(1)H, (13)C and           (15)N NMR backbone assignments of the 269-residue serine protease PB92 from Bacillus alcalophilus.
The (1)H, (13)C and (15)N NMR resonances of the backbone of serine protease PB92 have been assigned. This 269-residue protein is one of the largest monomeric proteins assigned so far. The amount and quality of information available suggest that even larger proteins could be assigned with present methods. Measured chemical shifts show excellent agreement with the secondary structure.
Department of Chemistry, Utrecht University, Padualaan 8, 3584 CH, Utrecht, The Netherlands.
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