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. 2017 Aug 30;7:9597. doi: 10.1038/s41598-017-10246-9

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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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Mutants with increased affinity have fewer fluctuating residues. (a,b) Magnitude of the chemical shift changes caused by the H:R71A (a) and L:R45A (b) mutations shown in yellow for those greater than the average and in red for those greater than the average plus one standard deviation. (c) Relaxation dispersion profiles of H:R71 in free WT (black) and H:A71 in free H:R71A (red). (d) Relaxation dispersion profiles of L:R45 in free WT (black) and L:A45 in free L:R45A (red). (e,f) Amplitude of the R _ex rates for H:R71A (e) and L:R45A (f) mapped on the crystal structure of free HyHEL-10, as a continuous color scheme from purple to red. The V_H and V_L domains are shown in light green and light blue, respectively.