{"global_stoichiometry": "Hetero 12-mer - A6B6 ", "ligstr": "CIT:G:C6 H8 O7:192.12:CITRIC ACID:C(C(=O)O)C(CC(=O)O)(C(=O)O)O:InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12):KRKNYBCHXYNGOX-UHFFFAOYSA-N;FE:G:Fe 3:55.85:FE (III) ION:[Fe+3]:InChI=1S/Fe/q+3:VTLYFUHAOXGGBS-UHFFFAOYSA-N;CIT:I:C6 H8 O7:192.12:CITRIC ACID:C(C(=O)O)C(CC(=O)O)(C(=O)O)O:InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12):KRKNYBCHXYNGOX-UHFFFAOYSA-N;FE:I:Fe 3:55.85:FE (III) ION:[Fe+3]:InChI=1S/Fe/q+3:VTLYFUHAOXGGBS-UHFFFAOYSA-N", "uniprot_ac": "", "inchi": "InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)%%InChI=1S/Fe/q+3%%InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)%%InChI=1S/Fe/q+3", "reference": "J Am Chem Soc. 2013 Jul 17;135(28):10202-5.", "author": "Apostol, M.I., Perry, K., Surewicz, W.K.", "type": "Fibril", "ligand_id": "CIT%%FE%%CIT%%FE", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "", "gene_names": "", "chain_id": "G%%G%%I%%I", "ligand_mw": "192.12%%55.85%%192.12%%55.85", "inchi_key": "KRKNYBCHXYNGOX-UHFFFAOYSA-N%%VTLYFUHAOXGGBS-UHFFFAOYSA-N%%KRKNYBCHXYNGOX-UHFFFAOYSA-N%%VTLYFUHAOXGGBS-UHFFFAOYSA-N", "secondary_structure": "HDCVNI#CEEEEC&EQMCIT#CEEEEC&HDCVNI#CEEEEC&EQMCIT#CEEEEC&HDCVNI#CCEEEC&EQMCIT#CEEEEC&HDCVNI#CCEEEC&EQMCIT#CEEEEC&HDCVNI#CEEEEC&EQMCIT#CEEEEC&HDCVNI#CCEEEC&EQMCIT#CEEEEC", "amyloid_non_amyloid": "Non-amyloid", "length": "6", "remarks": "Fragment of human prion protein; Instead of forming a pair of sheets steric zipper reflective of amyloid, the DBPrP fragment assembled into distinct beta-sheet oligomers", "protein_name": "Prion protein", "peptide_protein_sequence": "chain-ID A: HDCVNI; chain-ID B: EQMCIT; chain-ID C: HDCVNI; chain-ID D: EQMCIT; chain-ID E: HDCVNI; chain-ID F: EQMCIT; chain-ID G: HDCVNI; chain-ID H: EQMCIT; chain-ID I: HDCVNI; chain-ID J: EQMCIT; chain-ID K: HDCVNI; chain-ID L: EQMCIT", "ligand_name": "CITRIC ACID%%FE (III) ION%%CITRIC ACID%%FE (III) ION", "ligand_smiles": "C(C(=O)O)C(CC(=O)O)(C(=O)O)O%%[Fe+3]%%C(C(=O)O)C(CC(=O)O)(C(=O)O)O%%[Fe+3]", "pdb_id": "4E1H", "ec_number": "", "pdb_classification": "CELL CYCLE", "mutation_s_field": "No", "ligand_formula": "C6 H8 O7%%Fe 3%%C6 H8 O7%%Fe 3", "r_value_free": "0.218", "alternative_name": "", "description": "The crystal structure of a fragment from human prion protein consisting of the disulfide-bond-linked portions of helices 2 and 3. Instead of forming a pair-of-sheets steric zipper structure characteristic of amyloid fibers, this fragment crystallized into a Beta-sheet-rich assembly of hexameric oligomers. This study reveals a never before observed structural motif for ordered protein aggregates and suggests a possible mechanism for self-propagation of misfolded conformations by such nonamyloid oligomers.", "resolution": "1.4", "pmid": "23808589", "entry": "S-0317"}