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Figure 9.
Figure 9. (a) Stereo ribbon diagrams of superpositions of the
structures of AP-B and AP-A. For each molecule, the structure
closest to the geometric average is shown. Structures were
superimposed over the backbone heavy atoms of residues 2–7 and
18–49, corresponding to the well-defined region of AP-B.
Colours are as follows: mauve/pink indicates the well-defined
region of AP-B, magenta the poorly defined loop; turquoise
indicates the well-defined region of AP-A, purple the poorly
defined loop. The side chains of Asp7, Asp9, Lys37, His39 and
Lys48 are shown in white in AP-B and red in AP-A. (b) Stereoview
of the structure of AP-B closest to the geometric average and
showing the positions of some of the residues (Asp7, Asp9,
Arg12, Asn35, Lys37, His39 and Lys48 coloured magenta) thought
to contribute to the receptor-binding surface of the molecule
(see text). A Connolly surface generated with a probe radius of
1.4 å is shown; the orientation of the molecule is the
same as in Figure 5. Figure 9. (a) Stereo ribbon diagrams of
superpositions of the structures of AP-B and AP-A. For each
molecule, the structure closest to the geometric average is
shown. Structures were superimposed over the backbone heavy
atoms of residues 2–7 and 18–49, corresponding to the
well-defined region of AP-B. Colours are as follows: mauve/pink
indicates the well-defined region of AP-B, magenta the poorly
defined loop; turquoise indicates the well-defined region of
AP-A, purple the poorly defined loop. The side chains of Asp7,
Asp9, Lys37, His39 and Lys48 are shown in white in AP-B and red
in AP-A. (b) Stereoview of the structure of AP-B closest to the
geometric average and showing the positions of some of the
residues (Asp7, Asp9, Arg12, Asn35, Lys37, His39 and Lys48
coloured magenta) thought to contribute to the receptor-binding
surface of the molecule (see text). A Connolly surface generated
with a probe radius of 1.4 å is shown; the orientation of
the molecule is the same as in [4]Figure 5.
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