{"global_stoichiometry": "Homo 6-mer - A6", "ligstr": "P4C:A:C14 H28 O8:324.37:O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL:C(COCCOCCOCCOCCOCCOCC=O)O:InChI=1S/C14H28O8/c15-1-3-17-5-7-19-9-11-21-13-14-22-12-10-20-8-6-18-4-2-16/h1,16H,2-14H2:CTLLATPOKUEFSQ-UHFFFAOYSA-N;P4C:B:C14 H28 O8:324.37:O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL:C(COCCOCCOCCOCCOCCOCC=O)O:InChI=1S/C14H28O8/c15-1-3-17-5-7-19-9-11-21-13-14-22-12-10-20-8-6-18-4-2-16/h1,16H,2-14H2:CTLLATPOKUEFSQ-UHFFFAOYSA-N", "uniprot_ac": "P0DJI8", "inchi": "InChI=1S/C14H28O8/c15-1-3-17-5-7-19-9-11-21-13-14-22-12-10-20-8-6-18-4-2-16/h1,16H,2-14H2%%InChI=1S/C14H28O8/c15-1-3-17-5-7-19-9-11-21-13-14-22-12-10-20-8-6-18-4-2-16/h1,16H,2-14H2", "reference": "Proc Natl Acad Sci U S A. 2014 Apr 8;111(14):5189-94.", "author": "Lu, J., Yu, Y., Zhu, I., Cheng, Y., Sun, P.D.", "type": "Protein", "ligand_id": "P4C%%P4C", "species": "Homo sapiens", "method": "X-RAY DIFFRACTION", "keyword": "Serum amyloid A-1 protein", "gene_names": "SAA1", "chain_id": "A%%B", "ligand_mw": "324.37%%324.37", "inchi_key": "CTLLATPOKUEFSQ-UHFFFAOYSA-N%%CTLLATPOKUEFSQ-UHFFFAOYSA-N", "secondary_structure": "MHHHHHHRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY#CCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHCCTTHHHHHHHHHHHHHHHTCHHHHHHHHHHHHHHHHHHHHHTCCHHHHHHHHHHHHHHHTTCCGGGGCCTTCCTTC&MHHHHHHRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY#CCCCCCCCHHHHHHHHHHHHHHHHHHHHHHHHHHCCTTCHHHHHHHHHHHHHHTCHHHHHHHHHHHHHHHHHHHHHTCCHHHHHHHHHHHHHHHTTCCGGGGCCTTCCTTC", "amyloid_non_amyloid": "Amyloid", "length": "111", "remarks": "Structure of native human serum amyloid A1", "protein_name": "Serum amyloid A-1 protein", "peptide_protein_sequence": "chain-ID A: MHHHHHHRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY; chain-ID B: MHHHHHHRSFFSFLGEAFDGARDMWRAYSDMREANYIGSDKYFHARGNYDAAKRGPGGVWAAEAISDARENIQRFFGHGAEDSLADQAANEWGRSGKDPNHFRPAGLPEKY", "ligand_name": "O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL%%O-ACETALDEHYDYL-HEXAETHYLENE GLYCOL", "ligand_smiles": "C(COCCOCCOCCOCCOCCOCC=O)O%%C(COCCOCCOCCOCCOCCOCC=O)O", "pdb_id": "4IP9", "ec_number": "", "pdb_classification": "PROTEIN BINDING", "mutation_s_field": "No", "ligand_formula": "C14 H28 O8%%C14 H28 O8", "r_value_free": "0.258", "alternative_name": "", "description": "They determined a structure of human SAA1 to understand its function and structural transition to amyloid. Native SAA1.1 exists as a hexamer, with subunits displaying a unique four-helix bundle fold stabilized by its long C-terminal tail. Structure-based mutational studies revealed two positive-charge clusters, near the center and apex of the hexamer, that are involved in SAA association with heparin. The binding of high-density lipoprotein involves only the apex region of SAA and can be inhibited by heparin. Peptide amyloid formation assays identified the N-terminal helices 1 and 3 as amyloidogenic peptides of SAA1.1.", "resolution": "2.5", "pmid": "24706838", "entry": "S-0330"}