Fig. 1.

Solid-state NMR dipolar order parameters for the (¹³C¹H)α (black; filled circles) and (¹³C¹H₂)α (red; open circles) spin systems in uniformly labeled Pf1 coat protein. The primary sequence (3) is shown for convenience. Order parameters are calculated from the motionally narrowed dipolar coupling by using Eq. 1. Black lines connect order parameters for contiguous residues in primary sequence. The dotted reference line delineates the static limit (order parameter of 1.0). Order parameters of 1.0 represent sites that are completely static and order parameters of 0.0 represent sites with isotropic motion on a submicrosecond time scale. The Cα sites are mostly static, and Gly-1 is the most dynamic site with an order parameter of 0.38 ± 0.03, which corresponds to a diffusion in a cone angle of 59.3° (36).