{"context":{"query":">>uniprot>>pdb","source_dataset":"uniprot","target_dataset":"pdb"},"stats":{"queried":6,"total":240,"mapped":5},"pagination":{"has_next":true,"next_token":"-1[]Q13451,1,Q13451,113,3][P10636,1,P10636,164,8]["},"schema":"id|title|method|resolution|source_organism|chain_count|header","mappings":[{"input":"O14746","source":"O14746|Telomerase reverse transcriptase","targets":["2BCK|Crystal Structure of HLA-A*2402 Complexed with a telomerase peptide|X-RAY DIFFRACTION|2.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4B18|The crystal structure of human Importin alpha 5 with TERT NLS peptide|X-RAY DIFFRACTION|2.52|HOMO SAPIENS; SYNTHETIC CONSTRUCT|0|TRANSPORT PROTEIN / PEPTIDE","4MNQ|TCR-peptide specificity overrides affinity enhancing TCR-MHC interactions|X-RAY DIFFRACTION|2.742|Homo sapiens; Pan troglodytes; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MEN|Human Leukocyte Antigen A02 presenting ILAKFLHWL, in complex with cognate T-Cell Receptor|X-RAY DIFFRACTION|2.81|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MEO|Human Leukocyte Antigen presenting ILGKFLHRL|X-RAY DIFFRACTION|1.772|Homo sapiens|0|IMMUNE SYSTEM","5MEP|Human Leukocyte Antigen A02 presenting ILGKFLHWL|X-RAY DIFFRACTION|2.71|Homo sapiens|0|IMMUNE SYSTEM","5MEQ|Human Leukocyte Antigen A02 presenting ILAKFLHTL|X-RAY DIFFRACTION|2.27|Homo sapiens|0|IMMUNE SYSTEM","5MER|Human Leukocyte Antigen A02 presenting ILAKFLHEL|X-RAY DIFFRACTION|1.88|Homo sapiens|0|IMMUNE SYSTEM","5UGW|STRUCTURE OF THE HUMAN TELOMERASE THUMB DOMAIN|X-RAY DIFFRACTION|2.31|Homo sapiens|0|TRANSFERASE","7BG9|The catalytic core lobe of human telomerase in complex with a telomeric DNA substrate|ELECTRON MICROSCOPY|3.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","7QXA|Cryo-EM map of human telomerase-DNA-TPP1 complex (sharpened)|ELECTRON MICROSCOPY|3.2|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","7QXB|Cryo-EM map of human telomerase-DNA-TPP1-POT1 complex (sharpened map)|ELECTRON MICROSCOPY|3.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","7QXS|Cryo-EM structure of human telomerase-DNA-TPP1-POT1 complex (with POT1 side chains)|ELECTRON MICROSCOPY|3.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","7TRD|Human telomerase catalytic core structure at 3.3 Angstrom|ELECTRON MICROSCOPY|3.3|Homo sapiens; SYNTHETIC CONSTRUCT|0|REPLICATION","7TRE|Human telomerase catalytic core with shelterin protein TPP1|ELECTRON MICROSCOPY|3.5|Homo sapiens; SYNTHETIC CONSTRUCT|0|REPLICATION","7TRF|Human telomerase catalytic core RNP with H2A/H2B|ELECTRON MICROSCOPY|3.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|REPLICATION","7V99|catalytic core of human telomerase holoenzyme|ELECTRON MICROSCOPY|3.54|Homo sapiens; SYNTHETIC CONSTRUCT|0|REPLICATION","9QAX|The catalytic core with C2 symmetry of human telomerase dimer|ELECTRON MICROSCOPY|3.3|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","9QAY|Catalytic core 1 of dimeric human telomerase|ELECTRON MICROSCOPY|3.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|DNA BINDING PROTEIN","9QAZ|Catalytic core 2 of dimeric human telomerase|ELECTRON MICROSCOPY|3.6|Homo sapiens; SYNTHETIC CONSTRUCT|0|DNA BINDING PROTEIN","9SHY|Cryo-EM structure of the catalytic core of human telomerase at the initiation state of the repeat addition cycle|ELECTRON MICROSCOPY|3.53|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","9SHZ|Cryo-EM structure of the catalytic core of human telomerase at the elongation state of the repeat addition cycle|ELECTRON MICROSCOPY|3.2|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN","9SI0|Cryo-EM structure of the catalytic core of human telomerase at the pre-termination state of the repeat addition cycle|ELECTRON MICROSCOPY|3.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|RNA BINDING PROTEIN"]},{"input":"Q86TI2","source":"Q86TI2|Dipeptidyl peptidase 9","targets":["6EOQ|DPP9 - Apo|X-RAY DIFFRACTION|3|Homo sapiens|0|HYDROLASE","6EOR|DPP9 - 1G244|X-RAY DIFFRACTION|2.9|Homo sapiens|0|HYDROLASE","6QZV|DPP9 bound to a dipeptide (MP) from the N-terminus of BRCA2|X-RAY DIFFRACTION|3|Homo sapiens; SYNTHETIC CONSTRUCT|0|HYDROLASE","6X6A|Cryo-EM structure of NLRP1-DPP9 complex|ELECTRON MICROSCOPY|3.6|Homo sapiens|0|IMMUNE SYSTEM","6X6C|Cryo-EM structure of NLRP1-DPP9-VbP complex|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|IMMUNE SYSTEM","7A3F|Crystal structure of apo DPP9|X-RAY DIFFRACTION|2.9|Homo sapiens|0|HYDROLASE","7JKQ|Human DPP9-CARD8 complex|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|IMMUNE SYSTEM, HYDROLASE","7JN7|Human DPP9-CARD8 complex|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|IMMUNE SYSTEM, HYDROLASE","7SVL|DPP9 IN COMPLEX WITH LIGAND ICeD-2|X-RAY DIFFRACTION|2.46|Homo sapiens|0|HYDROLASE","7SVN|DPP9 IN COMPLEX WITH LIGAND ICeD-1|X-RAY DIFFRACTION|2.78|Homo sapiens|0|HYDROLASE","7ZXS|Crystal structure of DPP9 in complex with a 4-oxo-b-lactam based inhibitor, A295|X-RAY DIFFRACTION|1.81|Homo sapiens|0|HYDROLASE","9GOC|Crystal structure of DPP9 Ser730Ala in complex with sulphostin.