Complete (15)N and (1)H NMR Assignments for the Amino-Terminal Domain of the Phage 434 Repressor in the Urea-Unfolded Form

The amino-terminal DNA-binding domain consisting of residues 1-69 of the phage 434 repressor in the urea-unfolded form was examined. The findings suggest that for most amino acid residues, the 1H chemical shifts of the urea-unfolded protein are very similar to the random coil values; however, some discrete regions of the polypeptide chain were identified that are likely to retain residual nonrandom spatial structure.