1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus.
CdnL, a 164-residue protein essential for Myxococcus xanthus viability, is a member of a large family of bacterial proteins of unknown structure and function. Here, we report the (1)H, (13)C and (15)N backbone and side chain assignments for the stable C-terminal domain of CdnL identified by limited proteolysis.
Mirassou
Yasmina
Y
Instituto de Química Física Rocasolano, CSIC, 28006, Madrid, Spain.
García-Moreno
Diana
D
Santiveri
Clara M
CM
Santoro
Jorge
J
Elías-Arnanz
Montserrat
M
Padmanabhan
S
S
Jiménez
M Angeles
MA
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D002247:Carbon Isotopes / Q000737:chemistry; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D008969:Molecular Sequence Data; D016941:Myxococcus xanthus / Q000737:chemistry*; D009587:Nitrogen Isotopes / Q000737:chemistry; D017434:Protein Structure, Tertiary; D011522:Protons
D001426:Bacterial Proteins; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D011522:Protons