Serine/threonine-Protein Phosphatase 2A 56 Kda Regulatory Subunit Gamma Isoform
(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
LEU-225
GLU-226
3.5
3.5
-3.1
5.0
57.5
60.7
8.3
GLU-226
ILE-227
5.9
6.0
-3.3
4.4
61.9
57.7
-5.6
ILE-227
LEU-228
8.4
8.5
-20.0
9.6
39.8
32.0
72.2
LEU-228
GLY-229
6.4
6.7
6.3
6.3
141.9
134.5
-99.2
GLY-229
SER-230
5.0
5.2
-12.9
1.9
51.8
46.5
61.7
SER-230
ILE-231
8.6
8.6
0.3
0.6
115.7
120.2
52.8
ILE-231
ILE-232
9.3
9.3
-9.9
11.2
38.3
37.5
-32.1
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
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
TYR-263
HIS-264
3.4
3.4
14.0
-4.8
27.3
26.0
65.0
HIS-264
PRO-265
5.9
6.0
-11.1
3.5
138.6
136.6
-48.6
PRO-265
GLN-266
6.7
6.6
-9.2
13.9
117.0
114.2
-9.9
GLN-266
LEU-267
3.6
3.5
-15.5
10.0
118.6
123.8
-19.8
LEU-267
ALA-268
2.7
2.4
-6.8
12.5
153.5
149.1
21.4
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