Tryptophan Synthase Beta Chain 1
(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-88
GLN-89
7.3
7.2
4.7
-0.4
115.0
114.2
-17.0
GLN-89
ALA-90
3.7
3.6
-3.2
2.8
119.9
119.4
25.7
ALA-90
LEU-91
2.9
2.7
1.0
-0.9
100.8
101.2
-27.1
LEU-91
LEU-92
6.6
6.3
6.7
-11.2
158.0
157.4
41.4
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
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
HIS-180
TYR-181
4.4
4.7
-17.1
18.1
71.6
72.4
7.1
TYR-181
LEU-182
5.4
5.9
-18.2
17.0
84.6
83.8
45.0
LEU-182
ILE-183
4.5
4.5
-10.0
4.3
94.0
91.6
43.8
ILE-183
GLY-184
7.6
7.8
0.0
-0.3
59.5
64.6
-8.3
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