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. 2019 Feb 4;9:1304. doi: 10.1038/s41598-018-37506-6

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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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Molecular modeling of EfTu interaction with SP. Binding of SP to folded (A) and unfolded (B) B. cereus EfTu calculated using AutoDock 4.2 should occur at the level of the inter-region between domains I and II of EfTu and the 4 N-terminal polar amino acids of SP. In the binding region (C), SP (bold lines) should interact principally with amino acids LYS10 – PRO11 – HIS12 – ASN14 – GLN98 – ASP100 – PRO203 – GLU204 – ARG205 – GLU206. The center of the grid for docking was EfTu LYS90 (size 126x126x126 points, path 0.375 A). Calculated binding values between SP and folded or unfolded EfTu were −7.85 and −7.75 Kcal/mol, respectively.