{"reference": "Proc Natl Acad Sci U S A. 2004 Mar 30;101(13):4435-40. Epub  2004 Feb 26", "alternative_name": "", "entry": "S-0061", "gene_names": "", "remarks": "SYNTHETIC 17 AMINO ACID LONG PEPTIDE THAT FORMS A NATIVE-LIKE COILED-COIL AT AMBIENT TEMPERATURE AND AGGREGATES INTO AMYLOID-LIKE FIBRILS AT HIGHER TEMPERATURES.", "secondary_structure": "XSIRELEARIRELELRIG#CCHHHHHHHHHHHHHHCC", "chain_id": "A%%A%%A", "inchi": "InChI=1S/C2H4O/c1-2-3/h2H,1H3%%InChI=1S/Na/q+1%%InChI=1S/Zn/q+2", "amyloid_non_amyloid": "Amyloid", "pmid": "15070736", "ligand_smiles": "CC=O%%[Na+]%%[Zn+2]", "keyword": "SYNTHETIC COILED-COIL PEPTIDE", "peptide_protein_sequence": "chain-ID A: XSIRELEARIRELELRIG", "uniprot_ac": "", "protein_name": "Synthetic", "r_value_free": "0.233", "mutation_s_field": "No", "ligand_mw": "44.05%%22.99%%65.41", "pdb_id": "1S9Z", "inchi_key": "IKHGUXGNUITLKF-UHFFFAOYSA-N%%FKNQFGJONOIPTF-UHFFFAOYSA-N%%PTFCDOFLOPIGGS-UHFFFAOYSA-N", "ec_number": "", "pdb_classification": "DE NOVO PROTEIN", "type": "Peptide", "author": "Kammerer, R.A., Kostrewa, D., Zurdo, J., Detken, A., Green, J.D., Meier, B.H., Winkler, F.K., Dobson, C.M., Steinmetz, M.O.", "species": "", "ligand_id": "ACE%%nan%%ZN", "method": "X-RAY DIFFRACTION", "ligand_name": "ACETYL GROUP%%SODIUM ION%%ZINC ION", "global_stoichiometry": "Homo 3-mer - A3", "resolution": "2.01", "ligand_formula": "C2 H4 O%%Na 1%%Zn 2", "length": "18", "ligstr": "ACE:A:C2 H4 O:44.05:ACETYL GROUP:CC=O:InChI=1S/C2H4O/c1-2-3/h2H,1H3:IKHGUXGNUITLKF-UHFFFAOYSA-N;nan:A:Na 1:22.99:SODIUM ION:[Na+]:InChI=1S/Na/q+1:FKNQFGJONOIPTF-UHFFFAOYSA-N;ZN:A:Zn 2:65.41:ZINC ION:[Zn+2]:InChI=1S/Zn/q+2:PTFCDOFLOPIGGS-UHFFFAOYSA-N", "description": "A simplified peptide sequence designed de novo to fold into a coiled-coil conformation under ambient conditions but to transform into amyloid fibrils at elevated temperatures. The crystal structure of the coiled-coil form was determined and molecular model for the peptide in its fibrillar state was proposed. The relative stabilities of the two structural forms and the kinetics of their interconversion were found to be highly sensitive to small sequence changes."}