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. 2017 Jul 11;7:5093. doi: 10.1038/s41598-017-04108-7

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© The Author(s) 2017

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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Binding of IMB-YH-8 to PknB as measured by surface plasmon resonance (a) and isothermal titration calorimetry (b). (a) Upper panel: Blank subtracted sensorgram for the binding of IMB-YH-8 (range from 12.5 to 200 μM). Lower panel: The affinity for IMB-YH-8 binding (K _D = 25.3 μM) was calculated from the association equilibrium data. (b) Thermograms (upper panel) and binding isotherms with theoretical fits (lower panel) obtained for the binding of IMB-YH-8 to PknB.