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. Author manuscript; available in PMC: 2021 Jan 22.
Published in final edited form as: J Am Chem Soc. 2020 Jan 9;142(3):1348–1358. doi: 10.1021/jacs.9b10521

Figure 1. NMR Spectrum of HNH.

Figure 1.

(a) Architecture of the Cas9 protein (PDB code: 4UN3),5 highlighting its protein domains as follows: HNH (green), RuvC (blue), PAM interacting region (PI, gold) and recognition lobe (REC, gray). In the close-up view, a model of the HNH structure determined from NMR data (green) is overlaid with that of HNH from the full-length Cas9 (gray). (b) 1H-15N HSQC NMR spectrum of the HNH nuclease domain from S. pyogenes Cas9 (the inset reports two peaks out of range). (c) Consensus chemical shift index (CSi), indicating the predicted secondary structure for the HNH construct based on the NMR chemical shifts (black bars from 0 to 1 indicate α-helix, while bars from 0 to −1 indicate β-sheet, see the Methods section) compared to that of HNH from the full-length Cas9 (shown on top of the graph as sequence, with α-helical and β-sheet regions indicated as tubes and arrows).