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. 2022 Aug 19;12:14158. doi: 10.1038/s41598-022-17913-6

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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¹H STD-NMR experiment of 7.44 binding to NHR2. (A) Reference spectrum of 7.44. Assignment of the individual peaks is indicated (see 7.44 structure in the bottom panel). (B) ¹H STD-NMR spectrum of ligand 7.44 in the presence of NHR2. Relative intensities are indicated on top of the corresponding peaks and mapped onto the structure of 7.44. The circles are colored by the relative intensity of the protons, which is correlated with the proximity to the protein: red—100% (the closest), lighter red—97% to 64%, faded red—48% to 19%. The proton numbering is indicated by the red numbers. Data was acquired at 600 MHz and 298 K, with a 100-fold molar excess of 7.44.