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

4 N-terminal residues are vector-derived: G689, S690, H691 and M692.
The residues 5 to 155 correspond to residues 693 to 843 within the full length protein.
The protein has eighteen cysteines that are shown by mass spectrometry to form nine disulphide bonds.
The predicted disulphide bonding pattern has yet to be confirmed experimentally.

Nmr Solution Structure Of Factor I-Like Modules Of Complement C7

complement component 7 [synthetic construct]

complement protein C7 precursor [Homo sapiens]

complement component C7 precursor [Homo sapiens]

complement component C7 precursor [Pongo abelii]

PREDICTED: complement component C7-like [Macaca mulatta]

PREDICTED: complement component C7 [Pan troglodytes]

PREDICTED: complement component C7 isoform X1 [Pan paniscus]

RecName: Full=Complement component C7; Flags: Precursor

The C-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 1H, 15N and 13C assignment
has been achieved, accounting for all assignment apart from a flexible
N-terminus cloning artefact and an undefined loop.

Torrey Pines Institute for Molecular Studies

SIMULATED ANNEAILING, RESTRAINED MOLECULAR DYNAMICS