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. 2017 Dec 1;7:16696. doi: 10.1038/s41598-017-16959-1

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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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Structure of the cortactin repeats. (A) Normalized pair distribution function P(r) for cortactinCRH calculated with GNOM⁴⁴. 1.1 mg/mL (blue) and 0.4 mg/mL (red) samples. (B) Ab initio models of CortactinCRH show extensive conformational diversity (blue). The averaged model (orange) is elongated. Models were calculated by use of DAMMIF⁴⁵. (C) Calculated R _g values for the cortactinCRH sequence. Relative frequency of calculated R _g values from analysis of 100,000 molecular models of cortactinCRH as an unfolded protein based on its sequence by use of the program Flexible-Meccano³¹. Frequency of calculated R _g values (green) is compared to the observed R _g for cortactinCRH. The experimental R _g of cortactinCRH falls at the distribution peak of the calculated range.