S-Adenosylhomocysteine Hydrolase
(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
ALA-394
GLU-395
4.0
2.5
-8.2
17.7
46.6
54.7
-41.3
GLU-395
ALA-396
6.6
5.6
-19.2
2.6
21.5
18.6
83.7
ALA-396
HIS-397
7.1
6.0
10.6
-16.4
126.5
127.3
15.9
HIS-397
LEU-398
3.5
2.4
13.3
6.0
100.5
98.3
13.3
LEU-398
GLY-399
5.0
4.3
165.8
-166.1
149.6
157.0
-0.9
GLY-399
LYS-400
6.6
5.9
10.0
14.2
132.1
132.5
-40.1
LYS-400
LEU-401
3.3
2.8
0.4
-12.7
77.2
83.8
-9.4
LEU-401
ASN-402
4.3
4.6
-3.2
6.1
77.4
83.3
-1.6
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
PHE-424
LYS-425
9.6
10.2
2.8
67.9
131.8
95.2
-151.0
LYS-425
PRO-426
6.7
6.4
-52.6
6.6
47.4
34.1
166.4
PRO-426
ASP-427
5.9
5.1
-14.9
-13.7
103.1
95.1
-23.2
ASP-427
HIS-428
4.8
3.3
16.6
14.1
104.7
117.3
-28.3
HIS-428
TYR-429
1.4
0.6
-41.9
25.1
124.2
135.4
-38.2
TYR-429
ARG-430
1.6
2.1
19.2
-16.4
56.8
74.6
-25.0
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