{"global_stoichiometry": "Homo 15-mer - A15", "ligstr": "", "uniprot_ac": "Q13148", "inchi": "", "reference": "Nat Struct Mol Biol. 2018 Jun;25(6):463-471.", "author": "Guenther, E.L., Cao, Q., Trinh, H., Lu, J., Sawaya, M.R., Cascio, D., Boyer, D.R., Rodriguez, J.A., Hughes, M.P., Eisenberg, D.S.", "type": "Fibril", "ligand_id": "", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Segment of TAR DNA-binding protein 43", "gene_names": "", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "NFGAFS#CCCSCC", "amyloid_non_amyloid": "Non-amyloid", "length": "6", "remarks": "Crystal structure of the segment, NFGAFS, from the low complexity domain of TDP-43, residues 312-317", "protein_name": "TAR DNA-binding protein 43", "peptide_protein_sequence": "chain-ID A: NFGAFS", "ligand_name": "", "ligand_smiles": "", "pdb_id": "5WHN", "ec_number": "", "pdb_classification": "PROTEIN FIBRIL", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.16", "alternative_name": "", "description": "To uncover the structural origins of two modes of Beta-sheet-rich aggregation (reversible stress granules and irreversible pathogenic amyloid), they have determined ten structures of segments of the LCD of human TDP-43. Six of these segments form steric zippers characteristic of the spines of pathogenic amyloid fibrils; four others form LARKS, the labile amyloid-like interactions characteristic of protein hydrogels and proteins found in membraneless organelles, including stress granules. 312NFGAFS317 forms a LARKS structure and its microcrystalline aggregates are labile", "resolution": "1.1", "pmid": "29786080", "entry": "S-0486"}