Ure2 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
 ALA-262   LEU-263  7.8 7.9 12.0 -10.7 47.5 52.2 -2.8
 LEU-263   ALA-264  6.4 6.5 15.2 -6.5 63.1 62.4 11.6
 ALA-264   GLU-265  6.2 6.0 -0.3 -4.1 55.2 56.9 21.5
 GLU-265   ARG-266  5.3 4.5 4.5 1.6 90.0 87.1 2.4
 ARG-266   ARG-267  1.7 1.8 -1.2 7.2 150.3 149.8 27.3

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
 PHE-294   PHE-295  4.4 5.4 -32.6 12.7 99.6 98.2 -29.6
 PHE-295   ASP-296  0.7 1.7 8.4 -7.3 85.3 90.7 -13.0
 ASP-296   TYR-297  3.9 4.3 -9.6 5.8 126.6 123.1 -8.7
 TYR-297   PRO-298  5.6 6.6 18.9 0.6 45.3 43.6 77.2

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