The only available deposition for the E protein in the Protein Data Bank (PDB) is the NMR set of 16 structures of a truncated SARS-CoV channel in lyso-myristoyl phosphatidylglycerol micelles (PDB 5X29 , see also Table and Fig. ). While these NMR models are lacking precision of X-ray structures, they offer several snapshots of the channel dynamics, which could be advantageous in the docking studies. It appears that the channel, and, specifically, its pore fluctuates wildly. Depicted on Fig. are the lumen radii calculated with HOLE program . The narrowest part of the channel could be 2.6-4.8Å wide, with an average of 4.4Å. Fluctuations of similar magnitude are visible along the whole length of the channel. Table . The sequences of E proteins from human SARS coronaviruses (as listed on uniprot.org ); the substructure of E protein, studied by NMR and deposited in Protein Data Bank (PDB); the modelled structure of E protein used for docking screening in this study. Blue -residues specific to SARS-CoV; red -residues specific to SARS-CoV-2; green -PBM .