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Figure 8.
Figure 8. Stereo view of the back-
bone atoms of N-SH3 residues Ala5
to Asp23 and Lys50 to Ile53. The
Figure shows the SH3 conserved
``AXD'' sequence (Ala5 to
Phe9), the variable RT-loop (resi-
dues Lys10 to Ser18) including the
3 10 helix-like turn at Ala13 to
Glu16, the type II turn at the SH3
conserved ``RGD'' loop (Arg21 to
Asp23), and the conserved 310 helix
(Lys50 to Ile53). Backbone (N, C
a
,
C) atoms (gray); HN (light blue,
unprotected from solvent exchange;
blue, protected from solvent
exchange); O (pink, non-H-bond
acceptor; red, H-bond acceptor);
side-chain carbon atoms (white);
side-chain oxygen atoms (magenta).
The side-chains of residues that
participate in H-bonds (Asp8, Ser18, and Asp23) are shown (see the text). H-bonds are depicted as colored broken
lines: included in the structure calculations as restraints (green); not included as restraints but amide proton donor
protected from solvent exchange and H-bond observed in at least 75% of the chemical shift refined structures (yel-
low); same as yellow but amide proton donor not protected from solvent exchange (white). This Figure was made
with the program INSIGHTII (Molecular Simulations, San Diego CA).
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