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
 LEU-147   ASP-148  6.2 6.3 5.0 -20.8 115.1 116.5 30.9
 ASP-148   ALA-149  2.5 2.7 12.8 -12.9 119.5 107.5 -3.0
 ALA-149   SER-150  2.2 1.7 6.4 6.2 108.9 111.7 7.3
 SER-150   SER-151  4.0 3.8 0.3 -5.8 161.4 157.6 8.4

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-173   LEU-174  7.6 7.6 -5.6 12.8 51.2 48.7 -10.9
 LEU-174   LEU-175  4.5 4.5 -5.5 -3.3 19.8 21.9 27.9
 LEU-175   ALA-176  6.5 6.5 -20.6 23.5 83.1 84.0 13.4
 ALA-176   GLU-177  8.8 9.4 1.8 -6.4 90.0 94.9 5.4
 GLU-177   ILE-178  7.0 8.1 -8.3 22.5 27.4 26.2 -76.0
 ILE-178   LYS-179  5.5 6.2 -16.2 8.3 43.5 42.3 27.3
 LEU-193   VAL-194  11.5 11.4 -4.1 -14.2 26.9 34.6 82.5

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