Supplementary Figure 4: Validation of BH_10 backbone NMR assignments with TALOS-N analysis.
From: De novo design of a non-local β-sheet protein with high stability and accuracy
a, Sequence window displaying the BH_10 protein sequence with each residue colored according to classification in TALOS-N analysis (J. Biomol. NMR 56, 227–241, 2013). Green, good classification; yellow, ambiguous/no classification; red, bad classification (in the case of L66, its bad classification is likely due to its loop position); gray, no classification. b, Bottom, TALOS-N-derived secondary structure index (SSI) derived from combined 1H, 15N and 13C chemical shifts for BH_10. α-helices are colored red and β-sheets are colored aqua. Top, the random coil index order parameter (RCI-S2) for BH_10. Analysis of these NMR backbone resonance assignments using TALOS-N shows excellent agreement between the chemical-shift-derived secondary structure index and the DSSP annotation of the de novo model
