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
 ILE-180   LEU-181  7.2 7.6 -6.5 4.7 83.0 81.6 28.9
 LEU-181   ASP-182  4.4 4.5 -1.6 7.3 53.8 55.7 -76.1
 ASP-182   ARG-183  6.9 7.1 5.5 -13.2 169.3 171.0 92.8
 ARG-183   GLN-184  6.7 6.7 -2.8 3.0 50.4 54.3 -1.7
 GLN-184   ASP-185  6.5 6.4 3.9 2.4 148.2 150.0 -47.2

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


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-236   ASN-237  9.9 10.1 5.2 -12.8 139.0 141.9 37.1
 ASN-237   GLY-238  9.5 10.1 16.0 -12.7 91.3 94.3 13.9
 GLY-238   ASN-239  12.0 12.5 -18.5 19.7 126.6 123.2 -11.8
 ASN-239   GLY-240  10.1 10.7 11.2 -22.3 102.5 109.9 -26.4
 GLY-240   THR-241  6.5 7.3 23.5 -14.8 38.2 43.0 70.1

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