Chitin Oligosaccharide Binding Protein
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
TYR-240
PRO-241
7.2
7.3
-2.6
2.9
48.5
45.7
3.2
PRO-241
ALA-242
7.2
7.2
-18.5
4.8
70.8
75.6
16.4
ALA-242
ALA-243
4.5
4.0
3.0
-5.7
130.3
136.8
10.0
ALA-243
GLY-244
1.6
2.0
-16.0
-17.0
64.5
68.3
26.4
GLY-244
THR-245
2.0
2.2
41.1
-0.4
63.5
54.0
45.0
THR-245
GLN-246
5.2
5.5
7.2
-1.7
66.4
64.1
-1.6
Graph shows rotational transition at bending residues and can be used
to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
VAL-482
MET-483
10.7
10.8
11.3
-12.1
100.2
102.5
1.2
MET-483
SER-484
7.1
7.2
-1.5
0.0
133.2
133.1
1.0
SER-484
GLY-485
3.8
3.9
-19.2
-21.9
49.5
47.8
53.8
GLY-485
ALA-486
1.1
1.9
24.0
-29.1
98.5
77.3
10.2
ALA-486
TRP-487
2.6
3.0
11.9
16.4
68.0
82.8
16.4
TRP-487
MET-488
6.0
6.6
-44.0
31.5
34.4
32.1
18.5
MET-488
TYR-489
8.3
8.1
5.3
6.8
78.8
77.0
4.1
TYR-489
GLN-490
11.4
11.5
7.3
-2.2
144.9
144.0
-7.7
Graph shows rotational transition at bending residues and can be used
to identify hinge bending residues.
Probably only informative for interdomain rotations greater than 20 degrees