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. 2022 Sep 5;13:5232. doi: 10.1038/s41467-022-32822-y

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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. 4 — a Chemical structure of fMLF and its non-formyl analogs. b Slab views of the binding pocket of fMLF (left, cryo-EM model), MLF (middle, docking model), and tBOC-MLF (right, docking model) in FPR1, respectively. The ligands are displayed in licorice with carbon in orange. The binding pocket is highlighted in white. c Molecular interaction of bound fMLF (left), MLF (middle), and tBOC-MLF (right) with the FPR1 binding pocket. d Chemical structures of WKYMVm, AG-14 and Compound 17b (Cpd 17b). e Slab views of the binding pocket of WKYMVm, AG-14 and Cpd 17b, all from docking models. f molecular interaction of bound WKYMVm (left), AG-14 (middle), and Cpd 17b (right) with the FPR1 binding pocket, respectively. The residues of FPR1 within 4.5 Å to the atoms of the ligands are shown as green licorice.