The SARS-CoV-2 genome encodes for approximately 30 proteins. Within the international project covid19-nmr, we distribute the spectroscopic analysis of the viral proteins and RNA. Here, we report NMR chemical shift assignments for the protein nsp7. The 83 amino acid nsp7 protein is an essential cofactor in the RNA-dependent RNA polymerase. The polymerase activity and processivity of nsp12 are greatly enhanced by binding 1 copy of nsp7 and 2 copies of nsp8 to form a 160 kD complex. A separate hexadecameric complex of nsp7 and nsp8 (8 copies of each) forms a large ring-like structure. Thus, nsp7 is an important component of several large protein complexes that are required for replication of the large and complex coronavirus genome. We here report the near-complete NMR backbone and sidechain resonance assignment (¹H,¹³C,¹⁵N) of isolated nsp7 from SARS-CoV-2 in solution. Further, we derive the secondary structure and compare it to the previously reported assignments and structure of the SARS-CoV nsp7.

SARS-CoV-2 基因组编码大约 30 种蛋白质。在国际项目 covid19-nmr 中，我们分发了病毒蛋白和 RNA 的光谱分析。在这里，我们报告了蛋白质 nsp7 的 NMR 化学位移分配。83 个氨基酸的 nsp7 蛋白是 RNA 依赖性 RNA 聚合酶中必不可少的辅助因子。通过结合 1 个拷贝的 nsp7 和 2 个拷贝的 nsp8 形成一个 160 kD 的复合物，大大增强了 nsp12 的聚合酶活性和持续合成能力。nsp7 和 nsp8 的一个单独的十六聚体复合物（每个 8 个拷贝）形成一个大的环状结构。因此，nsp7 是复制大型复杂冠状病毒基因组所需的几种大型蛋白质复合物的重要组成部分。我们在这里报告了近乎完整的 NMR 骨干和侧链共振分配 ( ¹H, ¹³ C, ¹⁵ N) 从 SARS-CoV-2 中分离出来的 nsp7 在溶液中。此外，我们推导出二级结构并将其与先前报道的 SARS-CoV nsp7 的分配和结构进行比较。