More subtle computational techniques based on protein conformation have in this project suggested relationships between SARS-CoV and hemagglutinins and neuraminidases of other viruses, but they essentially support prior work. Recall that Zhang and Yap [13] noted a suggestive structure similarity between SARS-CoV S1 and influenza virus neuraminidase. Using various computational techniques they compared the 3D structure of SARS-CoV S1 Protein Data Bank 3D structures 1INY (neuraminidase from influenza A virus complexed with a sialic acid phosphonate analogue inhibitor) and 1B9T (neuraminidase from influenza B virus with novel aromatic inhibitors). This observation does not necessarily suggest by itself a common function, because many protein folding patterns are used by nature for diverse purposes, but armed with that information a more careful use of sequence alignment is helpful. The following part of a Clustal omega sequence alignment done in the present study also includes the hemagglutinin esterase sites in E3 of the bovine coronavirus [8] (E3-CoV-Q14EB1.1 below) and that studied by Zeng et al. [9] (Hem-est-CoV-3CL5 below). Substrate binding residues in deduced for SARS-CoV S1 by Zhan and Yap [13] are shown by #.