{"resolution": "2.32", "ligand_mw": "", "secondary_structure": "EVHHQKLVFFAEDVG#CCCCCCCCCSTTCCC&EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYGMSWVRQAPGKGLELVASINSNGGSTYYPDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCASGDYWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT#CCEEEEECCEEECTTCCEEEEEEEESSCGGGSCEEEEEECTTCCCEEEEEECSSSCCEECCTTTBTTEEEEEETTTTEEEEEECSCCGGGCEEEEEECSSCBCCCEEEEECCCCCBCCEEEEECCCCCCCCCCEEEEEEEEEEEBSSCCEEEEGGGTBCTTEEECCCEECTTSCEEEEEEEEEEGGGTTTSCCEEEEEEGGGTEEEEEECCCCCCCCCCC&DIVMTQSPLSLPVTPGEPASISCRSSQSLVYSNGDTYLHWYLQKPGQSPQLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCSQSTHVPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC#CCCEEEECSEEEECTTSCEEEEEEESSCCBCTTSCBCEEEEEECSSSCCEEEEETTTEECTTCCTTEEEEEETTEEEEEESSCCGGGCEEEEEEECSSSSCEECCCEEEEECCCCBCCEEEEECCCHHHHHTTEEEEEEEEEEEBSSCCEEEEEETTEECCSSEEEEECCCCTTTCCEEEEEEEEEEHHHHHTCCEEEEEEECTTCSSCEEEEEETTCC", "inchi": "", "method": "X-RAY DIFFRACTION", "ec_number": "", "uniprot_ac": "", "remarks": "Crystal structure of crenezumab Fab in complex with Abeta", "description": "To understand the structural basis for this binding profile and activity, they determined the crystal structure of crenezumab in complex with ABeta. The structure reveals a sequential epitope and conformational requirements for epitope recognition, which include a subtle but critical element that is likely the basis for crenezumab's versatile binding profile. They find interactions consistent with high affinity for multiple forms of ABeta, particularly oligomers. Of note, crenezumab also sequesters the hydrophobic core of ABeta and breaks an essential salt-bridge characteristic of the Beta-hairpin conformation, eliminating features characteristic of the basic organization in ABeta oligomers and fibrils, and explains crenezumab's inhibition of aggregation and promotion of disaggregation.", "type": "Inhibitor complex", "ligand_smiles": "", "chain_id": "", "species": "", "keyword": "", "ligstr": "", "pmid": "27996029", "mutation_s_field": "No", "author": "Ultsch, M., Li, B., Maurer, T., Mathieu, M., Adolfsson, O., Muhs, A., Pfeifer, A., Pihlgren, M., Bainbridge, T.W., Reichelt, M., Ernst, J.A., Eigenbrot, C., Fuh, G., Atwal, J.K., Watts, R.J., Wang, W.", "pdb_id": "5VZY", "amyloid_non_amyloid": "Non-amyloid", "inchi_key": "", "ligand_name": "", "ligand_formula": "", "ligand_id": "", "r_value_free": "0.249", "protein_name": "Amyloid-beta", "gene_names": "APP, A4, AD1", "global_stoichiometry": "Homo 2-mer -A2", "alternative_name": "ABPP, APPI, Alzheimer disease amyloid protein, Amyloid precursor protein, Amyloid-beta precursor protein, Cerebral vascular amyloid peptide, PreA4, Protease nexin-II", "peptide_protein_sequence": "chain-ID A: EVHHQKLVFFAEDVG; chain-ID H: EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYGMSWVRQAPGKGLELVASINSNGGSTYYPDSVKGRFTISRDNAKNSLYLQMNSLRAEDTAVYYCASGDYWGQGTTVTVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT; chain-ID L: DIVMTQSPLSLPVTPGEPASISCRSSQSLVYSNGDTYLHWYLQKPGQSPQLLIYKVSNRFSGVPDRFSGSGSGTDFTLKISRVEAEDVGVYYCSQSTHVPWTFGQGTKVEIKRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC", "pdb_classification": "IMMUNE SYSTEM", "reference": "Sci Rep. 2016 Dec 20;6:39374.", "length": "15 ,  220 ,  219", "entry": "S-0478"}