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. 2020 Apr 6;11:1713. doi: 10.1038/s41467-020-15575-4

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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 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. 4 — The portal assembly and the surrounding gp23* capsomers are colored and labeled as in Fig. 1a. a Tilt between the portal and the capsid. The tilt axis, portal axis, and capsid axis are shown. b Hydrophobic interaction between gp20 α2 and gp23* capsomers. c The potential methionine-metal clusters formed between the N-whisker methionine (M1) of subunits 1 and 6 of gp20 and subunits S5 and S2 of gp23*. Residues involved in forming the metal binding sites are labeled.