Figure 2.
Figure 2. Hydrogen-bond networks in the domain-swapped NrdH
dimer. A: The dimer interface. The -sheet
of the interface is formed by the residues 48-50 of both
domain-swapped monomers. The residues D37*, R40*, D40, and D41
of both 2
helices form a hydrogen-bond network. The molecule has the same
orientation as in Figure 1(A-D). B: View of the hydrogen-bond
network in the structure of C. ammonigenes NrdH formed by the
highly conserved WSGRFP sequence motif. Hydrogen bonds are drawn
as dashed lines.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
55,
613-619)
copyright 2004.
-sheet
of the interface is formed by the residues 48-50 of both
domain-swapped monomers. The residues D37*, R40*, D40, and D41
of both 
2
helices form a hydrogen-bond network. The molecule has the same
orientation as in Figure 1(A-D). B: View of the hydrogen-bond
network in the structure of C. ammonigenes NrdH formed by the
highly conserved WSGRFP sequence motif. Hydrogen bonds are drawn
as dashed lines.