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Figure 6.
Fig. 6. Residues h55-h58 of CGP
50,856 (solid bonds) with electron
density in the exosite of thrombin
(open bonds). The 2.2 2F0 - F,, UA
(Read, 1986) electrondensitycon-
toured at 1 rms above the meanslowly
fades away beyond theamino side of
residue h55, implying that the Pro-
(Gly), linker of CGP 50,856 as well
as residuh5extends out into the sol-
vent in some disorderly fashionafter
being cleaved. The side chain fh55-
Aspcouldalsonotbeinterpreted
from the electron density.
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