Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine
mutase (PAGM)

Chemical shift reference of 1H was based on the proton of water (4.784ppm at
298K) and then those of 15N and 13C were calculated based on their gyromagnetic
ratios.

Solution Structure Of The C-Terminal Domain Of Mouse Phosphoacetylglucosamine Mutase (Pagm)

phosphoglucomutase 3, isoform CRA_a [Mus musculus]

phosphoacetylglucosamine mutase isoform 1 [Mus musculus]

PREDICTED: phosphoacetylglucosamine mutase isoform X1 [Mus musculus]

RecName: Full=Phosphoacetylglucosamine mutase; Short=PAGM; AltName: Full=Acetylglucosamine phosphomutase; AltName: Full=N-acety

1mM C-terminal domain of Phosphoacetylglucosamine mutase(PAGM) U-15N, {13C;}
20mM Phosphate Buffer {Na;} 300mM {NaCl;} 1mM {d-DTT;} 0.02% {NaN3;} 10% D2O

C-terminal domain of Phosphoacetylglucosamine mutase(PAGM)

RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax