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. 2017 Nov 13;7:15440. doi: 10.1038/s41598-017-15549-5

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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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Simultaneous phosphorylation of all three sites (Ser203, 211 & 226) in the GR results in conformational changes in AF1. (A) Representative low-energy conformations of the non-phosphorylated AF1_C peptide. (B–D) close up view of non-phosphorylated Ser203, 211 & 226 residues, respectively. (E) Representative low-energy conformations of the AF1_C peptide when all three sites (Ser203, 211 & 226) are simultaneously phosphorylated. (F–H) close up view of phosphorylated Ser203, 211 & 226 residues and their respective binding to nearby residues. Phosphorylated Ser203 and 211 are shown forming a hydrogen bond network that is displayed as dots between donor and acceptor atoms.