Tryptophan Synthase

(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-93   GLN-94  7.4 7.4 1.7 -5.8 64.5 60.5 16.0
 GLN-94   ALA-95  3.9 3.9 6.7 -1.2 119.2 118.1 10.9
 ALA-95   LEU-96  3.3 3.5 -0.9 0.5 102.1 104.2 -14.4
 LEU-96   LEU-97  7.0 7.2 -5.1 6.1 154.2 159.1 25.0
 LEU-97   ALA-98  6.0 6.3 2.0 -1.7 93.1 90.5 10.4

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-185   TYR-186  5.0 4.7 -3.4 9.4 102.0 103.2 23.4
 TYR-186   MET-187  5.2 4.8 3.3 -2.0 78.4 76.4 12.8
 MET-187   LEU-188  3.9 3.7 18.5 -15.8 96.6 100.2 -2.2

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