Actin, Alpha Skeletal Muscle

(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
 ALA-138   VAL-139  5.6 6.0 5.7 -4.6 123.5 125.7 -3.9
 VAL-139   LEU-140  8.8 9.0 4.0 -4.6 158.1 154.1 0.4
 LEU-140   SER-141  7.0 6.9 5.8 -2.0 89.7 89.3 16.4
 SER-141   LEU-142  4.7 4.6 5.6 -12.6 91.9 98.8 -6.4
 LEU-142   TYR-143  8.3 8.2 11.9 -5.9 159.1 164.5 -22.7
 TYR-143   ALA-144  9.2 8.5 -1.6 -4.0 56.0 61.9 12.7

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


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-334   ARG-335  6.7 6.9 6.6 -5.7 135.9 134.5 12.5
 ARG-335   LYS-336  5.0 5.2 -4.6 -2.6 74.3 73.2 74.4
 LYS-336   TYR-337  5.6 5.6 1.6 9.1 62.6 60.2 -4.3

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