Lysr-Type Regulatory 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
GLY-79
ASP-80
9.4
9.7
34.4
2.1
38.4
23.8
21.2
ASP-80
ARG-81
8.3
9.2
-26.6
11.4
96.1
95.2
-4.4
ARG-81
SER-82
5.5
5.7
-12.7
27.5
56.8
60.7
-10.8
SER-82
ARG-83
3.9
5.0
-7.9
-7.8
114.8
122.5
-4.6
ARG-83
ALA-84
6.2
7.2
-39.6
60.9
152.4
152.2
11.2
ALA-84
ALA-85
3.7
5.2
-3.0
-2.8
79.7
77.6
-4.4
ALA-85
ALA-86
1.6
3.1
-8.0
2.5
76.6
79.6
-1.1
ALA-86
ARG-87
5.2
6.7
10.4
-16.8
31.9
32.7
-2.4
ARG-87
GLY-88
6.3
7.8
-6.7
-1.6
117.6
125.1
-1.2
GLY-88
ASP-89
5.3
5.7
39.6
-17.5
52.4
40.1
12.9
ASP-89
VAL-90
2.3
3.3
-169.2
-54.9
70.3
81.7
35.2
VAL-90
GLY-91
1.9
0.7
-176.9
45.7
73.6
65.6
53.7
GLY-91
GLU-92
3.5
4.2
-33.3
-6.0
119.7
133.0
-10.6
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