Complete 1 H, 13 C, 15 N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223–363)

Comprehensive resonance assignments and delineation of the secondary structure elements of the C-terminal Vpr-binding region of hHR23A, residues 223–363, were achieved by triple-resonance NMR experiments on uniformly 13 C, 15 N-labeled protein. Assignments are 100% and > 95% complete for backbone and side-chain resonances, respectively. This data constitutes important complementary information for our ongoing structure determination of the Vpr-hHR23A(223–363) complex. At high concentrations, severe line-broadening was observed for several residues in the 1 H– 15 N HSQC spectrum, most likely resulting from inter-molecular interactions.