Multifunctional Protein Sur E

(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
 THR-174   ARG-175  6.7 7.1 -1.4 1.2 57.3 55.8 0.2
 ARG-175   CYS-176  5.2 5.0 11.6 -20.1 52.5 58.2 -7.7
 CYS-176   GLY-177  6.1 5.5 11.9 -3.8 105.7 114.6 -24.0

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


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
 ASP-213   PHE-214  7.5 7.2 -2.4 7.4 45.4 50.5 -1.4
 PHE-214   ALA-215  10.4 10.2 -8.1 13.7 78.9 78.5 1.8
 ALA-215   ALA-216  12.8 12.6 -8.3 6.0 61.5 49.3 9.8

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