Figure 5.
Fig. 5. Stereoviews of the polypeptide backbone fold in
OmpX. (a) Superposition of the 20 DYANA conformers that were
selected to represent the NMR structure of OmpX. The
superposition is for pairwise global best fit of the N, C^ , and
C' backbone atoms of the -sheet amino
acid residues in conformers 2-20 with the corresponding atoms in
the conformer with the smallest residual target function value
(Table 1). (b) Comparison of the mean NMR structure (blue) and
the x-ray crystal structure (red) after superposition as in a.
Periplasmatic and extracellular spaces are indicated according
to ref. 23. The figure was prepared with the program MOLMOL (43).
, and
C' backbone atoms of the 
-sheet amino
acid residues in conformers 2-20 with the corresponding atoms in
the conformer with the smallest residual target function value
(Table 1). (b) Comparison of the mean NMR structure (blue) and
the x-ray crystal structure (red) after superposition as in a.
Periplasmatic and extracellular spaces are indicated according
to ref. 23. The figure was prepared with the program MOLMOL (43).