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. 2022 Nov 9;613(7944):558–564. doi: 10.1038/s41586-022-05514-2

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© The Author(s) 2022

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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Extended Data Fig. 7 — a, Overlay of nirmatrelvir and ensitrelvir binding to 3CL^pro. b, Several of the residues involved in direct interaction with nirmatrelvir. c, Several of the residues involved in formation of the S1 subsite. d, Interaction of L167 with nirmatrelvir. In a-d, nirmatrelvir is shown in yellow, enstirelvir is shown in lime green, the 3CL^pro-nirmatrelvir complex is shown in marine, and the 3CL^pro-ensitrelvir complex is shown in gray. Protomer A is shown in marine and protomer B is shown in green. Hydrogen bonds are indicated as black dashes. The 3CL^pro-nirmatrelvir complex and 3CL^pro-ensitrelvir complex were downloaded from PDB under accession codes 7VH8 and 7VU6, respectively.