|X-RAY DIFFRACTION|1.89|Homo sapiens|0|TRANSFERASE","9GOD|Crystal structure of DPP9 in complex with N-phosphono-(S)-3-aminopiperidine-2-one-based inhibitor|X-RAY DIFFRACTION|2.49|Homo sapiens|0|TRANSFERASE","9GON|Crystal structure of DPP9 in complex with sulphostin|X-RAY DIFFRACTION|1.89|Homo sapiens|0|TRANSFERASE"]},{"input":"Q13451","source":"Q13451|Peptidyl-prolyl cis-trans isomerase FKBP5","targets":["1KT0|Structure of the Large FKBP-like Protein, FKBP51, Involved in Steroid Receptor Complexes|X-RAY DIFFRACTION|2.7|Homo sapiens|0|ISOMERASE","3O5D|Crystal structure of a fragment of FKBP51 comprising the Fk1 and Fk2 domains|X-RAY DIFFRACTION|4|Homo sapiens|0|ISOMERASE","3O5E|Fk1 domain of FKBP51, crystal form VI|X-RAY DIFFRACTION|1.6|Homo sapiens|0|ISOMERASE","3O5F|Fk1 domain of FKBP51, crystal form VII|X-RAY DIFFRACTION|1.65|Homo sapiens|0|ISOMERASE","3O5G|Fk1 domain of FKBP51, crystal form I|X-RAY DIFFRACTION|2|Homo sapiens|0|ISOMERASE","3O5I|Fk1 domain of FKBP51, crystal form II|X-RAY DIFFRACTION|1.8|Homo sapiens|0|ISOMERASE","3O5J|Fk1 domain of FKBP51, crystal form III|X-RAY DIFFRACTION|1.7|Homo sapiens|0|ISOMERASE","3O5K|Fk1 domain of FKBP51, crystal form VIII|X-RAY DIFFRACTION|2.7|Homo sapiens|0|ISOMERASE","3O5L|Fk1 domain mutant A19T of FKBP51, crystal form I|X-RAY DIFFRACTION|1.3|Homo sapiens|0|ISOMERASE","3O5M|Fk1 domain mutant A19T of FKBP51, crystal form II|X-RAY DIFFRACTION|1.6|Homo sapiens|0|ISOMERASE","3O5O|Fk1 domain mutant A19T of FKBP51, crystal form III|X-RAY DIFFRACTION|1.15|Homo sapiens|0|ISOMERASE","3O5P|Fk1 domain mutant A19T of FKBP51, crystal form IV|X-RAY DIFFRACTION|1|Homo sapiens|0|ISOMERASE","3O5Q|Fk1 domain mutant A19T of FKBP51, crystal form IV, in presence of DMSO|X-RAY DIFFRACTION|0.96|Homo sapiens|0|ISOMERASE","3O5R|Complex of Fk506 with the Fk1 domain mutant A19T of FKBP51|X-RAY DIFFRACTION|1.1|Homo sapiens|0|ISOMERASE","4DRH|Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of mTOR at low pH|X-RAY DIFFRACTION|2.3|Homo sapiens|0|Isomerase/Transferase","4DRI|Co-crystal structure of the PPIase domain of FKBP51, Rapamycin and the FRB fragment of mTOR|X-RAY DIFFRACTION|1.45|Homo sapiens|0|Isomerase/Transferase","4DRK|EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND FKBP52: COMPLEX OF FKBP51 WITH {3-[(1R)-3-(3,4-dimethoxyphenyl)-1-({[(2S)-1-(3,3-dimethyl-2-oxopentanoyl)piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic acid|X-RAY DIFFRACTION|1.5|Homo sapiens|0|ISOMERASE","4DRM|EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND FKBP52: COMPLEX OF FKBP51 WITH {3-[(1R)-3-(3,4-dimethoxyphenyl)-1-({[(2S)-1-{[(1S,2R)-2-ethyl-1-hydroxycyclohexyl](oxo)acetyl}piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic acid|X-RAY DIFFRACTION|1.48|Homo sapiens|0|ISOMERASE","4DRN|EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND FKBP52: COMPLEX OF FKBP51 WITH {3-[(1R)-3-(3,4-dimethoxyphenyl)-1-({[(2S)-1-{[(1S,2R)-2-ethyl-1-hydroxycyclohexyl](oxo)acetyl}piperidin-2-yl]carbonyl}oxy)propyl]phenoxy}acetic acid|X-RAY DIFFRACTION|1.069|Homo sapiens|0|ISOMERASE","4DRO|EVALUATION OF SYNTHETIC FK506 ANALOGS AS LIGANDS FOR FKBP51 AND FKBP52: COMPLEX OF FKBP51 WITH (1R)-3-(3,4-dimethoxyphenyl)-1-phenylpropyl (2S)-1-{[(1R,2S)-2-ethyl-1-hydroxycyclohexyl](oxo)acetyl}piperidine-2-carboxylate|X-RAY DIFFRACTION|1.1|Homo sapiens|0|ISOMERASE","4DRP|Evaluation of Synthetic FK506 Analogs as Ligands for the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-3-(3,4-dimethoxyphenyl)-1-((S)-1-(2-((1R,2S)-2-ethyl-1-hydroxy-cyclohexyl)-2-oxoacetyl)piperidine-2-carbonyloxy)propyl)phenoxy)acetic acid from cocrystallization|X-RAY DIFFRACTION|1.8|Homo sapiens|0|ISOMERASE","4DRQ|Exploration of Pipecolate Sulfonamides as Binders of the FK506-Binding Proteins 51 and 52: Complex of FKBP51 with 2-(3-((R)-1-((S)-1-(3,5-dichlorophenylsulfonyl)piperidine-2-carbonyloxy)-3-(3,4-dimethoxy -phenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1|Homo sapiens|0|ISOMERASE","4JFI|Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with