{"amyloid_non_amyloid": "Amyloid", "description": "They analyse amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-Beta sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar Beta-arch conformations within the N-terminal 21 residues.", "ligand_formula": "", "chain_id": "", "global_stoichiometry": "Homo 12-mer - A12 ", "gene_names": "SAA1", "mutation_s_field": "No", "uniprot_ac": "P0DJI8", "species": "Homo sapiens", "ligand_name": "", "pdb_id": "6MST", "ligand_id": "", "reference": "", "resolution": "2.7", "inchi": "", "method": "ELECTRON MICROSCOPY", "ligand_smiles": "", "keyword": "Serum amyloid A-1 protein", "remarks": "Cryo-EM structure of human AA amyloid fibril", "length": "66", "peptide_protein_sequence": "chain-ID A: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID B: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID C: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID D: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID E: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID F: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID G: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID H: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID I: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID J: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID K: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR; chain-ID L: SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR", "protein_name": "Serum amyloid A-1 protein", "entry": "S-0562", "inchi_key": "", "author": "Liberta, F., Loerch, S., Rennegarbe, M., Schierhorn, A., Westermark, P., Westermark, G.T., Hazenberg, B.P.C., Grigorieff, N., Fandrich, M., Schmidt, M.", "ligstr": "", "secondary_structure": "SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC&SFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQR#CBSCEEEESCBCCTTCEEEEEECTTCCEESCCBSTEEESCEECCEECCCSEEECCCCCCCCCCCCC", "pdb_classification": "PROTEIN FIBRIL", "ligand_mw": "", "r_value_free": "", "alternative_name": "", "type": "Fibril", "pmid": "", "ec_number": ""}