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. 2020 Oct 26;11:5394. doi: 10.1038/s41467-020-19023-1

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© The Author(s) 2020

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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Fig. 4 — Structures obtained by FRET-assisted modeling (magenta) and target X-ray structures (black) are shown for each of the benchmarked proteins. FRET-selected structures are depicted in transparent magenta as a measure for uncertainty; a confidence level of 68% is assumed. RMSD of C_α atoms of the seed conformer (RMSD_seed) and FRET-selected conformers (RMSD_FRET) against the target crystal structure is shown below the protein name. Networks of FRET pairs and secondary structures of corresponding seed conformers (cyan) are shown below the selected ensembles.