entry,pdb_id,protein_name,alternative_name,species,length,mutation_s_field,amyloid_non_amyloid,type,global_stoichiometry,pdb_classification,method,resolution,r_value_free,gene_names,ec_number,peptide_protein_sequence,uniprot_ac,keyword,remarks,reference,author,pmid,secondary_structure,description,chain_id,ligand_id,ligand_formula,ligand_mw,ligand_name,ligand_smiles,inchi,inchi_key,ligstr S-0003,1AML,Amyloid-beta A4 protein,"ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II",Homo sapiens,40,No,Amyloid,Peptide,Monomer - A ,SERINE PROTEASE INHIBITOR,SOLUTION NMR,,,"APP, A4, AD1",,chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,P05067,AMYLOID A4,Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease,Eur J Biochem. 1995 Oct 1;233(1):293-8,"Sticht, H., Bayer, P., Willbold, D., Dames, S., Hilbich, C., Beyreuther, K., Frank, R.W., Rosch, P.",7588758,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCSSCCSSCCSSHHHHHHHHHHHSSSCCSSHHHHTTTTC,"One of the principle peptide components of the amyloid plaque deposits of Alzheimer's disease in humans is the 40-amino-acid peptide Beta-amyloid A4-(1-40)-peptide. Synthetic human A4-(1-40)-peptide was soluble and non-aggregating for several days in 40% (by vol). The main secondary-structure elements found were two helices, Gln15-Asp23 and Ile31-Met35, whereas the rest of the peptide was in random-coil conformation. A similar secondary structure is suggested for the aggregation part of prions.",,,,,,,,,