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. 2018 Sep 11;8:13588. doi: 10.1038/s41598-018-31739-1

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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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Analysis of BraA.eIF(iso)4E.c-1 protein domain tertiary structure. (A) The three-dimensional structural model was built based on the wheat eIF(iso)4E protein. (B) Four amino acid variations were detected between the BraA.eIF(iso)4E.c-1 and BraA.eIF(iso)4E.c-2 proteins. (C) The location of the three different amino acid variations is depicted in the structural model of the entire protein. (D) The 36^th amino acid changed from phenylalanine to leucine. (E) The 52^th amino acids changed from valine to alanine. (F) The 80^th changed from isoleucine to threonine. (G) The 150^th changed from proline to glutamine.