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
11.3
11.2
0.4
-4.9
94.2
96.2
-7.0
LEU-235
LYS-236
8.4
8.4
-10.3
-37.6
50.3
49.0
129.3
LYS-236
PRO-237
5.3
5.7
-47.0
-16.1
60.7
86.1
-8.1
PRO-237
GLY-238
3.7
3.1
-151.1
-173.6
112.6
63.4
5.7
GLY-238
THR-239
2.8
1.1
164.6
-1.7
28.0
71.2
-461.5
THR-239
HIS-240
2.1
4.1
144.7
17.0
93.3
34.5
260.3
HIS-240
HIS-241
2.8
5.3
86.5
13.6
51.1
48.7
229.5
HIS-241
THR-242
4.0
4.2
-21.7
1.5
97.4
117.6
-13.9
THR-242
ILE-243
7.6
7.7
-9.9
0.0
151.9
144.0
-33.3
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-308
LYS-309
3.7
3.8
32.4
-27.9
49.3
56.2
-14.6
LYS-309
THR-310
4.1
3.3
36.2
19.6
33.0
37.5
163.0
THR-310
LEU-311
3.0
2.2
-14.2
-21.4
83.4
103.9
-37.3
LEU-311
LEU-312
1.8
1.9
22.7
-8.9
89.8
85.4
-7.3
LEU-312
ASN-313
2.2
3.6
-11.0
14.7
159.0
166.4
17.4
ASN-313
ILE-314
2.7
3.1
-4.1
-7.3
120.8
127.0
-12.1
ILE-314
GLU-315
2.6
2.6
8.2
-1.3
102.0
95.3
-15.1
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