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. 2016 Dec 7;14:109. doi: 10.1186/s12915-016-0332-8

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© Ho et al. 2016

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided 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 Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.

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Fig. 5 — Assignment of the ¹⁵N BEST-TROSY of the LITAF Δ114–139 construct. Cross-peaks assigned to the structured LITAF domain have a wide proton distribution (~7.5 to 9.6 ppm) consistent with the secondary structure of β-strands. In contrast, cross-peaks assigned to the unstructured N-terminal proline-rich arm occupy the narrower random coil central region of the spectrum (7.8 to 8.4 ppm)