Sequence-specific assignments in the 1H NMR spectrum of the human inflammatory protein C5a.
Full sequence-specific assignments for the 1H NMR lines of the backbone protons of the human complement factor C5a are described and documented. The results were obtained by largely following the methodology developed by Wüthrich et al. [Wüthrich, K., Wider, G., Wagner, G., & Braun, W. (1982) J. Mol. Biol. 155, 311]. Assignments for the majority of the amino acid side chain protons were obtained by using a comparison of double- and triple-quantum-filtered two-dimensional correlated experiments together with the analysis of relayed coherence transfer spectra. The assignments provide the basis for the determination of the thus far unknown three-dimensional structure of C5a from nuclear Overhauser enhancement distance constraints.
Zuiderweg
E R
ER
Pharmaceutical Discovery, Abbott Laboratories, Abbott Park, Illinois 60064.
Mollison
K W
KW
Henkin
J
J
Carter
G W
GW
D000595:Amino Acid Sequence; D003182:Complement C5; D015936:Complement C5a; D006801:Humans; D006859:Hydrogen; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008969:Molecular Sequence Data; D011487:Protein Conformation
D003182:Complement C5; D006859:Hydrogen; D015936:Complement C5a