Figure 2.
Figure 2. Structure of TM0160. (A) Topology diagram of the
overall fold of TM0160. The long mixed -sheet is
shaded cyan. The dimerization helix (H2) is shaded yellow, while
the highly mobile C-terminal epitope tag helix (H5) in molecule
A is shaded red; all other helices are shaded green. The picture
was generated by TOPS (Westhead et al. 1999) and Topdraw (Bond
2003). (B) Stereo diagram of the TM0160 monomer generated by VMD
(Humphrey et al. 1996). C atom numbering
is every 20 residues. (C) Two orthogonal ribbon diagram
representation of the TM0160 dimer. The interchain disulfide is
depicted in a ball-and-stick representation and sits on the
molecular twofold displayed as an arrow in the top diagram and
as an oval in the bottom. The ribbon is colored from blue to
green in subunit A and green to red in subunit B. The figure was
generated using Bobscript (Kraulis 1991; Esnouf 1997) and
Raster3d (Meritt and Murphy 1994). (D) Representative 2Fo-Fc
electron density. The electron density of the region around the
molecular twofold axis details the interchain disulfide bond.
The electron density map is contoured at 1.5 standard deviations
above the mean.
The above figure is reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
3187-3199)
copyright 2004.
-sheet is
shaded cyan. The dimerization helix (H2) is shaded yellow, while
the highly mobile C-terminal epitope tag helix (H5) in molecule
A is shaded red; all other helices are shaded green. The picture
was generated by TOPS (Westhead et al. 1999) and Topdraw (Bond
2003). (B) Stereo diagram of the TM0160 monomer generated by VMD
(Humphrey et al. 1996). C 
atom numbering
is every 20 residues. (C) Two orthogonal ribbon diagram
representation of the TM0160 dimer. The interchain disulfide is
depicted in a ball-and-stick representation and sits on the
molecular twofold displayed as an arrow in the top diagram and
as an oval in the bottom. The ribbon is colored from blue to
green in subunit A and green to red in subunit B. The figure was
generated using Bobscript (Kraulis 1991; Esnouf 1997) and
Raster3d (Meritt and Murphy 1994). (D) Representative 2Fo-Fc
electron density. The electron density of the region around the
molecular twofold axis details the interchain disulfide bond.
The electron density map is contoured at 1.5 standard deviations
above the mean.