Cytidine Monophosphate Kinase

(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
 ASP-148   ALA-149  5.6 5.4 5.1 -5.7 97.8 95.0 25.4
 ALA-149   SER-150  6.8 6.8 -12.6 5.4 10.5 10.2 94.2
 SER-150   SER-151  7.7 7.6 -8.7 -0.1 74.9 76.7 -5.6

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


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-191   PRO-192  18.9 18.8 6.7 -12.1 67.8 72.8 -25.7
 PRO-192   LEU-193  15.7 15.6 -2.7 15.3 45.3 47.1 -89.4
 LEU-193   VAL-194  12.8 12.4 18.0 -7.8 87.4 78.7 -25.7

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