Two-dimensional super(1)H NMR studies on HPr protein from Staphylococcus aureus): Complete sequential assignments and secondary structure

Complete sequence-specific assignments of the super(1)H NMR spectrum of HPr protein from Staphylococcus aureus) were obtained by two-dimensional NMR methods. Important secondary structure elements that can be derived from the observed nuclear Overhauser effects are a large antiparallel beta -pleated sheet consisting of four strands, A, B, C, D, a segment S sub(AB) consisting of an extended region around the active-center histidine (His-15) and an alpha -helix, a half-turn between strands B and C, a segment S sub(CD) which shows no typical secondary structure, and the alpha -helical, C-terminal segment S sub(term).