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-0006,1BA6,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 ,GLYCOPROTEIN,SOLUTION NMR,,,"APP, A4, AD1",,chain-ID A: DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV,P05067,AMYLOID BETA-PEPTIDE,SOLUTION STRUCTURE OF THE METHIONINE-OXIDIZED AMYLOID BETA-PEPTIDE (1-40),Biochemistry. 1998 Sep 15;37(37):12700-6,"Watson, A.A., Fairlie, D.P., Craik, D.J.",9737846,DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV#CCCCCCCSSSSCSCHHHHHHHHHHHTCSTTTTTSCSSCCC,"The solution structure of ABeta(1-40)Met(O), the methionine-oxidized form of ABeta(1-40), has been investigated. Oxidation of Met35 may have implications in the aetiology of Alzheimer's disease. Experiments strongly suggest the presence of a helical region between residues 16 and 24 in ABeta(1-40)Met(O). Oxidation of Met35 causes a local and selective disruption of helix 2. In addition to this helix-coil rearrangement in aqueous micelles, the CD data show that oxidation inhibits a coil-to-Beta-sheet transition in water.",A,SME,C5 H11 N O3 S,165.21,METHIONINE SULFOXIDE,C[S@@](=O)CC[C@@H](C(=O)O)N,"InChI=1S/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-,10+/m0/s1",QEFRNWWLZKMPFJ-ZXPFJRLXSA-N,"SME:A:C5 H11 N O3 S:165.21:METHIONINE SULFOXIDE:C[S@@](=O)CC[C@@H](C(=O)O)N:InChI=1S/C5H11NO3S/c1-10(9)3-2-4(6)5(7)8/h4H,2-3,6H2,1H3,(H,7,8)/t4-,10+/m0/s1:QEFRNWWLZKMPFJ-ZXPFJRLXSA-N"