compound 1-[(9S,13R,13aR)-1,3-dimethoxy-8-oxo-5,8,9,10,11,12,13,13a-octahydro-6H-9,13-epiminoazocino[2,1-a]isoquinolin-14-yl]-2-(3,4,5-trimethoxyphenyl)ethane-1,2-dione|X-RAY DIFFRACTION|1.05|Homo sapiens|0|ISOMERASE","4JFJ|Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with compound (1S,6R)-10-(1,3-benzothiazol-6-ylsulfonyl)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.08|Homo sapiens|0|ISOMERASE","4JFK|Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with (1S,6R)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-10-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6-yl)sulfonyl]-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.15|Homo sapiens|0|ISOMERASE","4JFL|Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with 6-({(1S,5R)-3-[2-(3,4-dimethoxyphenoxy)ethyl]-2-oxo-3,9-diazabicyclo[3.3.1]non-9-yl}sulfonyl)-1,3-benzothiazol-2(3H)-one|X-RAY DIFFRACTION|1.2|Homo sapiens|0|ISOMERASE","4JFM|Increasing the Efficiency Efficiency of Ligands for the FK506-Binding Protein 51 by Conformational Control: Complex of FKBP51 with 2-(3,4-dimethoxyphenoxy)ethyl (2S)-1-[(2-oxo-2,3-dihydro-1,3-benzothiazol-6-yl)sulfonyl]piperidine-2-carboxylate|X-RAY DIFFRACTION|1.02|Homo sapiens|0|ISOMERASE","4R0X|Allosteric coupling of conformational transitions in the FK1 domain of FKBP51 near the site of steroid receptor interaction|X-RAY DIFFRACTION|1.2|Homo sapiens|0|ISOMERASE","4TW6|The Fk1 domain of FKBP51 in complex with iFit1|X-RAY DIFFRACTION|1.4|Homo sapiens|0|ISOMERASE","4TW7|The Fk1 domain of FKBP51 in complex with iFit4|X-RAY DIFFRACTION|1.25|Homo sapiens|0|ISOMERASE","4TX0|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-(2-methoxyethoxy)-3-(2-methoxyethyl)-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.03|Homo sapiens|0|ISOMERASE","4W9O|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-[(1R)-1,2-dihydroxyethyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.27|Homo sapiens|0|ISOMERASE","4W9P|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-5-[(1S)-1,2-dihydroxyethyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.5|Homo sapiens|0|ISOMERASE","4W9Q|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-[(3,5-dichlorophenyl)sulfonyl]-3-[2-(3,4-dimethoxyphenoxy)ethyl]-5-ethyl-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.08|Homo sapiens|0|ISOMERASE","5BXJ|Complex of the Fk1 domain mutant A19T of FKBP51 with 4-Nitrophenol|X-RAY DIFFRACTION|1.24|Homo sapiens|0|ISOMERASE","5DIT|The Fk1 domain of FKBP51 in complex with the new synthetic ligand (1R)-3-(3,4-dimethoxyphenyl)-1-f3-[2-(morpholin-4-yl)ethoxy]phenylgpropyl(2S)-1-[(2S,3R)-2-cyclohexyl-3-hydroxybutanoyl]piperidine-2-carboxylate|X-RAY DIFFRACTION|2.25|Homo sapiens|0|ISOMERASE","5DIU|The Fk1 domain of FKBP51 in complex with the new synthetic ligand 2-(3-((R)-1-((S)-1-((S)-2-cyclohexyl-2-(3,4,5-trimethoxyphenyl)acetyl)piperidine-2-carboxamido)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1.3|Homo sapiens|0|ISOMERASE","5DIV|The Fk1 domain of FKBP51 in complex with the new synthetic ligand (S)-N-(1-carbamoylcyclopentyl)-1-((S)-2-cyclohexyl-2-(3,4,5-trimethoxyphenyl)acetyl)piperidine-2-carboxamide|X-RAY DIFFRACTION|1.65|Homo sapiens|0|ISOMERASE","5NJX|Human FKBP51 protein in complex with C-terminal peptide of Human HSP 90-alpha|X-RAY DIFFRACTION|2.49|Homo sapiens; SYNTHETIC CONSTRUCT|0|ISOMERASE","5OBK|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1|Homo sapiens|0|ISOMERASE","5OMP|Human FKBP5 protein|X-RAY DIFFRACTION|1.88|Homo sapiens|0|ISOMERASE","6SAF|The Fk1 domain of FKBP51 in complex with (S)-(R)-3-(3,4-dimethoxyphenyl)-1-(3-(2-morpholinoethoxy)phenyl)propyl 1-((1R,4aR,8aR)-4-oxodecahydronaphthalene-1-carbonyl)piperidine-2-carboxylate|X-RAY DIFFRACTION|2.05|Homo sapiens|0|CHAPERONE","6TX4|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH 2-PYRIDONE|X-RAY DIFFRACTION|1.06|Homo sapiens|0|ISOMERASE","6TX5|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH 4-METHYLIMIDAZOLE|X-RAY DIFFRACTION|1.08|Homo sapiens|0|ISOMERASE","6TX6|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH NICOTINAMIDE|X-RAY DIFFRACTION|0.98|Homo sapiens|0|ISOMERASE","6TX7|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH 2-PIPERIDONE|X-RAY DIFFRACTION|1.13|Homo sapiens|0|ISOMERASE","6TX8|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH IMIDAZOLE|X-RAY DIFFRACTION|1.2|Homo sapiens|0|ISOMERASE","6TX9|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH HYDANTOIN|X-RAY DIFFRACTION|1.42|Homo sapiens|0|ISOMERASE","6TXX|CRYSTAL