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  6.0 6.0 -0.6 -3.9 42.4 43.8 -3.7
 SER-141   LEU-142  3.3 3.2 4.4 -7.1 145.6 151.8 9.1
 LEU-142   TYR-143  6.0 5.7 1.2 -4.8 87.5 90.9 27.3
 TYR-143   ALA-144  8.5 8.2 1.6 -1.0 100.8 99.9 -22.4
 ALA-144   SER-145  7.0 6.6 6.8 -6.3 167.3 165.6 5.9
 SER-145   GLY-146  6.5 6.0 -6.4 9.7 64.6 62.4 -18.7
 GLY-146   ARG-147  10.1 9.5 2.0 -15.1 115.2 115.9 12.0

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


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
 VAL-339   TRP-340  2.0 1.9 -1.4 3.1 51.7 51.2 -7.0
 TRP-340   ILE-341  4.6 4.5 4.7 -1.6 62.4 63.6 33.4
 ILE-341   GLY-342  7.3 7.1 -2.2 7.6 103.2 99.7 -33.3

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