Zinc-Alpha-2-Glycoprotein

(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-52   LEU-53  11.3 10.7 13.3 -19.9 90.6 91.1 -52.8
 LEU-53   TRP-54  10.1 9.8 2.9 6.5 148.8 151.4 -16.6
 TRP-54   ARG-55  10.6 10.3 -13.1 5.9 74.2 78.5 105.6
 ARG-55   GLN-56  14.3 13.9 8.1 -22.4 88.2 89.2 -16.5
 GLN-56   VAL-57  15.1 15.0 5.7 7.8 132.7 128.7 -135.4

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
 ILE-180   LEU-181  6.3 5.9 7.9 -9.5 80.9 80.8 11.0
 LEU-181   ASP-182  3.5 3.3 2.3 -7.3 53.0 51.3 -56.6
 ASP-182   ARG-183  6.4 6.1 -5.8 10.7 167.6 166.9 82.1
 ARG-183   GLN-184  5.7 5.6 0.3 1.0 54.6 48.0 -32.2
 GLN-184   ASP-185  5.6 5.7 1.4 -3.4 32.0 34.5 5.9

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