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. 2019 Mar 13;9:4392. doi: 10.1038/s41598-019-40558-x

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© The Author(s) 2019

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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Dimer of ThiL. (A) shows the dimer of AbThiL bound to ADP/TMP looking down a dyad. The model of chain A on the right side is colored by secondary structure elements, helices in purple, strands in yellow. The model of chain B on the left side is colored by domains, the A domain in light blue, the B domain in blue. Strands β0′ and β1′ are part of the β-sheet that is mostly located in domain A. (B,C) highlight the domain swap of the N-terminus. In (B), the dimer of AbThiL is shown in the same orientation as in. (A) Chain A is colored in light purple with secondary structure elements α1, β0 and β1 highlighted in purple and yellow, respectively, and loops between them in black. The corresponding region in chain B is marked in dark grey. In (C), the model of AaThiL is shown in the same orientation and the same color scheme. Helix α1 and strand β1 of AaThiL are located in the space that helix α1′ and strand β1′ occupy in AbThiL. Strand β0 is unique to AbThiL and part of a loop in AaThiL. Starting with strand β2 secondary structure elements match up again.