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. 2017 Jun 16;7:3666. doi: 10.1038/s41598-017-03966-5

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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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Red- (a and b) and ox- (c and d) dominated residue-residue interaction networks on two representative conformations of red- and ox-hPDI (C3 and C6 of FEL) between the b’ and a’ domains. Residues (C_α) within the hydrophobic pocket in each state are colored in red. Red and blue dash-lines indicate the ox- and red-dominated interactions, respectively. Secondary structures involve in formation of the upper edge of hydrophobic pocket are colored in brown (H9, H11 and L_B14-B15). Secondary structures of a’ domain that contribute in b’a’ interactions are colored in violet (L_B17-H15, L_B18-B19 and L_B19-B20).