2C-Methyl-D-Erythritol-2,4-Cyclodiphosphate Synthase

(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-51   ALA-52  11.5 11.6 -3.3 -7.7 77.0 73.9 10.3
 ALA-52   ALA-53  11.2 11.3 13.0 -11.8 143.6 138.1 3.3
 ALA-53   LEU-54  8.9 8.8 -2.2 8.9 103.2 105.7 -5.5
 LEU-54   GLY-55  6.8 7.0 -15.8 15.8 89.0 86.7 7.0
 GLY-55   ASP-56  3.2 3.5 22.5 -20.4 46.7 46.6 7.9
 ASP-56   ILE-57  1.4 1.5 8.7 -2.1 46.0 44.3 28.2
 ILE-57   GLY-58  0.5 0.5 -2.0 6.6 77.5 75.5 23.7
 GLY-58   LYS-59  4.0 3.9 -24.7 26.3 53.1 61.6 -11.2

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
 GLU-75   LEU-76  3.2 3.6 7.7 -10.7 5.0 6.0 -0.6
 LEU-76   LEU-77  2.4 2.6 -11.1 14.4 112.1 107.1 -8.0
 LEU-77   ARG-78  3.9 4.3 8.0 -12.8 98.5 96.7 4.9

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