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. 2020 Nov 20;21:82. doi: 10.1186/s12860-020-00328-4

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© The Author(s) 2020

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. 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 in a credit line to the data.

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Fig. 2 — Representative of the docking interaction of a protein receptor and putative anti-pneumonia AMPs produced by PATCHDOCK and visualized using PyMol. BOPAM-AB3, 2, and 4 had higher binding affinity than all anti-Acinetobacter baumannii AMPs, BOPAM-SP2, and 6 had higher binding affinity than all anti-Streptococcus pneumoniae AMPs whilst BOPAM-KP2 and 6 had higher binding affinity than all anti-Klebsiella pneumoniae AMPs