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. 2017 Sep 18;7:11748. doi: 10.1038/s41598-017-12168-y

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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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The binding mode of MYR with SLY based on molecular dynamics simulation. (a), (c) MYR can bind to the gap region between D2 and D3 in SLY; (b) residues of the binding site in the SLY-MYR complex; (d) the RMSD displayed by the backbone atoms of the protein during MD simulations of the SLY-MYR complex.