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. 2017 Nov 8;7:15042. doi: 10.1038/s41598-017-14886-9

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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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Computerized interaction of modeled-NS5A and HuscFvs and residues that were predicted to form contact interface between them. Left side of Panels A-E shows interactions of NS5A (beige) and respective HuscFvs (green). Right side of Panels A-E shows contact residues between NS5A and HuscFv5, HuscFv9, HuscFv16, HuscFv19 and HuscFv99, respectively. The NS5A amino acids are colored according to CINEMA color scheme: polar negative D and E are red; polar positive H, K, and R are blue; polar neutral S, T, N, and Q are green; non-polar aromatic F and Y are purple/magenta; non-polar aliphatic A, V, L, I, and M are white (grey in this study as the background is white); and P and G are brown. The π-π interaction is shown as dotted green line; H bond/salt-bridge is shown as dotted yellow line.