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. 2019 Apr 29;9:6627. doi: 10.1038/s41598-019-43004-0

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© The Author(s) 2019

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-based prediction of the stability of CRM1-NES peptide complex. (A) CRM1-NES peptide complex model generation and E_bind calculation procedure. (B) Generated models for the complex structures of CRM1-NES peptides with lowest E_bind. Class 1a peptides are displayed with CRM1 (in white) at the top. The hydrophobic (Φ) residues of these NES peptides (shown in the sticks) occupy the corresponding hydrophobic pockets (P0-P4) in CRM1. Peptides of other classes are shown at the bottom with the hydrophobic residues shown in the sticks.