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  11.9 11.9 2.0 -2.3 99.8 104.0 -10.0
 ALA-52   ALA-53  11.7 11.5 0.5 -13.7 146.5 148.4 44.4
 ALA-53   LEU-54  9.7 9.7 2.7 0.8 79.4 78.0 -37.3
 LEU-54   GLY-55  7.5 7.6 -13.9 14.5 83.3 85.0 16.7
 GLY-55   ASP-56  4.1 4.2 26.9 -21.4 50.2 48.5 9.1
 ASP-56   ILE-57  1.6 1.8 9.2 3.3 48.7 49.3 61.2
 ILE-57   GLY-58  0.5 0.7 -5.5 13.5 73.0 65.4 -24.5

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
 ARG-74   GLU-75  1.3 1.2 -0.1 12.4 102.8 102.2 0.2
 GLU-75   LEU-76  2.9 3.2 4.5 -11.9 9.5 14.8 -15.9
 LEU-76   LEU-77  2.4 2.7 -10.4 18.1 107.5 101.1 -1.5
 LEU-77   ARG-78  3.3 3.6 3.4 -12.9 103.5 103.7 2.1
 ARG-78   GLU-79  6.0 6.3 9.3 -12.7 53.5 52.4 -10.9

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