Figure 3.
FIG. 3. Stereo view of the same conformer as in Fig. 2 in
ribbon presentation. Only structure 2 is shown. Cysteines and
disulfide bonds are shown in yellow and Pro12 is in aquamarine.
Disulfide bonds (Cys2-Cys18, Cys6-Cys14 and Cys10-Cys19) as well
as the conserved Pro12 are indicated in ball-and-stick
representation. Dashed lines indicate the hydrogen bonds
identified by MOLMOL. These are bonds between Val5 (O) and Gln9
(HN), Val11 (O) and Cys14 (HN), and Pro15 (O) and Cys18 (HN).
The first H-bond belongs to the -helix, others belong
to the three different turns. Pro12 induces a I turn
from residues 11 to 14. All proline residues in the structure
can be shown to be in trans conformation from experimental
nuclear Overhauser effect distance information.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2004,
279,
30395-30401)
copyright 2004.
-helix, others belong
to the three different turns. Pro12 induces a 
I turn
from residues 11 to 14. All proline residues in the structure
can be shown to be in trans conformation from experimental
nuclear Overhauser effect distance information.