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. Author manuscript; available in PMC: 2023 Sep 6.
Published in final edited form as: J Am Chem Soc. 2022 May 31;144(23):10543–10555. doi: 10.1021/jacs.2c03320

Figure 2 |. Correlation spectra, inter-residue distance restraints and MAS NMR structure of a single NNTD chain.

Figure 2 |

a) Superposition of representative regions of 2D CORD spectra of U-13C,15N-NNTD acquired with the mixing times of 100 ms (blue) and 500 ms (gray). Aromatic and aliphatic regions are shown in the left and right panel, respectively. Representative cross peaks between amino acids are labeled by residue numbers. b) The number of all inter-residue distance restraints and long-range inter-residue distance restraints are plotted for each residue along the polypeptide chain. c) Superposition of the ten lowest-energy MAS NMR structures of a single chain of SARS-CoV-2 NNTD. β-strands are colored in blue and labeled. The number of scans, the number points in the direct and indirect dimensions are as follows: 2D CORD (100 ms mixing time)- 96 scans, 3072 t2 points, 840 t1 points; 2D CORD (500 ms mixing time)- 192 scans, 3072 t2 points, 667 t1 points.