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. 2022 Jan 10;13:19. doi: 10.1038/s41467-021-27669-8

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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. 5 — a Interactions between RLQ3 and the HLA-A2 α1 helix. The side chains of contacting residues are drawn in stick representation with carbon atoms in green (TCR α chain), pink (TCR β chain) or gray (HLA-A2), nitrogen atoms in blue, and oxygen atoms in red. Hydrogen bonds are indicated by red dashed lines, water molecules are shown as yellow spheres, and water-mediated hydrogen bonds are indicated by yellow dashed lines. b Interactions between RLQ3 and the HLA-A2 α2 helix. c Interactions between YLQ7 and the HLA-A2 α1 helix. TCR α chain, blue; TCR β chain, magenta. d Interactions between YLQ7 and the HLA-A2 α2 helix.