{Reference Type}: Journal Article
{Title}: Solid-state NMR chemical shift assignments of aquaporin Z in lipid bilayers.
{Author}: Xie H;Zhao Y;Wang J;Zhang Z;Yang J;
{Journal}: Biomol NMR Assign
{Volume}: 12
{Issue}: 2
{Year}: 10 2018
{Factor}: 0.731
{DOI}: 10.1007/s12104-018-9832-5
{Abstract}: Aquaporin Z is the first identified prokaryotic water channel in Escherichia coli with a high water permeability and strict substrate selectivity. Here we report nearly complete (94% of amino acid residues) 13C and 15N chemical shift assignments of AqpZ reconstituted in the lipid bilayers using a set of 2D and 3D magic angle spinning solid-state NMR spectra. Secondary structure of AqpZ predicted from chemical shift assignments is generally similar to that of X-ray structure with a number of differences in loop and near-loop regions. The BMRB accession number of the assignments is 27244.