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. 2022 Jun 5;17:14. doi: 10.1186/s13062-022-00325-x

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© The Author(s) 2022

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — Three-dimensional structure modeling of the MA-SARS2 spike. A Side view of S glycoprotein whose chain colored in Yellow/ Gray/ Rainbow, Drimer (ΔS2): two protomers lacking S2 subunit. B Zoomed-in of Drimer (ΔS2) as indicated. ROI-1: region 1 of interest, ROI-2: region 2 of interest; β, γ: S1 subunit of S glycoprotein. C Zoomed-in of ROI-1 after clockwise rotation by 90 degrees. Images show the interactions between H655 (a, c) or Y655 (b, d) with N657 in the presence or absence of furin cleavage finger. D Zoomed images of ROI-2 after clockwise flipping by 90 degrees (a, b) and subsequent clockwise rotation by 90 degrees (c, d). Images a, b show the interactions between two chains, c, d show the interactions between wild type (L216) or Ins215KLRS and other amino acids. Gray circle: Ins215KLRS mutation