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Figure 4.
Figure 4. Close up view of the hydrogen bond network around
the buried Asp19 and the adjacent loop Ile25-Arg30. (a) The
consensus structure found in ten out of 13 monomers, with the
peptide bond preceding Pro28 in the cis conformation. Shown is
monomer A of the tetragonal crystal form. (b) The same region in
the monoclinic crystal. (c) The same region in monomers E and G
of the orthorhombic crystal (monomer E is shown). The peptide
bond preceding Pro28 in (b) and (c) is in the trans
conformation. The conformational changes that are observed in
this loop have very little effect on the solvent accessibility
of the buried side-chains of Asp19, Gln21 and Arg31. The
electron density maps correspond with the 2 F[o] -F[c]maps of
the final refined models. A number of side-chains and their
corresponding electron density were omitted for clarity.
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