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. 2017 Apr 21;7:1069. doi: 10.1038/s41598-017-00917-y

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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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Overall structures of Smon0123. Structures (stereo-diagram with wall-eyed viewing) of ligand-free Smon0123 (N-28/C-5) (A) and CΔ0S-bound Smon0123 (N-18/C-5) (B). Cyan, α-helices; purple, β-strands; pink, loops and coils. CΔ0S bound to Smon0123 is shown in ball model (green, carbon atom; red, oxygen atom; and blue, nitrogen atom). Orange ball shows the metal ion. Structural comparison with ligand-free Smon0123 (N-28/C-5) (olive) and CΔ0S-bound Smon0123 (N-18/C-5) (blue) (C). Both N-domains of ligand-free and -bound Smon0123 proteins were superimposed. There is a structural difference (47° in angle) in the N- and C-domains between C∆0S-free and -bound Smon0123.