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. 2019 May 8;9:7083. doi: 10.1038/s41598-019-43646-0

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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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Close-up view of a section of the interface between Ras (green) and SOS (magenta) at the “catalytic” Ras-binding site of SOS²⁶, with Ras residue 33 shown in cyan. Hydrogen bonds are calculated using PyMOL and shown as dashed yellow lines. The left panel shows the wild-type Asp33 residue and the right panel shows the model of Asp33Glu. The mutation causes a change in the hydrogen bonding pattern at this site. Modelling this variant at the “distal” Ras-binding site of SOS shows a similar pattern of change in the hydrogen bonding pattern. No significant interatomic clashes are created.