Nonstructural Protein V
(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-149
ARG-150
17.1
19.2
-74.0
-27.0
115.0
90.0
-42.8
ARG-150
ASP-151
18.4
22.7
9.1
-67.7
46.8
80.0
-12.9
ASP-151
THR-152
15.5
23.8
-116.3
20.9
139.9
95.3
239.0
THR-152
GLY-160
13.9
22.8
100.0
-41.4
69.7
150.0
-26.0
GLY-160
GLY-161
17.2
20.8
-4.7
151.7
154.1
107.6
-127.0
GLY-161
PHE-162
19.1
18.9
139.1
59.9
37.8
83.5
-80.8
PHE-162
HIS-163
18.8
15.6
-28.0
-63.5
77.6
83.2
88.8
HIS-163
ARG-164
20.1
14.2
-42.8
46.3
83.2
107.3
-2.9
ARG-164
ARG-165
18.7
12.1
-26.8
-10.9
102.4
57.0
30.1
ARG-165
GLU-166
20.1
11.5
-16.7
0.3
38.1
111.7
21.3
GLU-166
TYR-167
22.4
12.8
-50.4
74.9
105.0
46.4
-29.3
TYR-167
SER-168
24.1
12.9
16.9
8.4
141.4
73.1
-13.8
SER-168
ILE-169
27.3
16.5
-147.5
-173.5
115.8
50.3
-12.8
ILE-169
GLY-170
29.3
16.4
-112.7
-19.6
51.5
70.5
128.5
GLY-170
TRP-171
32.8
19.7
24.3
55.1
59.0
93.5
-12.7
TRP-171
VAL-172
35.1
21.3
45.5
-0.3
104.1
39.6
-138.8
VAL-172
GLY-173
38.8
22.4
30.9
162.4
47.7
117.3
161.8
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