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. 2020 Oct 12;10:16986. doi: 10.1038/s41598-020-74099-5

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© The Author(s) 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Structural information of dimeric M^pro. The respective protomers of dimeric M^pro are shown in magenta and blue cartoon representations. The catalytic dyad, His41 and Cys145, are represented by the space-filling model. The three possible ligand binding sites were predicted. (a) Side view, (b) bottom view, (c) top view, (d) the view from the arrow of (a), and (e) the three domains of protomer (monomer) structure. Each protomer was composed of three domains: domains I, II, and III are residues 8–101 (red), 102–184 (blue), and 201–303 (green), respectively³. The lipophilic and hydrophilic regions in each site are depicted with green and orange.