Cyclohexadienyl Dehydratase

(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
 ASP-123   GLY-124  4.9 5.0 -6.8 24.9 138.7 139.8 158.9
 GLY-124   LYS-125  2.8 2.6 1.0 -5.7 88.7 89.5 -4.0
 LYS-125   THR-126  0.8 1.0 -8.2 3.8 62.0 63.0 20.5

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
 ALA-211   VAL-212  7.2 7.6 4.3 -28.0 93.3 97.1 -23.3
 VAL-212   HIS-213  8.1 8.4 -15.7 168.8 100.5 87.9 386.8
 HIS-213   PRO-214  7.2 7.4 -13.5 6.2 84.9 76.6 -15.8
 PRO-214   GLN-215  10.1 3.6 163.4 -38.9 66.8 88.3 -538.0
 PRO-217   PHE-218  7.9 4.6 14.8 11.7 157.8 146.2 -162.5
 PHE-218   ASP-219  6.5 5.7 12.0 21.1 139.9 121.7 -244.1
 ASP-219   PHE-220  4.8 5.0 34.5 3.0 57.6 52.1 186.9
 PHE-220   ALA-221  6.4 6.7 -5.9 1.8 66.3 67.1 4.4
 ALA-221   GLU-222  6.9 7.0 -5.2 6.0 141.2 138.9 -18.2

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