{"global_stoichiometry": "Hetero 3-mer - ABC ", "ligstr": "", "uniprot_ac": "", "inchi": "", "reference": "Proteins. 2013 Oct;81(10):1748-58.", "author": "Nisbet, R.M., Nuttall, S.D., Robert, R., Caine, J.M., Dolezal, O., Hattarki, M., Pearce, L.A., Davydova, N., Masters, C.L., Varghese, J.N., Streltsov, V.A.", "type": "Inhibitor complex", "ligand_id": "", "species": "", "method": "X-RAY DIFFRACTION", "keyword": "", "gene_names": "imm, ceiE7 & Ighg & Ighg & Igkc, Igk-C & Igkc, Igk-C", "chain_id": "", "ligand_mw": "", "inchi_key": "", "secondary_structure": "DAEFRHDSGYEVHHQKSELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQGAAADYKDDDDKAADYKDDDDK#CCCCCCCCCSSSSSCCCCCCSCGGGCCHHHHHHHHHHHHTTTSSSCSSSHHHHHHHHHHHHCCSSTTHHHHSCCSSSCCSSHHHHHHHHHHHHHSSCCCCCCCCCCCCCCCCCCCCCCCCCCCC&DAEFRHDSGYEVHHQKSELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQGAAADYKDDDDKAADYKDDDDK#CCCCCCCCCSSSSSCCCCCCSSGGGSBHHHHHHHHHHHHHSSSSSCSSSSHHHHHHHHHHTCCSCHHHHHHSCCTTSCCSSHHHHHHHHHHHHHHTCCCCBCCCCCCCCCCCCCCCCCCCCCCC&QVTLKESGPGILQPSQTLSLTCSFSGFSLRTSRVGVSWIRQPSGKGLEWLAHIYWDDDKRYNPSLESRLTISKDTSRNQVFLKITSVDTADTATYYCARRGFYGRKYEVNHFDYWGQGTTLTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSESITCNVAHPASSTKVDKKIVPRDCG#CCEECCBCCCEECTTSCCCEECCEESSCSTTSCCEEEEEEECSSCCCEEEEEECTTCCEEECTTTCTTCCEEEETTTTEEEECCCSCCGGGCSEEEEEEEECCSSCGGGCEEEEECCCCBCEECSSCCBCCCCCBCCCCSCSSCCSCEECCEEEESCBSSCCCBCCSTTCCCSCCCCEEEEESSSSEEEEECCEESSCSSSSSCCCCCBCCTTTCCCCCCCCCCCCCC&QVTLKESGPGILQPSQTLSLTCSFSGFSLRTSRVGVSWIRQPSGKGLEWLAHIYWDDDKRYNPSLESRLTISKDTSRNQVFLKITSVDTADTATYYCARRGFYGRKYEVNHFDYWGQGTTLTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSESITCNVAHPASSTKVDKKIVPRDCG#CCCEEEECCSEECSSSEEEEEEEECSSCSSSCCCEEEEEEECTTSCCEEEEEECSSSCBCCCTTTSSSEECCEETTTTEEEEEEESCCGGGCEEEEEEEEBCSSSCTTCCBCCCBCCCEEEEECCCCCBCCEEEEECCCSSSCCCSSEEEEEEEESBBSSCCCCCCSTTCCCCCCEECCCEEETTEEECEEEEEESSSSTTTSCCCBCCCCTTTCCCCCBCCCCCCCC&DIVMTQTPLSLPVSLGDQASISCRSSQTILHSNGNTYLEWYLQKPGQSPNLLIYKVSKRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSRVPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC#CCCEECSCSEEECCTTSCEEEECEESSCCCCTTSCCCCCEEECCTTSCCCCCBCTTTCCCTTCCTTEEEEECSSCEEEEESSCCSSSCEEEEECCSSSSSCBCCCCEEEECCCCCBCCCCCEECCCTTHHHHCCEEEEEEECSCBSCCCEEECCBCSSCCSCCCBCCBCCCCTTTCCCCEEEEEEECTTTSSSCCBCCCEEECTTCSSCBCCCCCSCCC&DIVMTQTPLSLPVSLGDQASISCRSSQTILHSNGNTYLEWYLQKPGQSPNLLIYKVSKRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSRVPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC#CCCEEEECSCCEECTTCCEEEEEEESSCCCCTTSCCCEEEEEECTTSCCCEEEETTTEECTTCCTTCCCCEETTEEEEEESSCCTTTCEEEEEEECSSSSCCBCCCEEEEECCCCBCCEEECCCCCGGGTTTTCEEECCEEEEEBSSCCCCCCCCSSSCCSSSCBCCEECCCTTTCCEEEECBEEECTTHHHHCCCCCCCCCCSSCSSCCCCCCCCCCC", "amyloid_non_amyloid": "Non-amyloid", "length": "124 ,  228 ,  228 ,  219 ,  219", "remarks": "Structural studies of the tethered N-terminus of the Alzheimer's disease amyloid-beta peptide; Abeta1-16Im7-WO2 Fab (antibody)", "protein_name": "Amyloid-Beta", "peptide_protein_sequence": "chain-ID A: DAEFRHDSGYEVHHQKSELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQGAAADYKDDDDKAADYKDDDDK; chain-ID B: DAEFRHDSGYEVHHQKSELKNSISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKITEHPDGTDLIYYPSDNRDDSPEGIVKEIKEWRAANGKPGFKQGAAADYKDDDDKAADYKDDDDK; chain-ID F: QVTLKESGPGILQPSQTLSLTCSFSGFSLRTSRVGVSWIRQPSGKGLEWLAHIYWDDDKRYNPSLESRLTISKDTSRNQVFLKITSVDTADTATYYCARRGFYGRKYEVNHFDYWGQGTTLTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSESITCNVAHPASSTKVDKKIVPRDCG; chain-ID H: QVTLKESGPGILQPSQTLSLTCSFSGFSLRTSRVGVSWIRQPSGKGLEWLAHIYWDDDKRYNPSLESRLTISKDTSRNQVFLKITSVDTADTATYYCARRGFYGRKYEVNHFDYWGQGTTLTVSSAKTTAPSVYPLAPVCGDTTGSSVTLGCLVKGYFPEPVTLTWNSGSLSSGVHTFPAVLQSDLYTLSSSVTVTSSTWPSESITCNVAHPASSTKVDKKIVPRDCG; chain-ID K: DIVMTQTPLSLPVSLGDQASISCRSSQTILHSNGNTYLEWYLQKPGQSPNLLIYKVSKRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSRVPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC; chain-ID L: DIVMTQTPLSLPVSLGDQASISCRSSQTILHSNGNTYLEWYLQKPGQSPNLLIYKVSKRFSGVPDRFSGSGSGTDFTLKISRVEAEDLGVYYCFQGSRVPLTFGAGTKLELKRADAAPTVSIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC", "ligand_name": "", "ligand_smiles": "", "pdb_id": "4F37", "ec_number": "", "pdb_classification": "IMMUNE SYSTEM", "mutation_s_field": "No", "ligand_formula": "", "r_value_free": "0.26899999", "alternative_name": "ImmE7, Microcin-E7 immunity protein & Immunoglobulin heavy chain gamma polypeptide & Immunoglobulin heavy chain gamma polypeptide", "description": "A crystal structure of ABeta residues 1-16 fused to the N-terminus of the Escherichia coli immunity protein Im7, and stabilized with the fragment antigen binding fragment of the anti-ABeta N-terminal antibody WO2. The structure demonstrates that ABeta residues 10-16, which are not in complex with the antibody, adopt a mixture of local polyproline II-helix and turn type conformations, enhancing cooperativity between the two adjacent histidine residues His13 and His14. Furthermore, this relatively rigid region of ABeta (residues, 10-16) appear as an almost independent unit available for trapping metal ions and provides a rationale for the His13-metal-His14 coordination in the ABeta1-16 fragment implicated in ABeta metal binding.", "resolution": "2.57", "pmid": "23609990", "entry": "S-0320"}