¹H, ¹³C, and ¹⁵N backbone resonance assignments for KPC-2, a class A serine-β-lactamase

The ever-increasing occurrence of antibiotic resistance presents a major threat to public health. Specifically, resistance conferred by β-lactamases places the efficacy of currently available antibiotics at risk. Klebsiella pneumoniae carbapenemase-2 (KPC-2) is a β-lactamase that enables carbapenem resistance and represents a clear and present danger to global public health. In order to combat bacterial infections harboring KPC-2 expression, inhibitors with improved potency need to be developed. Although the structure of KPC-2 has been solved by X-ray crystallography, NMR provides the unique opportunity to study the structure and dynamics of flexible loop regions in solution. Here we report the ¹H, ¹³C, and ¹⁵N backbone chemical shift assignments for KPC-2 in the apo state as the first step towards the study of KPC-2 dynamics in the presence and absence of ligands to enable the rational design of optimized inhibitors.