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
 LEU-140   SER-141  5.5 5.5 -1.3 0.8 102.6 102.9 -33.2
 SER-141   LEU-142  2.7 2.7 -2.3 -0.3 108.0 108.9 61.1
 LEU-142   TYR-143  6.3 6.3 -0.4 1.8 162.8 163.7 13.7

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
 ILE-341   GLY-342  3.3 3.4 1.1 -0.5 88.6 89.7 22.5
 GLY-342   GLY-343  4.1 3.9 6.1 -9.1 96.1 97.1 59.4
 GLY-343   SER-344  7.4 7.2 5.2 0.3 162.3 161.8 -145.0

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