Glutamine Binding Protein

(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
 TYR-86   LYS-87  6.9 7.2 2.4 -2.7 127.6 130.2 4.3
 LYS-87   SER-88  4.0 4.8 -6.5 14.2 120.7 119.3 6.3
 SER-88   GLY-89  0.7 1.1 -15.3 -41.1 54.4 47.1 68.8
 GLY-89   LEU-90  3.1 2.7 3.7 12.8 55.3 53.9 11.4

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
 LEU-180   GLU-181  7.4 6.7 -11.8 -0.1 101.1 102.5 12.6
 GLU-181   ALA-182  5.1 4.3 -34.3 -3.5 70.6 66.1 38.2
 ALA-182   GLN-183  1.7 2.0 12.8 23.9 77.3 67.5 43.1
 GLN-183   GLN-184  2.5 2.1 17.3 -10.8 123.2 129.2 -6.3
 GLN-184   TYR-185  5.3 5.3 7.4 -3.8 119.5 119.4 -8.0

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