A combination of solid state H-1 NMR chemical shift measurements and empirical chemical shift calculations has been used to interpret H-1 solid state chemical shifts of a model peptide (Ala-Gly)(15) for the crystalline domain of Bombyx mori silk fibroin in silk I and silk II structures, including a treatment of both intra- and intermolecular arrangements. Silk I and silk II are the structures of silk fibroin before and after spinning, respectively. Two peaks with equal intensity were observed for the amide protons of (AG)(15) in silk I, whereas only one broad peak was observed for silk II, reflecting a difference of 1.1 ppm in Ala H-N shift between silk I and silk II, but a difference of only 0.2 ppm in Gly H-N shift. Chemical shift calculations predicted chemical shifts that are in good agreement with the experimental observations and showed that the origin of these chemical shift differences was predominantly the magnetic anisotropy effect from the C=O bond that hydrogen bonds with H-N, which has a more favorable geometry for Ala H-N in silk II than for the other H-N. This result shows that We Could distinguish between proton chemical shift effects arising from intermolecular interactions and those from intramolecular interactions by combining observation of the solid state H-1 NMR chemical shift and empirical chemical shift calculation.