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. 2017 Aug 15;7:8145. doi: 10.1038/s41598-017-08414-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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Binding discrimination in Fab NC41–influenza virus neuraminidase N9 and Fab 44.1–hen egg-white lysozyme complexes. Surface area change upon binding (ΔSASA) vs. Interface scores for model structures in antibody cross-docking tests using bound, unbound, and homology-modeled backbones in (a) influenza virus neuraminidase N9, and (b) hen egg-white lysozyme. Sixteen non-cognate structures (grey) are compared to cognate structures (turquoise); black outline indicates the top-scoring model for each antibody–antigen pair. The top-scoring cognate complexes generated using bound (red), unbound (blue), and homology (green) complexes in (c) influenza virus neuraminidase N9, and (d) hen egg-white lysozyme complexes. (e) Top-scoring cognate (blue) and non-cognate (grey) antibody against hen egg-white lysozyme.