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Figure 5.
Figure 5. Crystal Structure of the N50/C36 Complex
(A)
Ribbon diagram of the N50/C36 complex. The N termini of the N50
(red) and C36 (green) chains are indicated.
(B) Conserved
grooves on the surface of the N50 coiled-coil trimer. The C36
peptides drawn as an atomic model are shown against a surface
representation of the N50 trimer. The view is in approximately
the same orientation as in (A). The solvent-accessible surface
is colored according to the local electrostatic potential;
colors range from dark blue, representing the most positive
area, to deep red, representing the most negative area.
(C)
Cross-section of the N50/C36 complex in the Thr923 layer
showing “x-like” packing of side chains that project
simultaneously toward the 3-fold axis. The 2F[o] − F[c]
electron density map contoured at 1.5σ is shown with the
refined molecular model.
(D) Cross-section of the N50/C36
complex in the Ser919–Leu920 layer showing “y-like”
packing of alternating small and large side chains in a
hexagonal arrangement. Figure 5. Crystal Structure of the
N50/C36 Complex(A) Ribbon diagram of the N50/C36 complex. The N
termini of the N50 (red) and C36 (green) chains are
indicated.(B) Conserved grooves on the surface of the N50
coiled-coil trimer. The C36 peptides drawn as an atomic model
are shown against a surface representation of the N50 trimer.
The view is in approximately the same orientation as in (A). The
solvent-accessible surface is colored according to the local
electrostatic potential; colors range from dark blue,
representing the most positive area, to deep red, representing
the most negative area.(C) Cross-section of the N50/C36 complex
in the Thr923 layer showing “x-like” packing of side chains
that project simultaneously toward the 3-fold axis. The 2F[o]
− F[c] electron density map contoured at 1.5σ is shown with
the refined molecular model.(D) Cross-section of the N50/C36
complex in the Ser919–Leu920 layer showing “y-like”
packing of alternating small and large side chains in a
hexagonal arrangement.
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