We report the experimental determination of the C-13(alpha) chemical shift tensors of Ala, Leu, Val, Phe, and Met in a number of polycrystalline peptides with known X-ray or de novo solid-state NMR structures. The 700 Hz dipolar coupling between C-13(alpha) and its directly bonded N-14 permits extraction of both the magnitude and the orientation of the shielding tensor with respect to the C-alpha-N bond vector. The chemical shift anisotropy (CSA) is recoupled under magic-angle spinning using the SUPER technique (Liu et al., J. Magn. Reson. 2002, 155,15-28) to yield quasi-static chemical shift powder patterns. The tensor orientation is extracted from the C-13-N-14 dipolar modulation of the powder line shapes. The magnitudes and orientations of the experimental C-13(alpha) chemical shift tensors are found to be in good accord with those predicted from quantum chemical calculations. Using these principal values and orientations, supplemented with previously measured tensor orientations from C-13-N-15 and C-13-H-1 dipolar experiments, we are able to predict the (, psi, chi(1)) angles of Ala and Val within 5.8 degrees of the crystallographic values. This opens up a route to accurate determination of torsion angles in proteins based on shielding tensor magnitude and orientation information using labeled compounds, as well as the structure elucidation of noncrystalline organic compounds using natural abundance C-13(alpha) NMR techniques.