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Article Abstract
We report the NMR resonance assignments of N-terminal signal sequence deleted secretory protein Rv0603 (∆-Rv0603) from Mycobacterium tuberculosis H37Rv. ∆-Rv0603 displayed good peak yield and signal dispersion in 2D [N-H] HSQC spectrum, which prompted us to proceed for resonance assignments on this construct. Standard triple-resonance experiments for resonance assignments were recorded on [U-N]-∆Rv0603 and [U-N, C]-∆Rv0603 samples. We obtained 97% of backbone H, 98% of C, 98% of H, 96% of C´, 100% of C, 100% of H and 98% of side-chain H 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.
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