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
9.0
8.9
2.6
-0.3
54.1
58.1
5.9
ALA-89
ALA-90
6.0
5.8
7.5
-22.0
104.5
110.7
18.5
ALA-90
ASP-91
2.4
2.3
42.5
2.7
71.8
65.7
43.8
ASP-91
SER-92
3.0
1.8
-8.5
-4.1
54.2
74.0
16.3
SER-92
ARG-93
5.1
4.4
-21.6
7.3
64.4
62.3
14.2
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-188
LYS-189
3.5
3.7
-7.1
7.7
59.5
56.7
5.0
LYS-189
TYR-190
2.4
2.8
-13.0
21.2
126.7
122.3
9.6
TYR-190
PHE-191
3.5
4.0
-7.8
12.6
141.0
136.8
23.4
PHE-191
GLY-192
1.1
2.0
0.3
-5.5
99.1
94.9
22.6
GLY-192
ASP-193
2.3
2.1
9.9
-14.9
70.3
57.0
-0.2
ASP-193
GLY-194
5.7
4.9
28.9
-9.1
37.2
44.7
19.4
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