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. 2015 Mar 27;16:103. doi: 10.1186/s12859-015-0528-x

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© Moonrin et al.; licensee BioMed Central. 2015

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. 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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The interactions of the key residues of MIG-6_s1 with nearby residues. (A) The hydrophobic interactions and hydrogen bonds of Phe352 and nearby residues. (B) The hydrophobic interactions and hydrogen bonds ofTyr358 and nearby residues. (C) The π-π interactions between the aromatic rings of Phe352 and Tyr358. (D) The hydrogen bond and hydrophobic interactions of Tyr341. (E) The hydrogen bonds between polar residues of EGFR kinase Glu907 and Thr349 of MIG-6_s1. (F) The hydrogen bonds and hydrophobic interactions of Gln350. (G) The hydrogen bonds of Asn343 to Thr885 and Gly959. The important interactions were plotted by LIGPLOT program.