Tryptophan Synthase Beta Chain 1

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 GLY-88   GLN-89  5.7 5.8 10.5 -6.5 120.1 120.4 -13.5
 GLN-89   ALA-90  2.3 2.4 -3.5 0.3 115.4 112.4 3.1
 ALA-90   LEU-91  2.0 1.7 3.9 1.0 101.9 100.0 -8.5

Downloading Image

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
i
Residue
i+1
Distance of hinge axis to residue i in conformer 1
(A)
Distance of hinge axis to residue i in conformer 2
(A)
Change in psi (i)
(deg)
Change in phi (i+1)
(deg)
Angle of psi(i) axis to hinge axis conformer 1
(deg)
Angle of psi(i) axis to hinge axis conformer 2
(deg)
Percentage Progress
 HIS-180   TYR-181  5.9 5.9 -13.1 14.2 69.5 71.3 -12.0
 TYR-181   LEU-182  6.5 7.0 -3.6 -3.5 78.2 78.1 24.2
 LEU-182   ILE-183  5.1 5.3 -6.8 1.0 93.7 88.5 33.7
 ILE-183   GLY-184  7.8 8.1 -4.9 -7.8 52.5 58.6 51.1

Downloading Image

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