Backbone resonance assignments for the rat GMEB-2 SAND domain

full-length protein activates parvovirus nickase NS1 protein

The first three N-terminal residues, GAM, were not derived from GMEB2 but from
the linker resulting from cleavage of the N-terminal Histag. The backbone NH/N
HSQC cross-peak signal for some the N-terminal G residue was not observed in
the NMR spectra.

Information obtained from PDB's Chemical Component Dictionary
at http://wwpdb-remediation.rutgers.edu/downloads.html
Downloaded on Thu Jun 2 09:48:05 2011

1H, 13C and 15N backbone resonance assignments of the SAND domains from glucocorticoid modulatory element binding proteins-1 and -2.

There is a tripeptide N-terminal tag (GAM) followed by 98 residues of the rat
GMEB-2 protein, residues Glu 81 to Lys 178. Theoretical pI=8.33.
The protein sequence given should be numbered according to its occurrence in
the wild-type protein. Thus the first residue (G) should be numbered 78, and
the last residue (K) 178. Nevertheless, it should be noted that the first three
residues (GAM) are derived from an N-terminal tag.
The protein studied was produced from the rat GMEB2 gene, cloned from a rat
cDNA library. The corresponding GenBank code is AF059273. The protein
numbering, spanning rat GMEB2 residues E81-K178) is according to the wild-type
rat protein. Note, however, that for this GMEB2 construct, the corresponding
region in the HUMAN GMEB2 protein has an identical amino acid sequence. The
human GMEB protein is under GenBank code NM_012384, and the SAND domain therein
spans residues E82-K179.

Protein was expressed from an in-house modified pET-24d vector (originally
supplied by NOVAGEN) in E. coli induced with IPTG at 23 degrees C for 16
hours.

Samples were also stored under either nitrogen or argon gas in order to limit
oxidation of the numerous Cys residues (important in zinc-binding).