Figure 2.
Figure 2. Comparison with another structure. (A) Amino acid
sequence alignment of PH0186 and KaiCI from Synechococcus sp.
The secondary structure assignment for PH0186 is indicated by
helices ( -
and 3[10]-helices) and arrows ( -strands).
Each protein contains Walker motifs A and B, and two catalytic
carboxylate Glu residues. (B) Superposition of PH0186 (blue) and
KaiCI (red). (C) The comparative electrostatic potential
diagrams of PH0186 (a), and KaiCI (b). Positive and negative
potentials are represented by blue and red, respectively. The
maximum and the minimum values of electrostatic potentials are
±1 kT/e, respectively. Electrostatic potential of each
protein was calculated using default parameters of APBS.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2009,
75,
1035-1039)
copyright 2009.
-
and 3[10]-helices) and arrows ( 
-strands).
Each protein contains Walker motifs A and B, and two catalytic
carboxylate Glu residues. (B) Superposition of PH0186 (blue) and
KaiCI (red). (C) The comparative electrostatic potential
diagrams of PH0186 (a), and KaiCI (b). Positive and negative
potentials are represented by blue and red, respectively. The
maximum and the minimum values of electrostatic potentials are
±1 kT/e, respectively. Electrostatic potential of each
protein was calculated using default parameters of APBS.