Figure 1.
Figure 1. Schematic drawings of the three-dimensional structure
of C. ammoniagenes NrdH. The nomenclature of Martin (1995)[7]
was used for the helices and sheets and does not include the
-sheet
of the dimer-interface. The redox active cysteine residues at
the N-terminal of helix 1
are shown as ball-and-stick models. A: Closed monomer. B: Open
monomer. C: Domain-swapped dimer, colored according to the
B-factors from light blue (20 Å^2) to red (45 Å^2)
as indicated on the reference bar. D: surface representation of
the domain-swapped dimer. The surface was calculated with
program MolMol[22] using a solvent radius of 1.4 Å and
colored according to the electrostatic potential, calculated
with the program s
simplecharge
option.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2004,
55,
613-619)
copyright 2004.
-sheet
of the dimer-interface. The redox active cysteine residues at
the N-terminal of helix 
1
are shown as ball-and-stick models. A: Closed monomer. B: Open
monomer. C: Domain-swapped dimer, colored according to the
B-factors from light blue (20 Å^2) to red (45 Å^2)
as indicated on the reference bar. D: surface representation of
the domain-swapped dimer. The surface was calculated with
program MolMol[22] using a solvent radius of 1.4 Å and
colored according to the electrostatic potential, calculated
with the program 
s
simplecharge
option.