{"global_stoichiometry": "Monomer - A ", "ligstr": "NH2:A:H2 N:16.02:AMINO GROUP:[NH2]:InChI=1/H3N/h1H3:QGZKDVFQNNGYKY-UHFFFAOYAF", "uniprot_ac": "P10997", "inchi": "InChI=1/H3N/h1H3", "reference": "Biochim Biophys Acta. 2011 Oct;1808(10):2337-42.", "author": "Nanga, R.P., Brender, J.R., Vivekanandan, S., Ramamoorthy, A.", "type": "Peptide", "ligand_id": "NH2", "species": "Homo sapiens", "method": "SOLUTION NMR", "keyword": "Islet amyloid polypeptide", "gene_names": "IAPP", "chain_id": "A", "ligand_mw": "16.02", "inchi_key": "QGZKDVFQNNGYKY-UHFFFAOYAF", "secondary_structure": "KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYX#CCSSSTHHHHHHHHHHHCTTHHHHHHHHCTTTTTTTCC", "amyloid_non_amyloid": "Amyloid", "length": "38", "remarks": "Solution NMR structure of human amylin in SDS micelles at pH 7.3", "protein_name": "Islet amyloid polypeptide", "peptide_protein_sequence": "chain-ID A: KCNTATCATQRLANFLVHSSNNFGAILSSTNVGSNTYX", "ligand_name": "AMINO GROUP", "ligand_smiles": "[NH2]", "pdb_id": "2L86", "ec_number": "", "pdb_classification": "APOPTOSIS", "mutation_s_field": "No", "ligand_formula": "H2 N", "r_value_free": "", "alternative_name": "Amylin, Diabetes-associated peptide, Insulinoma amyloid peptide", "description": "The structure of the naturally occurring peptide in detergent micelles at a neutral pH. The structure has an overall kinked helix motif, with residues 7-17 and 21-28 in a helical conformation, and with a 3(10) helix from Gly 33-Asn 35. In addition, the angle between the N- and C-terminal helices is constrained to 85\u00c2\u00b0. The greater helical content of human IAPP in the amidated versus free acid form is likely to play a role in its aggregation and membrane disruptive activity.", "resolution": "", "pmid": "21723249", "entry": "S-0118"}