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.

中文翻译：

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结核分枝杆菌 H37Rv 分泌蛋白 Rv0603 的共振分配和二级结构预测。

我们报告了来自结核分枝杆菌H37Rv的 N 端信号序列缺失的分泌蛋白 Rv0603 (Δ _1–28 -Rv0603)的 NMR 共振分配。∆ _1–28 -Rv0603 在 2D [ ¹⁵ N- ¹ H] HSQC 光谱中显示出良好的峰产量和信号色散，这促使我们继续对该构造进行共振分配。在 [ U - ¹⁵ N]-ΔRv0603 和 [ U - ¹⁵ N, ¹³ C]-ΔRv0603 样品上记录了用于共振分配的标准三重共振实验。我们获得了 97% 的主链¹ H ^N，98% 的¹³ C^α、98% 的¹ H ^α、96% 的¹³ C´、100% 的¹³ C ^β、100% 的¹ H ^β和 98% 的侧链¹ H 化学位移。该蛋白质与已知结构的任何其他蛋白质没有任何序列相似性。确定其溶液结构将有助于了解其生物学功能。