Figure 2.
Figure 2. A, Stereo view of the bundle of 20 energy-minimized
CYANA conformers representing the structure of
neurabin[986-1056] (PDB ID 2GLE). The superposition is the best
fit of the backbone atoms N, C^ ,
C of
residues 4-70. Side chains with low local RMSD (<0.7) within the
bundle are shown in cyan. Side chains of residues with high
local RMSD (>0.7) are shown in green. Backbones are shown in
dark blue. Aromatic heavy side chains are colored in orange. The
local RMSD of Trp7, Trp15, Tyr24, and Phe28 are 0.31, 0.11,
0.87, and 0.62, respectively. B, Electrostatic surface of the
neurabin SAM domain (left) and 180° rotation around x-axes
(right). Red represents negative charges and blue positive
charges. C, Ribbon presentation of the closest conformer to the
mean coordinates of the bundle of 20 conformers used to
represent the NMR structure of the neurabin SAM (left) and the
shank3 SAM domain (right). The regular secondary structure
elements are identified.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
69,
192-198)
copyright 2007.
,
C 
of
residues 4-70. Side chains with low local RMSD (<0.7) within the
bundle are shown in cyan. Side chains of residues with high
local RMSD (>0.7) are shown in green. Backbones are shown in
dark blue. Aromatic heavy side chains are colored in orange. The
local RMSD of Trp7, Trp15, Tyr24, and Phe28 are 0.31, 0.11,
0.87, and 0.62, respectively. B, Electrostatic surface of the
neurabin SAM domain (left) and 180° rotation around x-axes
(right). Red represents negative charges and blue positive
charges. C, Ribbon presentation of the closest conformer to the
mean coordinates of the bundle of 20 conformers used to
represent the NMR structure of the neurabin SAM (left) and the
shank3 SAM domain (right). The regular secondary structure
elements are identified.