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. 2018 Oct 15;8:15248. doi: 10.1038/s41598-018-33568-8

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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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Molecular model of OmpR. The dimer form of OmpR structure and the zoom-in region of the phosphorylation site Asp55 are shown. The monomer of OmpR is shown in yellow and magenta color. The residues Asp55, Gly63 and Thr83 are highlighted in ball-and-stick format and colored by element (carbon, gray; nitrogen, blue; oxygen, red). The figures were produced using Discovery Studio visualizer (Accelrys).