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
7.4
-3.9
4.1
48.5
45.3
3.2
PRO-241
ALA-242
7.2
7.2
-18.4
5.7
70.8
76.1
15.2
ALA-242
ALA-243
4.5
4.0
5.0
-8.0
130.3
135.9
11.4
ALA-243
GLY-244
1.6
2.0
-15.2
-19.5
64.5
68.2
25.7
GLY-244
THR-245
2.0
2.2
40.7
1.9
63.5
54.6
45.8
THR-245
GLN-246
5.2
5.5
7.4
-1.4
66.4
63.6
-2.1
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
11.5
-12.2
100.2
102.9
2.1
MET-483
SER-484
7.1
7.2
-2.0
0.6
133.2
133.5
0.2
SER-484
GLY-485
3.8
3.9
-18.9
-23.2
49.5
47.5
54.3
GLY-485
ALA-486
1.1
1.9
24.8
-29.0
98.5
77.2
9.6
ALA-486
TRP-487
2.6
3.0
10.8
17.3
68.1
82.6
16.2
TRP-487
MET-488
6.0
6.6
-43.4
31.1
34.4
31.7
17.5
MET-488
TYR-489
8.3
8.1
7.1
5.7
78.8
77.1
5.9
TYR-489
GLN-490
11.4
11.5
7.2
-1.5
144.9
143.6
-9.0
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