A single polypeptide chain which is organised into 2 domains that are connected by a flexible 20 amino acid linker.

The full length protein is an electroneutral antiporter for K+ and H+ ions across the inner membrane.

Biochimica et biophysica acta. Biomembranes
Solution structure of the cytoplasmic domain of NhaP2 a K+/H+ antiporter from Vibrio cholera.

Cytoplasmic tail of NhaP2 a K+/H+ antiporter from Vibrio cholera
Sequence corresponds to the 158 amino acid fragment consisting of T397 to R555 (the full length NhaP2 protein is 581 amino acid residues) plus an additional 6 residues (ENLYFQ) at the C-terminal end of the molecule which are the remnants of the TEV protease cleavage site after TEV treatment to remove the His6-tag. The 165th and final residue is the initiating Methionine that is required for the bacterial over-expression of the protein and which preceeds the first residue T2 observed in the NMR structure. The 158 amino acid fragment corresponds to the predicted RCK and TrkA-like domains found in the cytoplasmic tail of the NhaP2 K+/H+ antiporter.

Protein structure corresponding to a 165 amino acid fragment of the C-terminal tail for the NhaP2 K+/H+ antiporter from Vibrio cholera

Bruker Avance III HD NMR spectrometer equipped with a triple-resonance cryoprobe.

Bruker Avance III NMR spectrometer with a 5 mm, triple axis XYZ gradient TCI H&F-C/N-D CryoProbe

Varian Inova 600 MHz NMR spectrometer equipped with a triple-resonance probe.

Buffer used for NMR experiments contained 20 mM MES-NaOH pH 6.5, 150 mM NaCl, 5 mM TCEP, 0.1 mM AEBSF (4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride) and 0.02% sodium azide

AEBSF (4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride)

NMR measurements were made in a buffer containing 20 mM MES-NaOH pH 6.5, 0.15 M NaCl, 5 mM TCEP, 0.1 mM AEBSF (4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride) and 0.02% sodium azide at 300degK supplemented with 7 % (v/v) deuterium oxide and 5 uM DSS (4,4-dimethyl-4-silapentane-1-sulfonic acid) and sealed under argon.

NMR measurements were made in a buffer prepared in 100 % (v/v) deuterium oxide containing 20 mM MES-NaOH pH 6.5, 0.15 M NaCl, 5 mM TCEP, 0.1 mM AEBSF (4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride) and 0.02% sodium azide at 300degK supplemented with 5 uM DSS (4,4-dimethyl-4-silapentane-1-sulfonic acid) and sealed under argon.

NMR measurements were made in a buffer containing 20 mM MES-NaOH pH 6.5, 150 mM NaCl, 5 mM TCEP, 0.1 mM AEBSF (4-(2-aminoethyl) benzenesulfonyl fluoride hydrochloride) and 0.02% sodium azide at 300degK supplemented with supplemented with 7 % (v/v) deuterium oxide and 5 uM DSS (4,4-dimethyl-4-silapentane-1-sulfonic acid) and sealed under argon.

NMRPipe: a multidimensional spectral processing system based on UNIX pipes.

NMRFAM-SPARKY: enhanced software for biomolecular NMR spectroscopy.

TALOS-N: Prediction of Protein Backbone and Sidechain Torsion Angles from NMR Chemical Shifts

Integrative NMR for biomolecular research

Backbone and sidechain Torsion Angles prediction

National Magnetics Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, WI

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0520, USA.

National Magnetics Resonance Facility at Madison, Biochemistry Department, University of Wisconsin-Madison, Madison, WI 53706, USA.