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Solid state 31P n.m.r. data concerning the structure of the RNA in TMV are presented in light of the prior diffraction and model building results on this system (Stubbs et al., 1977; Stubbs & Stauffacher, 1981). The 31P chemical shift anisotropy powder pattern of a stationary, unoriented solution of TMV shows the RNA to be immobilized by the coat protein-RNA interactions, since the principal values (sigma 11 = 83, sigma 22 = 25, sigma 33 = -108 p.p.m. relative to external 85% H3PO4) are essentially the same as those of a static phosphodiester group. There are three peaks in the isotropic 31P n.m.r. spectrum obtained with magic angle sample spinning, indicating three distinct phosphate environments. There are three peaks in the 31P n.m.r. spectrum from an oriented TMV solution, indicating three distinct phosphate orientations.