Backbone chemical shift assignments of the LexA catalytic domain in its active conformation

J Biomol NMR. 2005 Apr;31(4):371-2. doi: 10.1007/s10858-005-0944-8.
No abstract available

Publication types

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

MeSH terms

  • Bacterial Proteins / chemistry*
  • Carbon Isotopes
  • Catalytic Domain
  • Crystallography, X-Ray
  • Dimerization
  • Escherichia coli / metabolism
  • Hydrogen
  • Magnetic Resonance Spectroscopy
  • Molecular Conformation
  • Mutation
  • Nitrogen Isotopes
  • Nuclear Magnetic Resonance, Biomolecular / methods*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary
  • Rec A Recombinases / chemistry
  • Serine Endopeptidases / chemistry*

Substances

  • Bacterial Proteins
  • Carbon Isotopes
  • LexA protein, Bacteria
  • Nitrogen Isotopes
  • Hydrogen
  • Rec A Recombinases
  • Serine Endopeptidases