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. 2019 Jan 11;9:59. doi: 10.1038/s41598-018-37276-1

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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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Peptide plane flipping. (A) System 2 (2N0A, WT, Neutral pH, 498 K), (B) System 4 (2N0A, WT, Low pH, 498 K), (C) System 5 (2N0A, A30P, Neutral pH, 300 K), (D) System 12 (2N0A, ACE-N-terminal, Neutral pH, 498 K), (E) System 13 (2KKW, WT, Neutral pH, 498 K) and (F) System 14 (2KKW, WT, Low pH, 498 K). The main chain atoms of the α-strand residues are displayed whereas side chain and non-polar hydrogen atoms are not displayed for clarity. First α-strand conformation is represented by pink stick model while initial conformation at the beginning of the production run is shown by green stick model. Flip of CO-NH plane is highlighted.