{"resolution": "1.1", "ligand_mw": "", "secondary_structure": "SYSGYS#CCCSCC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "P35637", "remarks": "SYSGYS from low-complexity domain of FUS, residues 37-42; kinked beta sheets", "description": "They determined the atomic structures of five segments from protein low-complexity domains associated with membraneless assemblies. Their common structural feature is the stacking of segments into kinked Beta sheets that pair into protofilaments. Unlike steric zippers of amyloid fibrils, the kinked sheets interact weakly through polar atoms and aromatic side chains. SYSGYS from low-complexity domain of FUS, residues 37-42.", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "SYSGYS peptide  from low-complexity domain of FUS", "ligstr": "", "pmid": "29439243", "mutation_s_field": "No", "author": "Hughes, M.P., Sawaya, M.R., Boyer, D.R., Goldschmidt, L., Rodriguez, J.A., Cascio, D., Chong, L., Gonen, T., Eisenberg, D.S.", "pdb_id": "6BWZ", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.165", "protein_name": "RNA-binding protein FUS", "gene_names": "", "global_stoichiometry": "", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: SYSGYS", "pdb_classification": "PROTEIN FIBRIL", "reference": "Science. 2018 Feb 9;359(6376):698-701.", "length": "6", "entry": "S-0504"}