Mitogen-Activated Protein Kinase 14
(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-240
THR-241
4.6
5.4
0.1
0.9
147.3
140.5
-20.9
THR-241
PRO-242
6.1
6.6
-10.4
-25.4
55.3
63.1
115.2
PRO-242
GLY-243
4.7
4.6
17.1
-8.7
71.9
81.7
36.9
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
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-260
SER-261
13.4
12.4
13.8
-27.2
137.2
131.0
63.0
SER-261
LEU-262
16.0
15.7
72.4
-49.6
139.2
134.0
-120.8
LEU-262
THR-263
13.5
14.6
-6.2
-3.0
33.6
22.5
40.9
THR-263
GLN-264
12.6
15.1
-8.2
34.6
98.7
72.0
-60.5
GLN-264
MET-265
9.2
11.5
9.7
-2.4
133.6
92.8
3.2
MET-265
PRO-266
6.8
9.2
-35.6
-4.3
100.5
80.0
-6.7
PRO-266
LYS-267
3.1
5.9
-27.6
7.7
105.2
115.3
12.8
LYS-267
MET-268
2.6
4.3
-4.2
-20.7
31.9
38.5
83.3
MET-268
ASN-269
5.4
6.8
10.2
-1.7
93.3
90.4
-30.4
ASN-269
PHE-270
6.8
7.7
-10.7
9.9
99.4
108.9
-51.8
PHE-270
ALA-271
10.2
10.7
3.4
-3.9
131.3
136.7
-20.1
ALA-271
ASN-272
12.2
11.8
-10.3
14.0
54.7
56.7
1.2
ASN-272
VAL-273
11.4
11.8
-40.0
33.3
116.2
119.3
82.3
VAL-273
PHE-274
13.2
13.5
-5.3
1.7
96.5
95.8
4.9
PHE-274
ILE-275
15.9
16.0
-35.2
14.5
36.7
41.4
156.6
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