1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli.
Haupt
Melina
M
Coles
Murray
M
Truffault
Vincent
V
Bramkamp
Marc
M
Altendorf
Karlheinz
K
Kessler
Horst
H
D000251:Adenosine Triphosphatases / Q000737:chemistry*; D000255:Adenosine Triphosphate / Q000737:chemistry; D001665:Binding Sites; D002247:Carbon Isotopes; D027682:Cation Transport Proteins / Q000737:chemistry*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry*; D006859:Hydrogen; D006868:Hydrolysis; D007477:Ions; D009682:Magnetic Resonance Spectroscopy; D009587:Nitrogen Isotopes; D010766:Phosphorylation; D017434:Protein Structure, Tertiary; D011522:Protons; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry
D002247:Carbon Isotopes; D027682:Cation Transport Proteins; D029968:Escherichia coli Proteins; D007477:Ions; D009587:Nitrogen Isotopes; D011522:Protons; D006859:Hydrogen; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; C058166:potassium translocating Kdp-ATPase, E coli; D000254:Sodium-Potassium-Exchanging ATPase