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. 2024 Oct 7;15:8574. doi: 10.1038/s41467-024-52808-2

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 2 — A–C Cryo-EM maps of BA.2.86-S-protein bound to human ACE2 (S; same colors as Fig. 1C, ACE2; dark gray). A Two-RBD-up state (top), and three-RBD-up state (bottom). B Two-RBD-up−one-RBD-down_three-ACE2 state. C Comparison of the angles formed by the three residues: N164 of the NTD and two G476 of the up-RBD for two-RBD-up_two-ACE2 (34.2°, left) and two-RBD-up−one-RBD-down_three-ACE2 (110.9°, right), respectively. D Close-up view of the two-RBD-up−one-RBD-down_three-ACE2 state. The N165-linked glycan in the NTD and the N322-linked glycan in ACE2 are situated close to each other.