Capsid 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
PHE-2218
LEU-2219
15.1
14.4
-2.9
2.6
22.9
24.5
5.0
LEU-2219
VAL-2220
13.5
12.9
-12.0
15.4
53.6
57.0
-16.4
VAL-2220
PRO-2221
15.8
15.2
-5.1
-3.2
19.2
26.0
65.8
PRO-2221
PRO-2222
15.7
14.9
15.1
1.3
111.2
120.7
13.6
PRO-2222
THR-2223
13.2
12.8
65.7
-94.2
146.6
141.0
131.5
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
PHE-2503
VAL-2504
21.6
21.3
-2.5
6.7
50.5
46.7
-13.2
VAL-2504
SER-2505
22.8
22.2
-4.6
-1.5
18.8
24.1
36.3
SER-2505
TRP-2506
24.1
23.5
10.3
-5.6
88.7
90.7
-10.8
TRP-2506
VAL-2507
26.3
26.1
-27.6
45.0
68.8
64.7
-24.1
VAL-2507
SER-2508
29.8
29.3
-6.3
-6.7
80.3
62.0
57.1
SER-2508
ARG-2509
33.3
32.3
17.0
-17.6
33.5
56.3
1.4
ARG-2509
PHE-2510
36.0
36.0
6.0
13.1
72.0
78.9
61.3
PHE-2510
TYR-2511
37.7
36.9
-30.6
-0.9
98.8
134.1
-80.6
TYR-2511
GLN-2512
35.0
34.6
-6.8
-11.0
146.7
147.5
-47.5
GLN-2512
LEU-2513
37.0
36.6
3.5
9.1
53.8
47.8
50.9
LEU-2513
LYS-2514
35.1
34.8
-2.5
0.9
114.6
113.1
15.3
LYS-2514
PRO-2515
35.7
35.0
-4.4
-2.0
162.5
161.1
-45.1
PRO-2515
VAL-2516
37.4
36.9
-10.4
1.7
130.5
133.0
-61.7
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