NMR analysis of the homodimeric structure of a D-Ala-D-Ala metallopeptidase, VanX, from vancomycin-resistant bacteria

There is one zinc ion attached to each subunit.
The active site of VanX coordinates the zinc ion (Zn2+) through His116, Asp123, Glu181, and His184.

Unlike the sequence for this crystal structure, our sequence contains C78S and C157S double mutations.

NmrPipe was used to process the data. The command "bruker" automatically calibrated the references.
In other words, the water 1H peak at 303K was assumed to be at 4.725 ppm.
For the 13C and 15N references, the nmrPipe command 'bruker' was also used for calibration in the same way.

Protein science : a publication of the Protein Society
Analysis of the homodimeric structure of a D-Ala-D-Ala metallopeptidase, VanX, from vancomycin-resistant bacteria.

The sequence GPGMGGSG corresponds to the peptide that remains in the N-terminus after cleavage of the (His)6 tag with HRV3C.
The residual number 1 starts with the Met in the subsequent sequence MEIGF.

For both pH 4 and pH 7 assignments, the 1H/15N chemical shift values of the amide groups registered are from the TROSY peaks.

Bruker BioSpin Avance III HD spectrometer

50 mM potassium phosphate buffer (pH 7.0) containing 30 uM ZnCl2

20 mM sodium acetate buffer (pH 4.0) containing 30 uM ZnCl2