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. 2020 Jun 23;10:10205. doi: 10.1038/s41598-020-66431-w

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© The Author(s) 2020

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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The post-acylation structure of Glu166Tyr shows displacement of Tyr166 and DW away from the PenP-cephaloridine acyl adduct. (a) The active site in the post-acylation structure. Fo-Fc omit map (purple) is drawn in mesh format and contoured at 2.0 σ to highlight the newly formed acyl adduct between Ser70 and the cephaloridine substrate. The dashed lines indicate hydrogen bonds. (b) Superposition of post-acylation structure (cyan) with the apo structure (golden). The acyl adduct is highlighted in green. The two water molecules are enlarged for presentation effect.