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. 2017 Jun 14;7:3537. doi: 10.1038/s41598-017-03814-6

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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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Chemical shift perturbation. (a) Residues with large chemical shift changes (Δδ_NH > 0.04 ppm) upon Az binding to an ATPase domain of Hsc70 were mapped in blue on the structure (PDB entry 2E8A). Subdomains IA, IIA, IB and IIB are shown in the structure (b) Chemical shift changes of M87-H89 and K248-K250 after addition of Az to an ATPase domain of Hsc70 are shown in 2D ¹⁵N-¹H TROSY HSQC spectra. The ratios of protein to Az are 1:0 (blue), 1:0.5 (green), 1:1 (yellow), 1:1.25 (magenta) and 1:1.5 (red).