Backbone and side-chains 1H, 13C and 15N NMR assignment of human beta-parvalbumin

beta-parvalbumin, also known as oncomodulin, is a small Ca2+-binding protein belonging to the so-called EF-hand family. At variance with the ubiquitary a-parvalbumin, the b-form is almost exclusively expressed in tumor cells. The solution structure of the recombinant human protein has been solved by us (Babini et al. 2004) mostly based on proton assignment. As this protein is a potential drug target, its full assignment may be of general interest per se.We present here its virtually complete assignment, obtained with the aid of 13C- direct detection 2D experiments, including a novel pulse sequence designed for the assignment of aromatic Cc nuclei (see Supplementary material). All backbone resonances are assigned except for the HN and N of M1. Still unassigned are the N terminal in Lys residues, the ring NH and N signals of H108, and the guanidine signals of R20 and R49. In summary, 93.7% 1H, 99.4% 13C and 89.8% 15N of the total protein nuclei were assigned.