Figure 1.
Fig. 1. The active site of ASV IN (catalytic core
domain). A, F[o] F[c]
difference density "omit" map, contoured at 2.5 , showing
the position of the side chain of D64N (blue) compared with the
side chain of Asp-64 (brown) in the active conformation. The
hydrogen bonding pattern of a structurally conserved water
molecule observed in all ASV IN structures is also shown. B,
hydrogen bonding of the side chain of D64N with Asn-160. The
hydrogen bonding pattern of a structurally conserved water
molecule observed in all ASV IN structures is also shown. C,
hydrogen bonding of the side chain of Asp-64 with the
structurally conserved water.
F[c]
difference density "omit" map, contoured at 2.5 
, showing
the position of the side chain of D64N (blue) compared with the
side chain of Asp-64 (brown) in the active conformation. The
hydrogen bonding pattern of a structurally conserved water
molecule observed in all ASV IN structures is also shown. B,
hydrogen bonding of the side chain of D64N with Asn-160. The
hydrogen bonding pattern of a structurally conserved water
molecule observed in all ASV IN structures is also shown. C,
hydrogen bonding of the side chain of Asp-64 with the
structurally conserved water.