Molybdopterin Biosynthesis Protein Moea

(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
 PRO-51   GLY-52  15.1 15.1 -1.1 -7.2 77.7 81.5 17.7
 GLY-52   PHE-53  11.3 11.4 3.7 -8.7 151.6 142.7 79.9
 PHE-53   ASP-54  11.9 12.0 12.9 -17.6 121.2 123.3 -4.0
 ASP-54   ASN-55  14.4 14.3 4.5 -7.5 70.8 71.8 -7.3

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
 ARG-138   ARG-139  15.7 16.0 -7.3 -10.1 29.6 35.0 93.2
 ARG-139   GLY-140  13.4 13.3 -8.7 3.6 78.6 88.5 -23.7
 GLY-140   GLU-141  14.9 14.6 2.2 10.6 77.9 72.7 46.1
 GLU-141   ASP-142  18.3 18.1 12.2 -20.3 135.7 137.1 -20.6

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