Lysine, Arginine, Ornithine-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-88
ALA-89
9.1
8.9
-1.4
2.0
125.9
121.4
1.8
ALA-89
ALA-90
6.1
5.9
0.6
-17.3
104.3
107.4
15.2
ALA-90
ASP-91
2.4
2.4
52.1
-5.6
71.9
63.9
47.1
ASP-91
SER-92
3.1
1.8
-10.0
-0.1
54.3
73.7
14.4
SER-92
ARG-93
5.1
4.4
-23.3
10.2
64.2
60.9
16.0
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
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
LYS-189
TYR-190
2.4
2.7
-4.2
15.3
126.6
120.3
17.0
TYR-190
PHE-191
3.4
3.9
-7.3
10.6
140.9
137.0
20.4
PHE-191
GLY-192
1.0
1.9
-1.6
-7.1
80.8
85.2
24.2
GLY-192
ASP-193
2.3
2.0
12.8
-14.4
70.2
55.5
1.7
ASP-193
GLY-194
5.8
5.0
23.6
-6.6
37.3
44.2
12.8
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