{"resolution": "1.2", "ligand_mw": "", "secondary_structure": "AMMAAA#CEEEEC&AMMAAA#CEEEEC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "", "remarks": "Segment AMMAAA from the low complexity domain of TDP-43, residues 321-326", "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. Segments 321AMMAAA326 and 333SWGMMGMLASQ343 are Class 7 steric zippers with face-to-back and up-up orientation.", "type": "Fibril", "ligand_smiles": "", "chain_id": "", "species": "Homo sapiens", "keyword": "AMMAAA", "ligstr": "", "pmid": "29786080", "mutation_s_field": "No", "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.", "pdb_id": "6CEW", "amyloid_non_amyloid": "Amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.218", "protein_name": "TDP-43", "gene_names": "", "global_stoichiometry": "Homo 10-mer - A10", "alternative_name": "", "peptide_protein_sequence": "chain-ID A: AMMAAA; chain-ID B: AMMAAA", "pdb_classification": "PROTEIN FIBRIL", "reference": "Nat Struct Mol Biol. 2018 Jun;25(6):463-471.", "length": "6", "entry": "S-0522"}