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. 2018 Oct 9;8:15005. doi: 10.1038/s41598-018-33379-x

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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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Mapping of ALYREF/REF2-I interaction with KSHV ORF57 by NMR. Perturbations in ¹⁵N HSQC spectra were used to map interactions of ¹⁵N-labeled REF2-I constructs with unlabeled ksORF57 constructs. (A) Signal shifts and intensity perturbations induced by ksORF57Δ53 on REF^1–155 mapped onto its sequence. (B) Signal shifts and intensity perturbations induced by ksORF57^68–178 on REFΔ53 mapped onto its sequence. Secondary structure elements are highlighted on the primary sequence; α-helix in red, β-sheet in yellow. Broadened residues indicated by circles and moderate and large shifts indicated by light and dark blocks, respectively. (C) Example spectrum of free ¹⁵N labeled REFFΔ53 (red) is overlaid with spectrum upon addition of ksORF57^68–178 (blue) shows spectral perturbations assigned to RRM region of REF2-I.