1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli

J Biomol NMR. 2004 Jul;29(3):437-8. doi: 10.1023/B:JNMR.0000032512.08757.8b.
No abstract available

Publication types

  • Letter
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / chemistry*
  • Adenosine Triphosphate / chemistry
  • Binding Sites
  • Carbon Isotopes
  • Cation Transport Proteins / chemistry*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry*
  • Hydrogen
  • Hydrolysis
  • Ions
  • Magnetic Resonance Spectroscopy
  • Nitrogen Isotopes
  • Phosphorylation
  • Protein Structure, Tertiary
  • Protons
  • Sodium-Potassium-Exchanging ATPase / chemistry

Substances

  • Carbon Isotopes
  • Cation Transport Proteins
  • Escherichia coli Proteins
  • Ions
  • Nitrogen Isotopes
  • Protons
  • Hydrogen
  • Adenosine Triphosphate
  • Adenosine Triphosphatases
  • potassium translocating Kdp-ATPase, E coli
  • Sodium-Potassium-Exchanging ATPase