Mrna Capping Enzyme
(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
LYS-234
LEU-235
5.0
5.1
4.0
13.6
122.9
125.3
-15.9
LEU-235
LYS-236
4.2
4.2
0.7
58.9
112.2
122.2
-30.6
LYS-236
PRO-237
6.5
6.5
14.0
-9.8
138.0
98.9
10.1
PRO-237
GLY-238
7.9
8.8
2.0
163.2
150.6
161.2
-606.0
GLY-238
THR-239
5.6
8.1
146.1
15.5
161.2
115.9
800.5
THR-239
HIS-240
7.6
5.8
16.8
39.7
86.5
115.2
-60.4
HIS-240
HIS-241
8.5
7.8
10.4
36.0
82.9
81.3
97.9
HIS-241
THR-242
6.1
6.3
30.4
7.2
152.7
153.9
-164.1
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
GLU-315
GLU-316
4.8
4.7
2.0
0.7
141.1
147.9
41.4
GLU-316
ASN-317
5.8
5.6
-4.6
10.4
78.8
76.3
-32.7
ASN-317
ILE-318
5.4
5.3
1.3
-10.6
156.5
154.0
71.5
ILE-318
THR-319
5.6
5.3
2.1
-7.4
103.9
91.3
18.1
THR-319
ILE-320
7.9
7.5
11.6
-17.7
167.8
164.2
23.8
ILE-320
ASP-321
8.6
8.6
9.8
-9.2
123.3
117.4
31.8
ASP-321
GLU-322
11.3
11.5
17.6
-12.1
94.3
96.6
-66.8
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