Clpb Protein

(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
 GLY-138   ARG-139  15.3 14.7 -139.7 54.0 135.3 58.3 53.7
 ARG-139   THR-140  14.3 11.2 149.8 33.1 96.7 75.6 -147.3
 THR-140   VAL-141  11.3 10.7 -27.2 81.2 72.7 76.7 270.8
 VAL-141   GLN-142  12.0 13.2 -176.7 -7.0 25.5 96.7 -115.1
 GLN-142   THR-143  9.4 11.9 -1.6 80.3 62.3 85.4 -23.8
 THR-143   GLU-144  9.9 8.6 10.0 62.7 155.6 138.0 -69.1
 GLU-144   HIS-145  9.1 8.6 49.0 -52.5 92.8 152.3 4.6
 HIS-145   ALA-146  7.7 7.3 120.2 -169.9 27.9 109.7 -8.6
 ALA-146   GLU-147  7.9 5.1 -21.1 113.6 120.2 128.0 44.9
 GLU-147   SER-148  5.2 4.5 -8.9 124.6 97.7 53.5 -9.4
 SER-148   THR-149  6.4 8.0 -38.7 40.0 54.8 41.1 -0.9
 THR-149   TYR-150  6.5 8.7 44.6 -158.7 84.8 137.7 44.7
 TYR-150   ASN-151  9.0 9.9 41.1 9.9 90.8 101.3 1.6
 ASN-151   ALA-152  7.7 9.4 -24.9 29.3 19.0 13.5 -4.3

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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