Mitogen-Activated Protein Kinase Fus3

(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
 LYS-49   PRO-50  12.1 12.1 -58.9 12.1 39.3 52.7 248.2
 PRO-50   LEU-51  11.0 11.1 -15.4 -9.8 27.5 15.9 198.0
 LEU-51   PHE-52  13.3 13.3 -0.4 0.5 61.2 54.1 -0.2
 PHE-52   ALA-53  11.5 11.9 6.8 1.9 109.1 97.3 -34.8

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
 GLU-330   PHE-331  13.7 13.6 -12.4 6.2 24.0 43.6 26.3
 PHE-331   ASP-332  12.1 13.4 -6.0 11.0 81.8 104.4 8.8
 ASP-332   HIS-333  14.5 15.8 4.7 2.2 99.0 90.3 9.6
 HIS-333   TYR-334  17.5 18.4 -31.0 -31.4 40.5 27.0 456.7
 TYR-334   LYS-335  17.4 18.4 5.1 -30.2 124.5 125.4 80.4
 LYS-335   GLU-336  20.6 20.1 23.7 48.5 142.3 150.3 -545.7
 GLU-336   ALA-337  18.2 18.0 26.0 -17.1 70.3 91.0 40.2
 ALA-337   LEU-338  15.5 15.7 9.4 -29.7 108.5 83.8 6.6
 LEU-338   THR-339  12.0 12.1 -4.7 -16.8 52.9 41.2 117.2
 THR-339   THR-340  9.7 9.6 6.7 -4.7 64.9 69.7 12.9
 THR-340   LYS-341  7.0 6.6 -3.4 -0.9 94.2 104.8 -16.2
 LYS-341   ASP-342  4.6 4.5 -0.5 2.6 140.7 150.9 10.2

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