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![[Figure 2]](ni5019fig2mag.jpg)
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Figure 2
Final electron densities for the most relevant regions of new-inactive Mpro. 2Fo − Fc maps contoured at the 1.0σ level are shown. (a) and (b) show two views of the final electron density for the oxyanion loop in the new conformation. Leu141 and the solvent-exposed Phe140 and Lys137 side chains have incomplete densities indicating various degrees of flexibility. (c) Simulated-annealing omit map (oxyanion-loop residues 138–146 were omitted) viewed as in (b). (d) Electron density in the inter-protomer (intra-dimer) interaction area between the oxyanion loop of one protomer and the N-finger of the other protomer (residues Ser1′–Met6′). |
![[Figure 2]](ni5019fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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