Sequence-Specific Assignments in the¹H NMR Spectrum of the Human Inflammatory Protein C5a

Full sequence-specific assignments for the¹H 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 Wiithrich et. al. [Wuthrich, 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.