Nucleocapsid 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
SER-392
GLY-393
18.1
17.5
-24.8
49.2
40.3
49.5
-82.7
GLY-393
GLY-394
15.2
14.7
-7.9
-75.2
67.3
50.7
203.4
GLY-394
ASN-395
13.3
13.5
-25.6
-13.0
129.8
109.6
-130.8
ASN-395
THR-396
13.3
10.6
62.1
24.7
82.9
121.7
-136.4
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
MET-426
ALA-427
11.1
9.1
0.3
15.1
157.8
164.2
-68.3
ALA-427
ALA-428
10.2
9.2
-40.1
98.1
49.3
56.5
-111.8
SER-438
ASP-439
6.7
8.7
-112.0
22.8
105.4
91.5
-144.9
ASP-439
MET-440
6.2
7.7
-6.0
9.0
134.2
113.7
-48.7
MET-440
ARG-441
3.9
4.1
21.5
1.1
32.8
27.9
141.0
ARG-441
THR-442
6.7
6.2
-9.5
22.8
136.8
136.2
28.4
THR-442
GLU-443
6.6
6.3
-0.4
5.9
107.7
105.2
19.1
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