Figure 1.
Figure 1. a: F[o]-F[c] omit electron density map contoured at 3
and
final model showing a side view of the heme environment in hh
MbNO. The dashed yellow line represents the 3.0 Å distance
between N^ of
the distal His64 residue and the N atom of the nitrosyl ligand.
Carbon, oxygen, nitrogen, and iron atoms are colored gray, red,
blue, and brown, respectively. b: Top view of the heme in hh
MbNO, with the NO ligand on the side of the porphyrin ring
facing the viewer. The coloring scheme is the same as in (a)
with the exception of the proximal His93 ligand, which is shown
in yellow for clarity.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2003,
53,
182-192)
copyright 2003.
and
final model showing a side view of the heme environment in hh
MbNO. The dashed yellow line represents the 3.0 Å distance
between N^ 
of
the distal His64 residue and the N atom of the nitrosyl ligand.
Carbon, oxygen, nitrogen, and iron atoms are colored gray, red,
blue, and brown, respectively. b: Top view of the heme in hh
MbNO, with the NO ligand on the side of the porphyrin ring
facing the viewer. The coloring scheme is the same as in (a)
with the exception of the proximal His93 ligand, which is shown
in yellow for clarity.