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. 2022 May 9;13:2530. doi: 10.1038/s41467-022-30258-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. 1 — a Chemical structures of ATP-competitive and allosteric inhibitors. b Crystal structure of EGFR(T790M/V948R) in complex with osimertinib and EAI045 (PDB 7JXM). The C-helix is colored red, Asp-Phe-Gly (DFG) motif in orange, ATP-site inhibitor in magenta, and allosteric inhibitor in green. c EGFR(L858R/V948R) in complex with osimertinib and JBJ-063 (PDB 7K1H). The P-loop and side chain of F723 from EGFR(L858R/V948R) in complex with AMP-PNP and JBJ-063 is shown in dark gray for comparison (PDB 7K1I). d EGFR(T790M/V948R) in complex with osimertinib and DDC4002 (PDB 6XL4).