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. 2017 Jun 6;7:2863. doi: 10.1038/s41598-017-02671-7

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© The Author(s) 2017

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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Binding mode of SHK and lead compound PMM-158 with STAT3 (PDB code: 1BG1). (A) 2D diagram of the interaction between SHK and amino acid residues of the nearby active site. (B) 3D diagram of SHK inserted in the STAT3 binding site: for clarity, 3D structure of the protein is presented in line ribbon and only interacting residues are displayed. (C) 2D diagram of the interaction between PMM-158 and amino acid residues of the nearby active site. (D) 3D diagram of PMM-158 inserted in the STAT3 binding site: for clarity, 3D structure of the protein is presented in line ribbon and only interacting residues are displayed. (E)The RMSDs of the three studied complexes obtained during 5 ns of MD simulations, SHK (blue), lead compound (red) and PMM-172 (black).