Figure 1.
Fig. 1. A, residual B-factor plot for the wild-type
TRPSIPP (green) and the A169L/ C170WF-IPP
(black) structures (top). The plot of the residual B-factor
ratio (mutant B[fac]/wild-type B[fac]) is shown. Although both
complexes have different mean B-factors, the B-factor comparison
allows the identification of changes within the COMM domain
(bottom). B, C[ ]r.m.s.
deviation (RMSD) of TRPSIPP and A169L/ C179WF-IPP
for the (top) and
(bottom)
subunits. Points I[ ]and I[
]represent
flexible surface residues. The insert shows a detailed view of
the r.m.s. deviation and the secondary structure assignment
within the COMM domain.
The above figure is reprinted
by permission from the ASBMB:
J Biol Chem
(2000,
275,
41058-41063)
copyright 2000.
A169L/ 
]r.m.s.
deviation (RMSD) of TRPSIPP and 
(top) and
]represent
flexible surface residues. The insert shows a detailed view of
the r.m.s. deviation and the secondary structure assignment
within the COMM domain.