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-0008,1BJC,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,28,K16F,Amyloid,Peptide,Monomer - A ,GLYCOPROTEIN,SOLUTION NMR,,,"APP, A4, AD1",,chain-ID A: DAEFRHDSGYEVHHQFLVFFAEDVGSNK,P05067,AMYLOID BETA-PEPTIDE,SOLUTION NMR STRUCTURE OF AMYLOID BETA[F16],J Struct Biol. 2000 Jun;130(2-3):142-52,"Poulsen, S.-A., Watson, A.A., Craik, D.J.",10940222,DAEFRHDSGYEVHHQFLVFFAEDVGSNK#CCTTTTCCCCCCCCTTHHHHHHHHSTTC,The structural effects of these mutations of a positively charged residue to hydrophobic residues at the Alpha-secretase cleavage site (Lys16-Leu17) were examined in the membrane-simulating solvent aqueous SDS micelles. Overall the three-dimensional structures were similar to that for the native ABeta(1-28) sequence in that they contained an unstructured N-terminus and a helical C-terminus. the K16F mutation shortened the helix to between residues 16 and 24.,,,,,,,,,