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. 2020 Dec 3;21(6):409–419. doi: 10.1038/s41435-020-00120-6

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© The Author(s), under exclusive licence to Springer Nature Limited part of Springer Nature 2020

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a Protein structure of SARS-CoV-2 Nsp3 depicting types and locations of fixed amino-acid substitutions within distinct macrodomains. The fixed amino-acid replacements are shown as spheres and labeled with the amino-acid position in Nsp3 protein. b Comparison of the three-dimensional (3D) conformations of the macrodomains (Mac-1, Mac-2, and Mac-3) within Nsp3. SARS-CoV-2 (YP_009725299.1) macrodomains were also compared to the corresponding homologous protein regions of bat-RatG13 (QHR63299.1), SARS-CoVBJ01 (AAP30028.1), and the predicted ancestral macrodomain of SARS-CoV-2 and bat-RaTG13/ZC45/ZXC21. Structural deviations in terms of backbone torsion angles (Φ°, Ψ°) are represented in red color and were examined by RMSD (root mean square deviation) values. c–e Close-up of 3D conformations of SARS-CoV-2 Mac-2 with corresponding homologous domains from predicted ancestor (aforementioned; left panel), bat-RatG13 (middle panel), and SARS-CoV (AAP30028.1; right panel). Comparisons of 3D conformations for Mac-1 is provided in Fig. 4 and sequence secondary structural level details for comparisons in b–e are given in Supplementary Tables S6, S7.