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. 2019 Nov 7;9:16162. doi: 10.1038/s41598-019-52121-9

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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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Crystal structure of the ring-like construct showing a fully shielded binding surface at 2.4 Å. N- and C-termini of the proteins are marked. (a) Asymmetric unit with the DARPins coloured in light blue (N-terminal DARPin) and marine (C-terminal DARPin), the shared helices in red, the dArmRP in orange and the peptide in green. (b) Top-view highlighting the shielded binding surface (an overview of the crystal packing is shown in Fig. 5). (c) Overlay of the designed model in grey with the crystal structure in red. (d) Close-up view of the binding surface showing the regular peptide binding. 2mF_o-DF_c electron density of the peptide contoured at 1 σ.