STRUCTURE OF HUMAN FKBP51 FK1 DOMAIN A19T MUTANT IN COMPLEX WITH SAFit2|X-RAY DIFFRACTION|2.1|Homo sapiens|0|ISOMERASE","7A6W|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 33-(Z)|X-RAY DIFFRACTION|1.85|Homo sapiens|0|ISOMERASE","7A6X|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 56|X-RAY DIFFRACTION|1.67|Homo sapiens|0|ISOMERASE","7AOT|The Fk1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphenyl)ethyl]-3,19-dioxa-10,13,16-triazatricyclo[18.3.1.0-5,10]tetracosa- 1(24),20,22-triene-4,11,14,17-tetrone|X-RAY DIFFRACTION|0.85|Homo sapiens|0|CHAPERONE","7AOU|The Fk1 domain of FKBP51 in complex with (2'R,5'S,12'R)-12'-cyclohexyl-2'-[2-(3,4-dimethoxyphenyl)ethyl]-3',19'-dioxa-10',13',16'-triazaspiro[cyclopropane-1,15'- tricyclo[18.3.1.0-5,10]tetracosane]-1'(24'),20',22'-triene-4',11',14',17'-tetrone|X-RAY DIFFRACTION|1.16|Homo sapiens|0|ISOMERASE","7APQ|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]thiazol-6-ylsulfonyl)-5-(methoxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.09|Homo sapiens|0|ISOMERASE","7APS|The Fk1 domain of FKBP51 in complex with (2S)-2-((1S,5R,6R)-10-((3,5-dichlorophenyl)sulfonyl)-2-oxo-5-vinyl-3,10-diazabicyclo[4.3.1]decan-3-yl)propanoic acid|X-RAY DIFFRACTION|0.94|Homo sapiens|0|ISOMERASE","7APT|The Fk1 domain of FKBP51 in complex with ((1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-2-oxo-5-vinyl-3,10-diazabicyclo[4.3.1]decan-3-yl)acetic acid|X-RAY DIFFRACTION|1.131|Homo sapiens|0|ISOMERASE","7APW|The Fk1 domain of FKBP51 in complex with (1S,5S,6R)-10-(benzo[d]thiazol-6-ylsulfonyl)-5-(methoxymethyl)-3-(pyridin-2-ylethyl)-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|0.89|Homo sapiens|0|CHAPERONE","7AWF|The Fk1 domain of FKBP51 in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphenyl)ethyl]-15,15,16-trimethyl-3,19-dioxa-10,13,16-triazatricyclo[18.3.1.0^5,^10]tetracosa-1(24),20,22-triene-4,11,14,17-tetrone|X-RAY DIFFRACTION|1.4|Homo sapiens|0|ISOMERASE","7AWX|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 55|X-RAY DIFFRACTION|2.2|Homo sapiens|0|ISOMERASE","7B9Y|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 64a|X-RAY DIFFRACTION|1.35|Homo sapiens|0|ISOMERASE","7B9Z|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 35-(E)|X-RAY DIFFRACTION|1.44|Homo sapiens|0|ISOMERASE","7BA0|Structure of the FKBP51FK1 domain in complex with the macrocyclic SAFit analogue 63|X-RAY DIFFRACTION|1.14|Homo sapiens|0|ISOMERASE","7ETT|The FK1 domain of FKBP51 in complex with peptide-inhibitor hit QFPFV|X-RAY DIFFRACTION|1.5|Homo sapiens; SYNTHETIC CONSTRUCT|0|ISOMERASE","7ETU|The FK1 domain of FKBP51 in complex with peptide-inhibitor hit SFPFT|X-RAY DIFFRACTION|1.39|Homo sapiens; SYNTHETIC CONSTRUCT|0|ISOMERASE","7ETV|The FK1 domain of FKBP51 in complex with peptide-inhibitor hit DFPFV|X-RAY DIFFRACTION|1.31|Homo sapiens; SYNTHETIC CONSTRUCT|0|ISOMERASE","7L7I|Cryo-EM structure of Hsp90:FKBP51:p23 closed-state complex|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|ISOMERASE/CHAPERONE","7R0L|Structure of the FK1 domain of the FKBP51 G64S variant in complex with SAFit1|X-RAY DIFFRACTION|1.1|Homo sapiens|0|ISOMERASE","8BA6|Structure of the FK1 domain of the FKBP51 G64S variant in complex with (2R,5S,12R)-12-cyclohexyl-2-[2-(3,4-dimethoxyphenyl)ethyl]-15,15,16-trimethyl-3,19-dioxa-10,13,16-triazatricyclo[18.3.1.0^5,^10]tetracosa-1(24),20,22-triene-4,11,14,17-tetrone|X-RAY DIFFRACTION|1.1|Homo sapiens|0|ISOMERASE","8BAJ|Structure of the FK1 domain of the FKBP51 G64S variant in complex with (1S,5S,6R)-10-((3,5-dichlorophenyl)sulfonyl)-5-(hydroxymethyl)-3-(pyridin-2-ylmethyl)-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.2|Homo sapiens|0|ISOMERASE","8CCA|The Fk1 domain of FKBP51 in complex with SAFit1|X-RAY DIFFRACTION|1.33|Homo sapiens|0|ISOMERASE","8CCB|The Fk1 domain of FKBP51 in complex with 2-(3-((1R)-1-(((2S)-1-(2-(5-chlorothiophen-2-yl)-2-cyclohexylacetyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1.7|Homo sapiens|0|ISOMERASE","8CCC|The Fk1 domain of FKBP51 in complex with 2-(3-((R)-1-(((S)-1-((S)-2-(5-chlorothiophen-2-yl)propanoyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1.55|Homo sapiens|0|ISOMERASE","8CCD|The Fk1 domain of FKBP51 in complex with 2-(3-((R)-1-(((S)-1-((S)-2-(5-chlorothiophen-2-yl)-2-(3,4,5-trimethoxyphenyl)acetyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|2.1|Homo sapiens|0|ISOMERASE","8CCE|The Fk1 domain of FKBP51 in complex with 2-(3-((R)-1-(((S)-1-((S)-2-(5-chlorothiophen-2-yl)butanoyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1.4|Homo