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. 2018 Aug 15;8:12163. doi: 10.1038/s41598-018-29683-1

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© The Author(s) 2018

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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Curcumin and harmine bind with high affinity to distinct sites on EGFR, ERK1 and Akt-1. Binding conformation of top ranked docked poses of (A,C,E) curcumin and (B,D,F) harmine on EGFR tyrosine kinase domain, ERK1 tyrosine kinase domain and Akt1 catalytic domain, respectively. Further details, including detailed labeling of interactive amino acid residues are provided in Supplemental Figs 3–6.