 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,805 | train | mutant | 3,775,467 | 175 | 3,779,387 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058G | Q3058G | 1 | 1 | 0 | 0 | 3,058 | Q | G | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,679 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.152851 | 0.199125 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650040,"numValue":0.152850772325218,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650041,"numValue":0.199125102414322,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8806 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,806 | train | mutant | 3,775,468 | 175 | 3,779,388 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058I | Q3058I | 1 | 1 | 0 | 0 | 3,058 | Q | I | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,680 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.634109 | 0.469228 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650042,"numValue":0.634108968039413,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650043,"numValue":0.469227899297745,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8807 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,807 | train | mutant | 3,775,469 | 175 | 3,779,389 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058L | Q3058L | 1 | 1 | 0 | 0 | 3,058 | Q | L | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,681 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.100224 | 0.261257 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650044,"numValue":0.100224251099692,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650045,"numValue":0.26125681958601,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8808 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,808 | train | mutant | 3,775,470 | 175 | 3,779,390 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058M | Q3058M | 1 | 1 | 0 | 0 | 3,058 | Q | M | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,682 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.581484 | 0.180928 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650046,"numValue":0.581483700376506,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650047,"numValue":0.180928178138009,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8809 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,809 | train | mutant | 3,775,471 | 175 | 3,779,391 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058N | Q3058N | 1 | 1 | 0 | 0 | 3,058 | Q | N | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,683 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.113991 | 0.329183 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650048,"numValue":0.113991456423867,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650049,"numValue":0.329183034314125,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8810 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,810 | train | mutant | 3,775,472 | 175 | 3,779,392 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058P | Q3058P | 1 | 1 | 0 | 0 | 3,058 | Q | P | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,684 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.998976 | 1.369763 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650050,"numValue":0.998976316459448,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650051,"numValue":1.36976258471487,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8811 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,811 | train | mutant | 3,775,473 | 175 | 3,779,393 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058R | Q3058R | 1 | 1 | 0 | 0 | 3,058 | Q | R | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,685 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.236426 | 0.339005 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650052,"numValue":0.23642629849513,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650053,"numValue":0.339004686179409,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8812 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,812 | train | mutant | 3,775,474 | 175 | 3,779,394 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058S | Q3058S | 1 | 1 | 0 | 0 | 3,058 | Q | S | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,686 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.066661 | 0.288006 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650054,"numValue":0.0666609851997983,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650055,"numValue":0.288005516539738,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8813 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,813 | train | mutant | 3,775,475 | 175 | 3,779,395 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058T | Q3058T | 1 | 1 | 0 | 0 | 3,058 | Q | T | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,687 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 0.704238 | 0.164858 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650056,"numValue":0.704238459730101,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650057,"numValue":0.164858338072997,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] | |||||||||||||||||||||||||
fireprotdb:8814 | fireprotdb | LiteFold/FireProtDB | labeled/fireprotdb/fireprotdb_search_all.jsonl | tables/labeled_fireprotdb_fireprotdb_search_all.jsonl.jsonl | 79354b4f8754e21c3eb41aaf3dd63ba34ae750cd | 8,814 | train | mutant | 3,775,476 | 175 | 3,779,396 | 3,685 | 3,685 | 26 | Dystrophin | Homo sapiens | 1 | 26 | Dystrophin | Homo sapiens | 1 | P11532 | IPR001589|IPR001715|IPR036872|IPR035436|IPR011992|IPR015153|IPR015154|IPR050774|IPR018159|IPR002017|IPR001202|IPR036020|IPR000433|IPR043145 | Q3058V | Q3058V | 1 | 1 | 0 | 0 | 3,058 | Q | V | 7 | CONSERVATION | 1DXX | 238 | null | false | false | null | null | 3,828,688 | Domainome DDG | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | null | 1.186584 | 0.806595 | DOMAINOME_DDG|DOMAINOME_DDG_STD | 1910 | ARTICLE | Site-saturation mutagenesis of 500 human protein domains. | 2,025 | 10.1038/s41586-024-08370-4 | 39779847 | Nature;637;885-894 | 1 | Beltran Antoni | [{"datasets":[],"id":9650058,"numValue":1.1865843404458,"references":[],"strValue":null,"type":"DOMAINOME_DDG"},{"datasets":[],"id":9650059,"numValue":0.806594683260139,"references":[],"strValue":null,"type":"DOMAINOME_DDG_STD"}] | [{"id":15518,"numValue":7.0,"position":3058,"positionArray":null,"positionRange":null,"strValue":null,"type":"CONSERVATION"}] |
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