Figure 3.
Fig. 3. Stereo views of the solution structure of
VVVV2KE. (A)Superposition of the 20 conformers representing the
NMR structure of VVVV2KE (left panel) and single conformer
closest to the average structure (right panel). The line
drawings include all heavy atoms. -Carbon
positions are identified by spheres, and the location of
approximately every tenth residue is labeled by its number in
the amino acid sequence. (B) Stereo views of the N-cap (left
panel) and C-cap (right panel) in the NMR structure of VVVV2KE.
The backbone atoms of the first five and last six residues,
respectively, were superimposed for minimum r.m.s.d. Only bonds
with backbone atoms and backbone carbonyl atoms are displayed,
except for the side chain of Asp1. The N- and C-terminal ends
are identified and hydrogen bonds drawn with dotted lines. The
N-cap hydrogen bond between the carboxyl group of Asp1 and the
backbone amide of Ser4 is identified in bold.
The above figure is reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2002,
269,
1259-1266)
copyright 2002.
-Carbon
positions are identified by spheres, and the location of
approximately every tenth residue is labeled by its number in
the amino acid sequence. (B) Stereo views of the N-cap (left
panel) and C-cap (right panel) in the NMR structure of VVVV2KE.
The backbone atoms of the first five and last six residues,
respectively, were superimposed for minimum r.m.s.d. Only bonds
with backbone atoms and backbone carbonyl atoms are displayed,
except for the side chain of Asp1. The N- and C-terminal ends
are identified and hydrogen bonds drawn with dotted lines. The
N-cap hydrogen bond between the carboxyl group of Asp1 and the
backbone amide of Ser4 is identified in bold.