The magnitudes and orientations of the principal elements of the N-15 chemical shift and H-1-N-15 dipolar coupling interaction tensors pertaining to the glycine residue in N-15-acetyl glycine (NAG) and [N-15-Gly]collagen were determined by the analysis of one-dimensional dipolar chemical shift powder patterns. A one-dimensional H-1-N-15 dipolar N-15 chemical shift spectrum was obtained on a [N-15-Gly]collagen fiber sample with the fiber axis oriented parallel to the external magnetic field. The dipolar chemical shift spectrum enabled the orientation of the peptide plane to be determined relative to the direction of the applied magnetic field or the triple-helix axis of the collagen fiber. The magnitudes of the principal elements of the tensors and their orientations in the molecular frame for these two sites are quite different. The magnitudes of the chemical shift tensors are 42.3, 67, and 223.4 ppm for [N-15-Gly]collagen and 37, 82.8, and 220.4 ppm for NAG. The angle CON) between the least shielded N-15 chemical shift tensor element, sigma(33N), and the N-H bond is 24.5 degrees for [N-15-Gly]collagen and 25.5 degrees (or 154.5 degrees) for NAG. The angle (alpha(N)) between the most shielded N-15 chemical shift tensor element, sigma(11N), and the projection of the N-H bond on the (sigma(11N)-sigma(22N) plane is 145 degrees for [N-15-Gly]collagen and 25 degrees (or 155 degrees, 205 degrees, or 335 degrees) for NAG. Because of the identical dipolar chemical shift powder patterns for four different alpha(N) values (35 degrees, 145 degrees, 215 degrees, and 325 degrees) the correct value of the alpha(N) angle was determined as 145 degrees using the dipolar chemical shift spectrum of the oriented [N-15-Gly]collagen sample.