Hspbp1 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
 ARG-237   ALA-238  9.4 9.0 13.5 -24.4 108.6 118.0 44.8
 GLN-240   GLN-241  12.9 12.6 26.1 -4.7 156.0 164.3 -101.9
 GLN-241   GLN-242  12.3 11.4 -21.4 1.1 90.2 77.0 132.1
 GLN-242   VAL-243  14.4 13.7 87.9 -76.3 83.1 98.4 45.5
 VAL-243   GLN-244  13.1 12.0 -19.4 15.6 163.6 151.1 -24.6
 GLN-244   LYS-245  14.8 14.2 -0.8 -0.5 117.0 121.1 7.4
 LYS-245   LEU-246  13.3 11.9 -11.3 14.0 106.4 116.8 -19.1
 LEU-246   LYS-247  9.7 8.7 19.0 -20.9 41.1 31.3 -9.7
 LYS-247   VAL-248  11.1 11.1 -11.0 13.4 150.1 138.8 9.6
 VAL-248   LYS-249  12.2 12.2 1.2 2.4 70.0 70.1 10.1
 LYS-249   SER-250  9.6 9.1 -5.8 0.0 109.8 124.6 -30.6
 SER-250   ALA-251  6.8 6.9 10.9 -3.8 24.0 21.9 38.6
 ALA-251   PHE-252  8.9 9.4 6.3 -13.5 44.3 56.1 -21.2
 PHE-252   LEU-253  9.1 9.3 -3.0 1.1 105.5 108.9 -12.6
 LEU-253   LEU-254  5.5 5.7 -10.7 11.3 126.6 139.2 16.8
 LEU-254   GLN-255  4.8 5.0 4.1 -10.3 21.5 27.2 -21.6

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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