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. 2019 May 16;9:7482. doi: 10.1038/s41598-019-44013-9

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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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Superimposition of WT-RpsA (A) and mutant (B–J) in apo state and complex (Com) state. RpsA and POA binding residues are 303, 307, 310, and 357. Superimposition of mutant D342N, D343N, A344P, and I351F and WT-RpsA before and after simulation. The difference in RMSDs have been shown with each superimposed structure.