Resonance assignments and secondary structure prediction of secretory protein Rv0603 from Mycobacterium tuberculosis H37Rv

We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆_1-28-Rv0603) from Mycobacterium tuberculosis H37Rv. ∆_1-28-Rv0603 displayed good peak yield and signal dispersion in 2D [¹⁵N-¹H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [U-¹⁵N]-∆Rv0603 and [U-¹⁵N, ¹³C]-∆Rv0603 samples. We obtained 97% of backbone ¹H^N, 98% of ¹³C^α, 98% of ¹H^α, 96% of ¹³C´, 100% of ¹³C^β, 100% of ¹H^β and 98% of side-chain ¹H chemical shifts. This protein does not show any sequence similarity to any other protein of known structure. Determination of its solution structure would facilitate understanding of its biological function.