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1 H-detected solid-state NMR experiments feasible at fast magic-angle spinning (MAS) frequencies allow accessing  1 H chemical shifts of proteins in solids, which enables their interpretation in terms of secondary structure. Here we present  1 H and  13 C-detected NMR spectra of the RNA polymerase subunit Rpo7 in complex with unlabeled Rpo4 and use the  13 C,  15 N, and  1 H chemical-shift values deduced from them to study the secondary structure of the protein in comparison to a known crystal structure. We applied the automated resonance assignment approach FLYA including  1 H-detected solid-state NMR spectra and show its success in comparison to manual spectral assignment. Our results show that reasonably reliable secondary-structure information can be obtained from  1 H secondary chemical shifts (SCS) alone by using the sum of  1 H α  and  1 H N  SCS rather than by TALOS. The confidence, especially at the boundaries of the observed secondary structure elements, is found to increase when evaluating  13 C chemical shifts, here either by using TALOS or in terms of  13 C SCS.

Including Protons in Solid-State NMR Resonance Assignment and Secondary Structure Analysis: The Example of RNA Polymerase II Subunits Rpo4/7