Determination of the residue-specific 15N CSA tensor principal components using multiple alignment media

The individual components of the backbone N-15 CSA tensor, sigma(11), sigma(22), sigma(33), and the orientation of sigma(11) relative to the NH bond described by the angle beta have been determined for uniformly labeled N-15, C-13 ubiquitin from partial alignment in phospholipid bicelles, Pf1 phage, and poly(ethylene glycol) by measuring the residue-specific residual dipolar couplings and chemical shift deviations. No strong correlation between any of the CSA tensor components is observed with any single structural feature. However, the experimentally determined tensor components agree with the previously determined average CSA principal components [Cornilescu and Bax (2000) J. Am. Chem. Soc. 122, 10143-10154]. Significant deviations from the averages coincide with residues in beta-strand or extended regions, while alpha-helical residue tensor components cluster close to the average values.