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. Resonance assignment and structural studies of largerproteins by nuclear magnetic resonance (NMR) can be challenging when exchange broadening, multiple stable conformations, and 1H back-exchange of the fully deuterated chain pose problems. These difficulties arise for the SARS-CoV-2 Main Protease, a homodimer of 2 × 306 residues. We demonstrate that the combinationof four-dimensional (4D) TROSY-NOESY-TROSY spectroscopy and 4DNOESY-NOESY-TROSY spectroscopy provides an effective tool for delineatingthe 1H–1H dipolar relaxation network. In combination with detailed structural information obtained from prior X-ray crystallography work, suchdata are particularly useful for extending and validating resonanceassignments as well as for probing structural features.

Four-dimensional NOE-NOE spectroscopy of SARS-CoV-2 Main Protease to facilitate resonance assignment and structural analysis