sapiens|0|ISOMERASE","8CCF|The Fk1 domain of FKBP51 in complex with 2-(3-((R)-1-(((S)-1-((S)-2-(5-chlorothiophen-2-yl)pent-4-enoyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|2|Homo sapiens|0|ISOMERASE","8CCG|The Fk1 domain of FKBP51 in complex with (2R,5S,12S)-12-(thiophen-2-yl)-2-[2-(3,4-dimethoxyphenyl)ethyl]-15,15-dimethyl-3,19-dioxa-10,13,16-triazatricyclo[18.3.1.0^5,^10]tetracosa-1(24),20,22-triene-4,11,14,17-tetrone|X-RAY DIFFRACTION|1.3|Homo sapiens|0|ISOMERASE","8CCH|The Fk1 domain of FKBP51 in complex with 2-(3-((1R)-1-(((2S)-1-(2-cyclohexyl-2-(thiophen-2-yl)acetyl)piperidine-2-carbonyl)oxy)-3-(3,4-dimethoxyphenyl)propyl)phenoxy)acetic acid|X-RAY DIFFRACTION|1.73|Homo sapiens|0|ISOMERASE","8CHN|The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|0.99|Homo sapiens|0|ISOMERASE","8CHP|The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-(3,5-dichlorophenyl)sulfinyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1|Homo sapiens|0|ISOMERASE","8CHQ|The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((S)-3,5-dichloro-N-methylphenylsulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.01|Homo sapiens|0|ISOMERASE","8CHR|The FK1 domain of FKBP51 in complex with (1S,5S,6R)-10-((R)-(3,5-dichlorophenyl)sulfonimidoyl)-3-(pyridin-2-ylmethyl)-5-vinyl-3,10-diazabicyclo[4.3.1]decan-2-one|X-RAY DIFFRACTION|1.1|Homo sapiens|0|ISOMERASE","8FFW|Cryo-EM structure of the GR-Hsp90-FKBP51 complex|ELECTRON MICROSCOPY|3.23|Homo sapiens|0|CHAPERONE","8PC2|SelDeg51 in complex with FKBP51FK1 domain and pVHL:EloB:EloC|X-RAY DIFFRACTION|2.8|Homo sapiens|0|ISOMERASE","8PJ8|FKBP51FK1 F67E/K60Orn (i, i+7) in complex with SAFit1|X-RAY DIFFRACTION|1.5||0|ISOMERASE","8PJA|FKBP51FK1 F67E/K58 (i, i+9) in complex with SAFit1|X-RAY DIFFRACTION|1.6||0|ISOMERASE","8R5K|The Fk1 domain of FKBP51 in complex with Antascomicine B|X-RAY DIFFRACTION|0.89|Homo sapiens|0|ISOMERASE","9EU6|The FK1 domain of FKBP51 in complex with SAFit-analog 23j|X-RAY DIFFRACTION|1.54|Homo sapiens|0|ISOMERASE","9EU7|The FK1 domain of FKBP51 in complex with SAFit-analog 15b|X-RAY DIFFRACTION|2.21|Homo sapiens|0|ISOMERASE","9EU8|The FK1 domain of FKBP51 in complex with SAFit-analog 15h|X-RAY DIFFRACTION|2.3|Homo sapiens|0|ISOMERASE","9EU9|The FK1 domain of FKBP51 in complex with SAFit-analog 15i|X-RAY DIFFRACTION|1.8|Homo sapiens|0|ISOMERASE","9EUA|The FK1 domain of FKBP51 in complex with SAFit-analog 23d|X-RAY DIFFRACTION|2.5|Homo sapiens|0|ISOMERASE","9EUB|The FK1 domain of FKBP51 in complex with SAFit-analog 24e|X-RAY DIFFRACTION|2|Homo sapiens|0|ISOMERASE","9EUC|The FK1 domain of FKBP51 in complex with SAFit-analog 23b|X-RAY DIFFRACTION|2.4|Homo sapiens|0|ISOMERASE","9EUD|The FK1 domain of FKBP51 in complex with SAFit-analog 23c|X-RAY DIFFRACTION|2.022|Homo sapiens|0|ISOMERASE","9EUE|The FK1 domain of FKBP51 in complex with SAFit-analog 23a|X-RAY DIFFRACTION|2|Homo sapiens|0|ISOMERASE","9EY3|The FK1 domain of FKBP51 in complex with (3S,11S,11aS)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxylic acid|X-RAY DIFFRACTION|1.16|Homo sapiens|0|ISOMERASE","9EY4|The FK1 domain of FKBP51 in complex with (3S,11S)-12-((3,5-dichlorophenyl)sulfonyl)-5-oxo-11-vinyldecahydro-1H-6,10-epiminopyrrolo[1,2-a]azonine-3-carboxamide|X-RAY DIFFRACTION|1.16|Homo sapiens|0|ISOMERASE","9GPK|The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog 12c/j|X-RAY DIFFRACTION|1.75|Homo sapiens|0|ISOMERASE","9GPL|The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog 11c/i|X-RAY DIFFRACTION|1.8|Homo sapiens|0|ISOMERASE","9GPM|The FK1 domain of FKBP51 in complex with the macrocyclic SAFit analog 12c/i|X-RAY DIFFRACTION|1.55|Homo sapiens|0|ISOMERASE"]},{"input":"Q15678","source":"Q15678|Tyrosine-protein phosphatase non-receptor type 14","targets":["2BZL|CRYSTAL STRUCTURE OF THE HUMAN PROTEIN TYROSINE PHOSPHATASE N14 AT 1. 