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. 2017 Nov 16;18:885. doi: 10.1186/s12864-017-4277-2

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© The Author(s). 2017

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. 3 — Multiple sequence alignment of the a-type domains of B. rapa PDI proteins and a typical human PDI. Residues highlighted in gray and light gray share 100% and >50% identity, respectively. Elements of the secondary structure are specified by blue colour bars (α-helices) and red colour bars (β-sheets). Red arrows indicate the two buried charged residues in the vicinity of the active site, orange arrow indicates the conserved arginine (R) and green arrow indicates the cis prolines (P) near each active site. Active-site residues within a domain are pink colour boxed