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. 2016 Oct 7;16:198. doi: 10.1186/s12862-016-0775-0

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© The Author(s). 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 4 — Cartoon representation of hypothetical positions of the positively selected sites in Anastrepha OBPs, based in their predicted 3D structures. α-helices are shown in pink, β-sheets in green, loops in white, disulphide bonds in yellow and positively selected sites in blue. N- and C-terminus residues are shown with red and light green circles, respectively. a) AoblOBP56h-1 and AfraOBP56h-1 representation; b) AoblOBP56h-2 and AfraOBP56h-2 representation; c) AoblOBP57c and AfraOBP57c representation; d) AoblOBP50a, AfraOBP50a-1 and AfraOBP50a-2 representation