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1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7.

作者信息

Phelan Marie M, Thai Chuong-Thu, Herbert Andrew P, Bella Juraj, Uhrín Dusan, Ogata Ronald T, Barlow Paul N, Bramham Janice

机构信息

Edinburgh Biomolecular NMR Unit, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, Scotland, UK.

出版信息

Biomol NMR Assign. 2009 Jun;3(1):49-52. doi: 10.1007/s12104-008-9139-z. Epub 2009 Jan 13.

Abstract

The carboxy terminus of human complement component C7 comprises two Factor I-like Modules (FIMs) which are essential for formation of the Membrane Attack Complex, the terminal pathway of the innate immune system. C7-FIMs is a 16.9 kDa, recombinant, disulphide-rich, protein encompassing this C-terminal domain. Using conventional triple resonance experiments 93% of the (1)H, (15)N and (13)C assignment has been achieved, accounting for all assignment apart from a flexible N-terminus cloning artefact and an undefined loop. The chemical shifts have been deposited in the BioMagResBank; Accession No. 15996.

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