{"global_stoichiometry": "", "ligstr": "", "uniprot_ac": "Q13148", "inchi": "", "reference": "Nat Struct Mol Biol. 2018 Apr;25(4):311-319.", "author": "Guenther, E.L., Ge, P., Trinh, H., Sawaya, M.R., Cascio, D., Boyer, D.R., Gonen, T., Zhou, Z.H., Eisenberg, D.S.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "ELECTRON MICROSCOPY", "keyword": "TAR DNA-binding protein 43", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "DLIIKGISVHI#CCCCCCCCCCC&DLIIKGISVHI#CCCCCCCCCCC&DLIIKGISVHI#CCCCCSSSCCC&DLIIKGISVHI#CCCCCSSSCCC&DLIIKGISVHI#CCCCCCSSCCC&DLIIKGISVHI#CCCCCCSSCCC&DLIIKGISVHI#CCCCCCCCCCC&DLIIKGISVHI#CCCCCCCCCCC&DLIIKGISVHI#CCCCCCCCCCC", "amyloid_non_amyloid": "Amyloid", "length": "11", "remarks": "CryoEM structure of the segment, DLIIKGISVHI, assembled into a triple-helical fibril", "protein_name": "TAR DNA-binding protein 43", "peptide_protein_sequence": "chain-ID 0: DLIIKGISVHI; chain-ID 1: DLIIKGISVHI; chain-ID 2: DLIIKGISVHI; chain-ID 3: DLIIKGISVHI; chain-ID 4: DLIIKGISVHI; chain-ID 5: DLIIKGISVHI; chain-ID 6: DLIIKGISVHI; chain-ID 7: DLIIKGISVHI; chain-ID 8: DLIIKGISVHI", "ligand_name": "", "ligand_smiles": "", "pdb_id": "5W7V", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "", "alternative_name": "", "description": "They show that the 247 DLIIKGISVHI 257 segment from the second RNA-recognition motif (RRM2) forms an array of amyloid polymorphs. These associations include seven distinct interfaces displaying five different symmetry classes of steric zippers. This segment can adopt three different backbone conformations that contribute to its polymorphic capabilities. The polymorphic nature of this segment illustrates at the molecular level how amyloid proteins can form diverse fibril structures.", "resolution": "3.8", "pmid": "29531287", "entry": "S-0485"}