{"method": "X-RAY DIFFRACTION", "mutation_s_field": "No", "ec_number": "", "description": "They found that the segment of the insulin B-chain with sequence LVEALYL is the smallest segment that both nucleates and inhibits the fibrillation of full-length insulin in a molar ratio-dependent manner, suggesting that this segment is central to the cross-Beta spine of the insulin fibril. In isolation from the rest of the protein, LVEALYL forms microcrystalline aggregates with fibrillar morphology, the structure of which they determined to 1 A resolution. The LVEALYL segments are stacked into pairs of tightly interdigitated Beta-sheets, each pair displaying the dry steric zipper interface typical of amyloid-like fibrils.", "ligstr": "", "pmid": "19864624", "remarks": "LVEALYL peptide derived from human insulin chain B, residues 11-17", "amyloid_non_amyloid": "Amyloid", "type": "Fibril", "inchi": "", "resolution": "1.0", "species": "Homo sapiens", "secondary_structure": "LVEALYL#CCCCCCC", "chain_id": "", "gene_names": "", "r_value_free": "0.18", "pdb_id": "3HYD", "reference": "Proc Natl Acad Sci U S A. 2009 Nov 10;106(45):18990-5.", "keyword": "Insulin", "protein_name": "Insulin", "ligand_formula": "", "peptide_protein_sequence": "chain-ID A: LVEALYL", "entry": "S-0248", "length": "7", "uniprot_ac": "P01308", "author": "Ivanova, M.I., Sievers, S.A., Sawaya, M.R., Wall, J.S., Eisenberg, D.", "ligand_smiles": "", "ligand_mw": "", "alternative_name": "", "ligand_name": "", "pdb_classification": "PROTEIN FIBRIL", "global_stoichiometry": "Homo 4-mer - A4 ", "inchi_key": "", "ligand_id": ""}