1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7.
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.
Phelan
Marie M
MM
Edinburgh Biomolecular NMR Unit, Joseph Black Building, University of Edinburgh, West Mains Road, Edinburgh, EH9 3JJ, Scotland, UK. marie.phelan@ed.ac.uk
Thai
Chuong-Thu
CT
Herbert
Andrew P
AP
Bella
Juraj
J
Uhrín
Dusan
D
Ogata
Ronald T
RT
Barlow
Paul N
PN
Bramham
Janice
J
D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D003184:Complement C7 / Q000737:chemistry* / Q000648:ultrastructure*; D005340:Fibrinogen / Q000737:chemistry* / Q000648:ultrastructure*; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D011522:Protons
D002247:Carbon Isotopes; D003184:Complement C7; D009587:Nitrogen Isotopes; D011522:Protons; D005340:Fibrinogen