The non-structural protein nsp3 from SARS-CoV-2 plays an essential role in the viral replication transcription complex. Nsp3a constitutes the N-terminal domain of nsp3, comprising a ubiquitin-like folded domain and a disordered acidic chain. This region of nsp3a has been linked to interactions with the viral nucleoprotein and the structure of double membrane vesicles. Here, we report the backbone resonance assignment of both domains of nsp3a. The study is carried out in the context of the international covid19-nmr consortium, which aims to characterize SARS-CoV-2 proteins and RNAs, providing for example NMR chemical shift assignments of the different viral components. Our assignment will provide the basis for the identification of inhibitors and further functional and interaction studies of this essential protein.

来自 SARS-CoV-2 的非结构蛋白 nsp3 在病毒复制转录复合物中起着至关重要的作用。Nsp3a构成nsp3的N端结构域，包括泛素样折叠结构域和无序酸性链。nsp3a 的这个区域与病毒核蛋白的相互作用和双膜囊泡的结构有关。在这里，我们报告了 nsp3a 的两个域的主干共振分配。该研究是在国际covid19-nmr的背景下进行的该联盟旨在表征 SARS-CoV-2 蛋白质和 RNA，例如提供不同病毒成分的 NMR 化学位移分配。我们的任务将为鉴定抑制剂和进一步研究这种必需蛋白质的功能和相互作用提供基础。