{"resolution": "1.99", "ligand_mw": "", "secondary_structure": "AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC&AIIGLM#CEEEEC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P05067", "remarks": "Structure of segment AIIGLM from the amyloid-beta peptide (Ab, residues 30-35)", "description": "ABeta molecules form Beta-sheet containing structures that assemble into a variety of polymorphic oligomers, protofibers, and fibers that exhibit a range of lifetimes and cellular toxicities. This polymorphic nature of ABeta has frustrated its biophysical characterization, its structural determination, and our understanding of its pathological mechanism. They determined eight new microcrystal structures of fiber-forming segments of ABeta. These structures, all of short, self-complementing pairs of Beta-sheets termed steric zippers, reveal a variety of modes of self-association of ABeta. ", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "AMYLOID BETA A4 PROTEIN", "ligstr": "", "pmid": "21949245", "mutation_s_field": "No", "author": "Colletier, J., Laganowsky, A., Landau, M., Zhao, M., Soriaga, A.B., Goldschmidt, L., Flot, D., Cascio, D., Sawaya, M.R., Eisenberg, D.", "pdb_id": "2Y3J", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.267", "protein_name": "Amyloid-beta A4 protein", "gene_names": "", "global_stoichiometry": "Homo 8-mer - A8 ", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: AIIGLM; chain-ID B: AIIGLM; chain-ID C: AIIGLM; chain-ID D: AIIGLM; chain-ID E: AIIGLM; chain-ID F: AIIGLM; chain-ID G: AIIGLM; chain-ID H: AIIGLM", "pdb_classification": "PROTEIN FIBRIL", "reference": "Proc Natl Acad Sci U S A. 2011 Oct 11;108(41):16938-43.", "length": "6", "entry": "S-0180"}