Solid-state NMR sequential assignments of the N-terminal domain of HpDnaB helicase

We present solid-state NMR assignments of the N-terminal domain of the DnaB helicase from Helicobacter pylori (153 residues) in its microcrystalline form. We use a sequential resonance assignment strategy based on three-dimensional NMR experiments. The resonance assignments obtained are compared with automated resonance assignments computed with the ssFLYA algorithm. An analysis of the C-13 secondary chemical shifts determines the position of the secondary structure elements in this alpha-helical protein.