Mrna Decapping Enzyme

(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
 GLU-137   LYS-138  9.9 10.0 -6.3 5.9 158.8 161.3 -0.1
 LYS-138   HIS-139  11.9 12.0 -3.1 -6.7 132.6 130.2 -22.6
 HIS-139   LEU-140  9.6 9.4 15.5 -4.3 84.1 81.6 8.6
 LEU-140   GLN-141  6.5 6.7 -11.6 2.0 120.6 132.0 -20.4
 GLN-141   LYS-142  9.0 9.2 10.3 7.8 7.6 23.6 49.8
 LYS-142   TYR-143  9.2 9.4 -28.1 3.9 116.8 120.6 -46.9
 TYR-143   LEU-144  5.4 5.7 20.4 -2.8 92.1 89.5 6.9
 LEU-144   ARG-145  5.8 5.7 0.0 85.2 145.1 159.8 207.5
 ARG-145   GLN-146  7.1 5.9 5.8 11.2 101.0 81.8 -30.5
 GLN-146   ASP-147  10.1 9.3 -29.7 -26.5 133.8 100.9 -68.3
 ASP-147   LEU-148  11.5 11.7 -39.2 9.4 122.1 127.5 -14.9
 LEU-148   ARG-149  13.7 13.7 1.0 -6.1 83.2 84.7 3.0

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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