Tryptophan Synthase Alpha Chain
(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
ILE-232
SER-233
8.4
7.8
18.9
-2.7
82.7
72.5
0.8
SER-233
GLY-234
5.2
4.8
-7.9
-38.6
118.1
105.7
-58.8
GLY-234
SER-235
1.9
1.5
123.5
115.5
39.6
62.9
-190.1
SER-235
ALA-236
0.7
2.3
-179.1
11.8
111.9
165.9
465.2
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
ALA-253
ALA-254
5.0
3.6
2.1
-2.9
47.9
53.1
1.6
ALA-254
LEU-255
2.1
1.0
15.6
-4.0
29.5
30.6
25.3
LEU-255
LYS-256
4.3
3.2
-3.6
-4.9
87.9
81.8
8.5
LYS-256
VAL-257
7.4
6.3
-2.7
-6.6
96.5
88.2
2.4
VAL-257
PHE-258
6.7
5.8
1.6
20.4
17.8
26.7
54.3
PHE-258
VAL-259
6.2
5.5
-6.4
8.2
123.4
119.4
-7.4
VAL-259
GLN-260
8.1
7.7
3.8
-2.6
100.9
104.7
-3.7
GLN-260
PRO-261
11.3
10.8
-5.0
3.7
118.2
114.0
1.4
PRO-261
MET-262
12.2
11.8
-8.5
8.0
169.1
169.9
-2.8
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