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. 2019 Dec 6;10:5579. doi: 10.1038/s41467-019-13346-4

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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. 1 — Structure of the HLA-A*68:01-NP₁₄₅ complex. Structure of the HLA-A*68:01 (white cartoon) bound to the NP₁₄₅ peptide (orange stick). a A zoomed view of the P2-Ala anchor residue interaction with the HLA-A*68:01 molecule, the blue dashed lines represent hydrophobic interactions. b The P12-Arg salt bridge network (red dashed lines) with the HLA-A*68:01 amino acids. c, d The electron density maps after refinement (c 2Fo-Fc map colored in purple and contoured at 1 σ) or before building the peptide in d (Fo-Fc or omit map colored in green and contoured at 3 σ). The orange dashed line on c, d represent the missing amino acid from the NP₁₄₅ peptide (P4–P8) in the crystal structure.