Figure 1.
Figure 1. (a) The monomer structure of XC5848 color-coded from
blue (N-terminal) to red (C-terminal). Distinct interactions
between the N-terminal residues with the extended 3/
2
hairpin
were circled in red and shown expanded in (b). (b) The 10
N-terminal residues were marked in blue, while other residues in
red. The conventional H-bonds/salt-bridges were annotated in
dotted green lines, while unconventional CH bonds
in dotted gray lines. The unique bonding force at the N-terminal
region are: (1) K3C O
R55H^N;
(2) Y4OH R55NH;
(3) Y4OH R59O^
;
(4) A5H^N R55C
O;
(5) H7C O
N64N^
;
(6) Y9H^N S63C
O;
(7) Y9C O
S63H^N;
(8) Y9OH D84O^
;
(9) T10C O
Q12H^N;
(10) W82C^ 3H
Y54;
(11) P6C^ H
W82.
(c) The dimer structure of XC5858. The interface is mainly
comprised of helix-helix interactions, which were shown expanded
in (d). (d) The interaction forces at this interface: (1) K23N^
E19O^
;
(2) H20N^ E19O^
;
(3) H20N^ Q12O^
and
vice versa.
The above figure is reprinted
by permission from John Wiley & Sons, Inc.:
Proteins
(2007,
68,
1006-1010)
copyright 2007.
3/
hairpin
were circled in red and shown expanded in (b). (b) The 10
N-terminal residues were marked in blue, while other residues in
red. The conventional H-bonds/salt-bridges were annotated in
dotted green lines, while unconventional CH 
bonds
in dotted gray lines. The unique bonding force at the N-terminal
region are: (1) K3C 
O
;
(4) A5H^N 
;
(6) Y9H^N 
3H