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. 2018 Dec 4;8:17611. doi: 10.1038/s41598-018-35464-7

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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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Models of V_HNAC1 in complex with NAC peptide. (a) Top four models obtained from simulations of the V_HNAC1-NAC complex and (b) a fifth model that was chosen based on SPR results. Models I, II and V were obtained for a 19-residue α-helical peptide from the NAC domain (amino acids 61–79) while Models III and IV were obtained for a 13-residue random coil peptide from the NAC domain (amino acids 66–78). NAC peptides are shown in cyan.