Figure 2.
Fig. 2. Residue Tyr106 predominantly adopts the outside
conformation in CheY95IV instead of the double conformations
seen in the wild-type structure (10). Shown here is a stereo
view of the final 2F[o] F[c]
electron density map (contoured at 1 ) of the
Tyr106 side chain for the structure of CheY95IV. The outside
conformation of Tyr106 in CheY95IV fits well in this density
(shown in black). For comparison, the inside conformation from
the wild-type structure is displayed in red. Note that this
conformation has a strained C[ ]-C[
]-C[
]angle
of 135°, which is roughly 20° off the ideal value for
this bond angle. Val95 is shown in its two conformations (green
and black lines) as inferred from the electron density at this
position.
F[c]
electron density map (contoured at 1 
) of the
Tyr106 side chain for the structure of CheY95IV. The outside
conformation of Tyr106 in CheY95IV fits well in this density
(shown in black). For comparison, the inside conformation from
the wild-type structure is displayed in red. Note that this
conformation has a strained C[ 
]-C[
]-C[
]angle
of 135°, which is roughly 20° off the ideal value for
this bond angle. Val95 is shown in its two conformations (green
and black lines) as inferred from the electron density at this
position.