Coat 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
LYS-244
THR-245
5.4
5.2
-17.7
-6.9
37.2
38.4
108.4
THR-245
ALA-246
2.5
2.1
0.8
2.7
96.4
95.3
-15.3
ALA-246
LYS-247
3.8
3.4
6.4
-1.4
88.2
86.4
-3.6
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
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
GLN-250
ALA-251
11.6
11.7
-3.9
15.3
65.0
67.5
-12.0
ALA-251
SER-252
14.9
15.0
15.7
-0.5
77.1
66.1
22.6
SER-252
ASN-253
18.3
18.3
-88.1
-59.5
38.2
62.3
510.2
ASN-253
ASP-254
18.6
18.3
-11.4
-123.7
99.6
77.6
-108.8
ASP-254
LYS-255
22.4
15.4
68.2
-141.3
44.8
88.2
-171.4
LYS-255
VAL-256
22.5
16.0
0.5
-65.0
92.1
33.4
-297.3
VAL-256
SER-257
19.1
16.8
-79.9
136.7
57.3
116.8
31.1
SER-257
ASP-258
15.8
13.6
-141.4
36.2
46.9
63.2
344.9
ASP-258
GLY-259
13.2
11.3
36.8
0.3
77.5
87.9
69.7
GLY-259
PRO-260
9.7
9.3
-54.4
-8.7
167.9
164.0
-337.3
PRO-260
THR-261
7.9
7.6
5.7
-17.4
55.1
59.9
-41.1
THR-261
TYR-262
10.2
10.1
3.1
-3.8
60.3
58.9
-8.9
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