{"global_stoichiometry": "Homo 12-mer - A12 ", "ligstr": "MPD:A:C6 H14 O2:118.17:(4S)-2-METHYL-2,4-PENTANEDIOL:C[C@@H](CC(C)(C)O)O:InChI=1S/C6H14O2/c1-5(7)4-6(2,3)8/h5,7-8H,4H2,1-3H3/t5-/m0/s1:SVTBMSDMJJWYQN-YFKPBYRVSA-N", "uniprot_ac": "", "inchi": "InChI=1S/C6H14O2/c1-5(7)4-6(2,3)8/h5,7-8H,4H2,1-3H3/t5-/m0/s1", "reference": "J Phys Chem B. 2014 Jul 3;118(26):7247-56.", "author": "Do, T.D., LaPointe, N.E., Sangwan, S., Teplow, D.B., Feinstein, S.C., Sawaya, M.R., Eisenberg, D.S., Bowers, M.T.", "type": "Fibril", "ligand_id": "MPD", "species": "synthetic construct", "method": "X-RAY DIFFRACTION", "keyword": "[Leu-5]-Enkephalin mutant - YVVFV", "gene_names": "", "chain_id": "A", "ligand_mw": "118.17", "inchi_key": "SVTBMSDMJJWYQN-YFKPBYRVSA-N", "secondary_structure": "YVVFV#CEEEC&YVVFV#CEEEC", "amyloid_non_amyloid": "Amyloid", "length": "5", "remarks": "[Leu-5]-Enkephalin mutant - YVVFV", "protein_name": "enkephalin mutants", "peptide_protein_sequence": "chain-ID A: YVVFV; chain-ID B: YVVFV", "ligand_name": "(4S)-2-METHYL-2,4-PENTANEDIOL", "ligand_smiles": "C[C@@H](CC(C)(C)O)O", "pdb_id": "4OLR", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "C6 H14 O2", "r_value_free": "0.187", "alternative_name": "", "description": "[YVVFV fibril structure] The peptides YVVFL form oligomers and amyloid-like fibrils. YVVFV shows an early stage oligomer distribution similar to those of the previous two, but amyloid-like aggregates are less abundant. Atomic resolution X-ray structures of YVVFV show two different modes of interactions at the dry interface between steric zippers and pairs of antiparallel Beta-sheets, but both are less favorable than the packing motif found in YVVFL. Both YVVFV and YVVFL can form a Class 6 steric zipper. However, in YVVFV, the strands between mating sheets are parallel to each other and in YVVFL they are antiparallel. ", "resolution": "1.1", "pmid": "24915112", "entry": "S-0358"}