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. 2019 Jan 10;9:54. doi: 10.1038/s41598-018-37185-3

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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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NMR solution structure of SLy1 SAM_C homodimer. (a) Superposition of the 15 lowest energy structures of the disulphide bond-stabilized homodimer of SAM_C. The backbones of the monomers are coloured teal and red. (b,c) Ribbon representation of the structure closest to the average backbone structure (r.m.s.d. = 0.19 Å) of the ensemble. α-helices are shown in teal and red in each monomer, whereas the 3₁₀-helix part in the composite helix c2 is shown in green and orange. Helices α5 and α5′ are in tight contact to form the major part of the interface. They run in a parallel fashion with an angle of ~−50° between their long axes. Helix α1 and the N-terminus of one monomer are in close proximity to the C-terminal region of helix α5′ of the opposing monomer, and also form part of the dimer interface.