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. 2018 Mar 21;9:1168. doi: 10.1038/s41467-018-03442-2

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© The Author(s) 2018

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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Fig. 1 — The structure and active site of AsqJ. a The dimeric protein structure of AsqJ (PDB ID:5DAQ; one subunit in the asymmetric unit), depicting the location of the active site. The inset shows a DFT model of the active site of AsqJ, comprising 194 atoms. Atoms marked with asterisk are kept fixed in the structure optimizations. b Reaction sequence catalyzed by AsqJ. Substrate 1 is the AsqK-produced NRPS product of anthranilic acid and Tyr(OMe); the N4-methyl group is derived from S-adenosylmethionine¹⁵