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. 2017 Nov 1;7:14847. doi: 10.1038/s41598-017-14840-9

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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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Results of blind docking calculations of steroids E2 (left) and EN (right) to hERα. At the top, cluster representant steroid conformations (spheres) and the corresponding rank numbers are shown. A small rank number corresponds to energetically favorable binding mode of the steroid. The receptor is shown as grey cartoon. At the bottom, a close-up of binding conformation of steroid E2 (magenta) and EN (green sticks) is shown in the ABS (Rank 2 in both cases). Neighbouring hERα residues are shown as sticks with grey carbon atoms.