Adenylate Kinase Isoenzyme-2
(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
ARG-138
ARG-139
1.5
1.5
7.5
-12.7
126.7
127.7
14.3
ARG-139
ILE-140
4.1
2.5
16.6
-33.8
156.9
147.5
24.8
ILE-140
THR-141
2.1
2.2
0.5
14.5
94.0
86.8
-6.8
THR-141
GLY-142
3.8
5.2
0.2
2.2
76.0
76.1
0.9
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
PRO-172
LEU-173
19.9
20.0
-7.5
12.4
103.4
106.9
-7.4
LEU-173
ILE-174
16.2
16.3
14.9
-20.6
90.3
90.1
-0.7
ILE-174
ARG-175
14.1
13.9
32.0
-38.1
118.4
108.7
20.6
ARG-175
ARG-176
11.4
10.7
-7.6
24.6
127.7
145.2
27.6
ARG-176
SER-177
7.9
8.3
116.3
12.0
119.4
101.7
-78.6
SER-177
ASP-178
8.6
9.0
-94.9
44.7
126.2
64.5
-48.1
ASP-178
ASP-179
8.0
5.7
-89.9
-10.8
64.2
11.6
192.3
ASP-179
ASN-180
7.2
5.4
-112.4
57.8
109.5
51.4
49.7
ASN-180
LYS-181
8.0
8.6
85.3
-8.2
125.9
126.6
-83.2
LYS-181
LYS-182
7.2
8.4
-15.9
3.8
93.5
105.1
2.5
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