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. 2022 Feb 11;8:12. doi: 10.1038/s41421-022-00374-6

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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 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 The top, side, and bottom view of the ASU. Four E1–E2–capsid heterotrimers in the ASU are colored slate, magenta, orange, and green. Residues involved in the interaction are displayed as spheres with the same color as the corresponding heterotrimers. The slate, magenta, and orange heterotrimers form the Q-trimer, and the green heterotrimer is from the neighboring I-trimer. b Zoomed-in view from the red box in a of the interaction between E2 (magenta) and the neighboring E2 (slate) protein. c Zoomed-in view from the orange box in a of the interaction between E1 and the neighboring E2 protein. d, e Zoomed-in views from the green and blue boxes in a, showing the interactions between E1 (magenta) and the neighboring E1 (green), which also represent the interactions between Q-trimer and I-trimer. f The interaction between one capsid protein (magenta) and a neighboring capsid protein (slate) in the Q-trimer. The yellow dashed lines indicate the distance between the atoms involved in the interaction (the cut-off distance is 3.5 Å).