65 A RESOLUTION|X-RAY DIFFRACTION|1.65|HOMO SAPIENS|0|HYDROLASE","6IWD|The PTP domain of human PTPN14 in a complex with the CR3 domain of HPV18 E7|X-RAY DIFFRACTION|1.8|Homo sapiens; Human papillomavirus type 18|0|ONCOPROTEIN","6JJW|Crystal Structure of KIBRA and PTPN14 complex|X-RAY DIFFRACTION|2.4|Homo sapiens; Mus musculus|0|SIGNALING PROTEIN"]},{"input":"P10636","source":"P10636|Microtubule-associated protein tau","targets":["1I8H|SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMAN TAU PHOSPHOTHREONINE PEPTIDE|SOLUTION NMR|||0|MEMBRANE PROTEIN/ISOMERASE","22JY|P301L/S320F human tau filaments from mouse brain|ELECTRON MICROSCOPY|2.2|Homo sapiens|0|PROTEIN FIBRIL","2MZ7|Structure of Tau(267-312) bound to Microtubules|SOLUTION NMR|||0|PROTEIN BINDING","2ON9|Structure of an amyloid forming peptide VQIVYK from the repeat region of Tau|X-RAY DIFFRACTION|1.51||0|PROTEIN FIBRIL","3OVL|Structure of an amyloid forming peptide VQIVYK from the TAU protein in complex with orange G|X-RAY DIFFRACTION|1.81||0|PROTEIN FIBRIL","4E0M|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form I)|X-RAY DIFFRACTION|1.75||0|PROTEIN FIBRIL","4E0N|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form II)|X-RAY DIFFRACTION|1.65||0|PROTEIN FIBRIL","4E0O|SVQIVYK segment from human Tau (305-311) displayed on 54-membered macrocycle scaffold (form III)|X-RAY DIFFRACTION|1.82||0|PROTEIN FIBRIL","4FL5|Crystal structure of human 14-3-3 sigma in complex with a Tau-protein peptide surrounding pS214|X-RAY DIFFRACTION|1.9|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","4GLR|Structure of the anti-ptau Fab (pT231/pS235_1) in complex with phosphoepitope pT231/pS235|X-RAY DIFFRACTION|1.9|Gallus gallus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4NP8|Structure of an amyloid forming peptide VQIVYK from the second repeat region of tau (alternate polymorph)|X-RAY DIFFRACTION|1.51||0|PROTEIN FIBRIL","4TQE|Structure of tau peptide in complex with Tau5 antibody Fab fragment|X-RAY DIFFRACTION|1.6|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","4Y32|Crystal structure of C-terminal modified Tau peptide-hybrid 109B with 14-3-3sigma|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","4Y5I|Crystal structure of C-terminal modified Tau peptide-hybrid 126B with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","5BTV|Crystal structure of human 14-3-3 sigma in complex with a Tau-protein peptide surrounding pS324|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","5DMG|X-RAY STRUCTURE OF THE FAB FRAGMENT OF THE ANTI TAU ANTIBODY RB86 IN COMPLEX WITH THE PHOSPHORYLATED TAU PEPTIDE (416-430)|X-RAY DIFFRACTION|2.5|Oryctolagus cuniculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5E2V|Anti-TAU AT8 FAB with doubly phosphorylated TAU peptide|X-RAY DIFFRACTION|1.64|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5E2W|Anti-TAU AT8 FAB with triply phosphorylated TAU peptide|X-RAY DIFFRACTION|1.5|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5HF3|Crystal structure of C-terminal modified Tau peptide-hybrid 201D with 14-3-3sigma|X-RAY DIFFRACTION|1.8|Homo sapiens; SYNTHETIC CONSTRUCT|0|SIGNALING PROTEIN","5K7N|MicroED structure of tau VQIVYK peptide at 1.1 A resolution|ELECTRON CRYSTALLOGRAPHY|1.1||0|PROTEIN FIBRIL","5MO3|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 8.5|X-RAY DIFFRACTION|1.69|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP1|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 7.5|X-RAY DIFFRACTION|3.1|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP3|Crystal structure of DC8E8 Fab in the complex with a 30-mer tau peptide at pH 6.5|X-RAY DIFFRACTION|2.75|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5MP5|Crystal structure of DC8E8 Fab in the complex with a 14-mer tau peptide at pH 6.5|X-RAY DIFFRACTION|2.31|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5N5A|Structure of Tau(254-290) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5N5B|Structure of Tau(292-319) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5NVB|Structure of Tau(254-268) bound to F-actin|SOLUTION NMR|||0|STRUCTURAL PROTEIN","5O3L|Paired helical filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|STRUCTURAL PROTEIN","5O3O|Pronase-treated paired helical filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","5O3T|Straight filament in Alzheimer's disease brain|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","5V5B|KVQIINKKLD, Structure of the amyloid spine from microtubule associated protein tau Repeat 2|ELECTRON CRYSTALLOGRAPHY|1.5||0|STRUCTURAL PROTEIN","5V5C|VQIINK, Structure of the amyloid-spine from microtubule associated protein tau Repeat 2|ELECTRON CRYSTALLOGRAPHY|1.25||0|STRUCTURAL PROTEIN","5ZIA|Crystal structure of human anti-tau antibody CBTAU-24.1 in complex with its phosphorylated tau peptide|X-RAY DIFFRACTION|2.603|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","5ZV3|Crystal structure of human anti-tau antibody CBTAU-28.1 in complex with its tau peptide|X-RAY DIFFRACTION|2.093|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6BB4|Fab/epitope complex of mouse monoclonal antibody C5.2 targeting a phospho-tau epitope.