The residue-specific C-13' CSA tensor principal components, sigma(11), sigma(22), sigma(33), and the tensor orientation defined by the rotation angles beta and gamma have been determined by solution NMR for uniformly labeled ubiquitin partially aligned in four different media. Spurious chemical shift deviations due to solvent effects were corrected with an offset calculated by linear regression of the residual dipolar couplings and chemical shifts at increasing alignment strengths. Analysis of this effect revealed no obvious correlation to solvent exposure. Data obtained in solution from a protein offer a better sampling of C-13' CSA for different amino acid types in a complex heterogeneous environment, thereby allowing for the evaluation of structural variables that would be challenging to achieve by other methods. The C-13' CSA principal components cluster about the average values previously determined, and experimental correlations observed between sigma(11), sigma(22) tensorial components and C'O center dot center dot center dot H-N hydrogen bonding are discussed. The inverse association of sigma(11) and sigma(22) exemplify the calculated and solid-state NMR observed effect on the tensor components by hydrogen bonding. We also show that C-13' CSA tensors are sensitive to hydrogen-bond length but not hydrogen-bond angle. This differentiation was previously unavailable. Similarly, hydrogen bonding to the conjugated NH of the same peptide plane has no detectable effect. Importantly, the observed weak correlations signify the presence of confounding influences such as nearest-neighbor effects, side-chain conformation, electrostatics, and other long-range factors to the C-13' CSA tensor. These analyses hold future potential for exploration provided that more accurate data from a larger number of proteins and alignments become available.