Xpf Endonuclease

(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-149   GLU-150  37.4 39.6 3.1 87.1 116.9 116.5 -42.5
 GLU-150   GLY-151  35.5 38.9 -2.6 -138.9 43.9 13.9 192.4
 GLY-151   GLY-152  36.3 37.8 168.5 2.6 111.2 106.9 -184.8
 GLY-152   GLN-153  38.4 34.4 113.4 -93.3 142.8 71.7 97.2
 GLN-153   ARG-154  38.2 32.7 22.0 -148.7 103.3 96.6 -143.9
 ARG-154   ILE-155  34.7 32.5 107.7 -2.4 57.9 19.9 93.6
 ILE-155   VAL-156  33.2 32.8 -17.3 -15.7 144.8 91.6 -16.3
 VAL-156   ILE-157  31.1 31.7 -12.5 -14.3 144.2 159.5 -27.3
 ILE-157   HIS-158  31.5 32.4 -32.2 16.9 117.7 85.1 5.3
 HIS-158   LYS-159  28.1 30.8 -26.1 -3.5 167.5 153.2 -40.9
 LYS-159   LYS-160  27.5 32.1 37.7 -4.3 82.4 87.9 14.6
 LYS-160   PRO-161  27.3 29.7 9.1 10.9 24.6 83.1 16.5
 PRO-161   ARG-162  25.4 29.9 8.1 -36.3 65.8 14.1 -45.1
 ARG-162   LEU-163  27.8 31.5 -56.6 -20.9 89.5 85.3 -2.2
 LEU-163   SER-164  28.8 28.9 18.6 60.9 30.2 43.1 71.7
 SER-164   ASP-165  27.1 29.3 120.1 27.0 101.8 74.2 10.1
 ASP-165   VAL-166  26.8 26.6 -177.0 10.2 95.8 104.1 122.0
 VAL-166   ARG-167  23.2 23.1 3.7 -12.6 146.5 156.9 2.9

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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