|X-RAY DIFFRACTION|2.099|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6CVJ|Model of synthetic tau (four tandem repeats of first repeat sequence) bound to the microtubule|ELECTRON MICROSCOPY|3.2|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","6CVN|Model of synthetic tau (R2x4) bound to the microtubule|ELECTRON MICROSCOPY|3.9|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","6DC8|Fab/epitope complex of mouse monoclonal antibody 8B2 targeting a non-phosphorylated tau epitope.|X-RAY DIFFRACTION|1.799|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6DC9|Fab/epitope complex of human chimeric monoclonal antibody h4E6 targeting a phosphorylated tau epitope.|X-RAY DIFFRACTION|2.999|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6DCA|Fab/epitope complex of mouse monoclonal antibody 6B2 targeting a non-phosphorylated tau epitope.|X-RAY DIFFRACTION|2.599|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6FAU|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2e-I with 14-3-3sigma|X-RAY DIFFRACTION|1.25|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FAV|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-I with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FAW|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2c-I with 14-3-3sigma|X-RAY DIFFRACTION|1.4|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FBW|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2f-II with 14-3-3sigma|X-RAY DIFFRACTION|1.45|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FBY|Crystal structure of C-terminal modified Tau peptide-hybrid 4.2b with 14-3-3sigma|X-RAY DIFFRACTION|1.5|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FI4|Crystal structure of C-terminal modified Tau peptide-hybrid 3.2e with 14-3-3sigma|X-RAY DIFFRACTION|2|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6FI5|Crystal structure of C-terminal modified Tau peptide-hybrid 3.2d with 14-3-3sigma|X-RAY DIFFRACTION|1.7|Homo sapiens; SYNTHETIC CONSTRUCT|0|STRUCTURAL PROTEIN","6GK7|Crystal structure of anti-tau antibody dmCBTAU-27.1, double mutant (S31Y, T100I) of CBTAU-27.1, in complex with Tau peptide A8119B (residues 299-318)|X-RAY DIFFRACTION|2.95|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6GK8|Crystal structure of anti-tau antibody dmCBTAU-28.1, double mutant (S32R, E35K) of CBTAU-28.1, in complex with Tau peptide A7731 (residues 52-71)|X-RAY DIFFRACTION|2.85|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6GX5|Narrow Pick Filament from Pick's disease brain|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6H06|FAB CBTAU-22.1 IN COMPLEX WITH TAU PEPTIDE V1088-5|X-RAY DIFFRACTION|2.63|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6HRE|Paired helical filament from sporadic Alzheimer's disease brain|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6HRF|Straight filament from sporadic Alzheimer's disease brain|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6LRA|The complex structure of PHF core domain peptide of tau and antibody's Fab domain.|X-RAY DIFFRACTION|1.9|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","6N4P|RQEFEV, crystal structure of the N-terminal segment RQEFEV from protein tau|X-RAY DIFFRACTION|1.851||0|PROTEIN FIBRIL","6NK4|KVQIINKKL, crystal structure of a tau protein fragment|ELECTRON CRYSTALLOGRAPHY|1.994||0|STRUCTURAL PROTEIN","6NWP|Chronic traumatic encephalopathy Type I Tau filament|ELECTRON MICROSCOPY|2.3|Homo sapiens|0|PROTEIN FIBRIL","6NWQ|Chronic traumatic encephalopathy Type II Tau filament|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","6ODG|SVQIVY, Crystal Structure of a tau protein fragment|X-RAY DIFFRACTION|1||0|PROTEIN FIBRIL","6PXR|Anti-TAU BIIB092 FAB with TAU peptide|X-RAY DIFFRACTION|1.556|Homo sapiens; Mus musculus|0|IMMUNE SYSTEM","6QJH|Cryo-EM structure of heparin-induced 2N4R tau snake filaments|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6QJM|Cryo-EM structure of heparin-induced 2N4R tau twister filaments|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6QJP|Cryo-EM structure of heparin-induced 2N4R tau jagged filaments|ELECTRON MICROSCOPY|3.5|Homo sapiens|0|PROTEIN FIBRIL","6QJQ|Cryo-EM structure of heparin-induced 2N3R tau filaments|ELECTRON MICROSCOPY|3.7|Homo sapiens|0|PROTEIN FIBRIL","6TJO|Cryo-EM structure of TypeI tau filaments extracted from the brains of individuals with Corticobasal degeneration|ELECTRON MICROSCOPY|3.2|Homo sapiens|0|PROTEIN FIBRIL","6TJX|Cryo-EM structure of TypeII tau filaments extracted from the brains of individuals with Corticobasal