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. 2018 Jan 18;8:1045. doi: 10.1038/s41598-018-19295-0

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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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Protein-protein docking analysis shows the specific amino acids responsible for the nsP1-nsP2 interaction. The protein-protein docking between nsP1-WT and nsP2-NT was performed using the ClusPro 2.0 web server. (a) The most stable conformation of the complex of nsP2-NT (green) and nsP1-WT (orange). Polar interacting residues within 2.6 Å distance of nsP1-WT (blue) and nsP2-NT (red) are marked in the complex. (b) The red bridges showing the polar interactions between residues of nsP1-WT (Orange) and nsP2-NT (Green).