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
 VAL-45   SER-46  14.5 14.8 -11.8 17.3 60.5 59.2 -16.7
 SER-46   PRO-47  10.9 11.2 -2.6 0.7 52.0 50.6 -6.1
 PRO-47   LEU-48  9.5 10.1 10.7 -32.1 84.7 85.2 -19.6
 LEU-48   ASP-49  6.0 6.4 27.8 -6.5 19.9 27.6 75.2
 ASP-49   VAL-50  3.5 3.7 2.1 -3.7 93.4 95.2 13.5
 VAL-50   PRO-51  3.8 4.3 0.0 -4.0 145.2 143.8 11.4
 PRO-51   GLY-52  3.4 4.0 -2.1 10.8 63.2 64.9 10.1
 GLY-52   PHE-53  1.2 1.6 -0.2 -6.1 94.0 97.3 15.1

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  4.2 4.4 14.8 -8.5 51.2 57.2 55.5
 ARG-139   GLY-140  2.3 1.9 14.2 3.5 117.6 120.7 -28.3
 GLY-140   GLU-141  1.7 1.8 -24.9 9.4 19.0 26.2 53.2
 GLU-141   ASP-142  1.5 2.1 -60.0 81.4 78.1 85.8 17.7
 ASP-142   ILE-143  5.3 5.8 15.5 -47.5 53.7 78.8 -9.4
 ILE-143   SER-144  6.6 6.7 35.5 -17.7 76.5 68.9 -6.7
 SER-144   ALA-145  6.1 6.4 6.9 0.8 44.1 46.2 17.2

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