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
LEU-385
PRO-386
11.3
11.6
11.1
3.0
70.0
69.8
22.6
PRO-386
LYS-387
11.4
11.1
1.5
0.9
117.7
109.8
-33.1
LYS-387
LYS-388
8.4
7.9
-9.0
11.9
39.6
39.9
-38.3
LYS-388
LEU-389
10.8
10.1
-16.4
9.5
32.9
26.8
50.8
LEU-389
ASP-390
10.7
10.0
3.7
4.6
105.3
102.7
-4.2
ASP-390
GLU-391
7.0
6.4
-17.5
11.5
60.6
58.3
30.5
GLU-391
ALA-392
6.8
5.7
9.7
-4.2
156.2
157.0
-33.4
ALA-392
VAL-393
9.1
7.8
-8.7
23.7
47.5
48.8
-43.3
VAL-393
ALA-394
6.9
5.7
-25.9
5.6
75.7
69.4
55.2
ALA-394
GLU-395
4.0
2.7
-16.9
20.7
46.2
56.1
-20.5
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
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
10.5
10.8
-16.0
87.5
46.0
79.9
-152.9
LYS-425
PRO-426
7.7
7.1
-71.0
21.1
49.1
36.5
174.5
PRO-426
ASP-427
6.8
6.2
-7.3
-26.7
102.8
93.2
-20.5
ASP-427
HIS-428
5.3
3.8
38.4
-8.5
106.8
126.2
-35.2
HIS-428
TYR-429
2.0
1.7
-18.5
0.3
122.0
130.2
-41.2
TYR-429
ARG-430
2.5
2.5
10.7
-6.4
58.0
73.4
-25.4
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