degeneration|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","6VH7|Doublet Tau Fibril from Corticobasal Degeneration Human Brain Tissue|ELECTRON MICROSCOPY|3.8|Homo sapiens|0|PROTEIN FIBRIL","6VHA|Singlet Tau Fibril from Corticobasal Degeneration Human Brain Tissue|ELECTRON MICROSCOPY|4.3|Homo sapiens|0|PROTEIN FIBRIL","6VHL|Paired Helical Filament from Alzheimer's Disease Human Brain Tissue|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6VI3|Straight Filament from Alzheimer's Disease Human Brain Tissue|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","6XLI|CRYSTAL STRUCTURE OF ANTI-TAU ANTIBODY PT3 Fab+pT212/pT217-TAU PEPTIDE|X-RAY DIFFRACTION|2|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7EYC|Crystal structure of Tau and acetylated tau peptide antigen|X-RAY DIFFRACTION|2.49|Mus musculus; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7KQK|anti-pTau C21-ABS Fab in complex with pTau peptide|X-RAY DIFFRACTION|2.6|Homo sapiens; SYNTHETIC CONSTRUCT|0|IMMUNE SYSTEM","7MKF|Paired helical tau filament extracted from PrP-CAA Patient brain tissue \\| tau filament \\| PHF Tau|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7MKG|Straight tau filament extracted from PrP-CAA Patient brain tissue \\| tau filament \\| SF Tau|ELECTRON MICROSCOPY|3.07|Homo sapiens|0|PROTEIN FIBRIL","7MKH|Paired helical tau filament extracted from GSS Patient brain tissue \\| tau filament from Gerstmann Straussler Scheinker disease \\| PHF Tau|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7NRQ|Paired helical filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.76|Homo sapiens|0|PROTEIN FIBRIL","7NRS|Conformation 1 of straight filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.68|Homo sapiens|0|PROTEIN FIBRIL","7NRT|Conformation 2 of straight filament from primary age-related tauopathy brain|ELECTRON MICROSCOPY|2.68|Homo sapiens|0|PROTEIN FIBRIL","7NRV|Paired helical filament from Alzheimer's disease with PET ligand APN-1607|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7NRX|Straight filament from Alzheimer's disease with PET ligand APN-1607|ELECTRON MICROSCOPY|3.55|Homo sapiens|0|PROTEIN FIBRIL","7P65|Progressive supranuclear palsy tau filament|ELECTRON MICROSCOPY|2.7|Homo sapiens|0|PROTEIN FIBRIL","7P66|Globular glial tauopathy type 1 tau filament|ELECTRON MICROSCOPY|3.0|Homo sapiens|0|PROTEIN FIBRIL","7P67|Globular glial tauopathy type 2 tau filament|ELECTRON MICROSCOPY|3.1|Homo sapiens|0|PROTEIN FIBRIL","7P68|Globular glial tauopathy type 3 tau filament|ELECTRON MICROSCOPY|2.9|Homo sapiens|0|PROTEIN FIBRIL","7P6A|Limbic-predominant neuronal inclusion body 4R tauopathy type 1a tau filament|ELECTRON MICROSCOPY|1.9|Homo sapiens|0|PROTEIN FIBRIL","7P6B|Limbic-predominant neuronal inclusion body 4R tauopathy type 1b tau filament|ELECTRON MICROSCOPY|2.2|Homo sapiens|0|PROTEIN FIBRIL","7P6C|Limbic-predominant neuronal inclusion body 4R tauopathy type 2 tau filament|ELECTRON MICROSCOPY|2.5|Homo sapiens|0|PROTEIN FIBRIL","7P6D|Argyrophilic grain disease type 1 tau filament|ELECTRON MICROSCOPY|3.3|Homo sapiens|0|PROTEIN FIBRIL","7P6E|Argyrophilic grain disease type 2 tau filament|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7PQC|tau-microtubule structural ensemble based on CryoEM data|ELECTRON MICROSCOPY|4.1|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","7PQP|tau-microtubule structural ensemble based on CryoEM data|ELECTRON MICROSCOPY|4.1|Homo sapiens; Sus scrofa|0|STRUCTURAL PROTEIN","7QJV|In vitro assembled tau filaments into Quadruple Helical Filaments type 1 (2c)|ELECTRON MICROSCOPY|3.29|Homo sapiens|0|PROTEIN FIBRIL","7QJW|In vitro assembled tau filaments with structures like chronic traumatic encephalopathy type II (8a)|ELECTRON MICROSCOPY|2.81|Homo sapiens|0|PROTEIN FIBRIL","7QJX|In vitro assembled 297-394 tau filaments, 700 rpm (34b)|ELECTRON MICROSCOPY|2.99|Homo sapiens|0|PROTEIN FIBRIL","7QJY|In vitro assembled 266/297 - 391 tau filaments with LiCl (9a)|ELECTRON MICROSCOPY|3.14|Homo sapiens|0|PROTEIN FIBRIL","7QJZ|In vitro assembled 266/297 - 391 tau filaments with LiCl (9b)|ELECTRON MICROSCOPY|3.4|Homo sapiens|0|PROTEIN FIBRIL","7QK1|In vitro assembled 297-394 tau filaments in PBS (35d)|ELECTRON MICROSCOPY|3.03|Homo sapiens|0|PROTEIN FIBRIL","7QK2|In vitro assembled 300-391 tau filaments in PBS (36a)|ELECTRON MICROSCOPY|2.61|Homo sapiens|0|PROTEIN FIBRIL","7QK3|In vitro assembled 258-391 tau filaments, 700 rpm (38a)|ELECTRON MICROSCOPY|2.44|Homo sapiens|0|PROTEIN FIBRIL"]}],"not_found":["P29122"]}