Neutrophil Cytosolic Factor 1

(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
 GLN-197   MET-198  11.5 11.3 -6.5 16.5 38.2 41.5 -34.3
 MET-198   LYS-199  11.3 11.6 -16.3 -3.7 36.0 33.0 108.7
 LYS-199   ALA-200  10.9 11.7 -12.1 -15.1 83.6 72.3 22.7
 ALA-200   LYS-201  7.2 8.2 4.8 20.3 135.3 156.1 -85.4
 LYS-201   ARG-202  6.1 8.2 37.3 -23.7 116.5 113.4 0.1
 ARG-202   GLY-203  3.4 5.3 0.0 -15.5 33.4 27.7 53.2
 GLY-203   TRP-204  2.6 4.7 13.6 0.9 101.8 96.0 -26.0
 TRP-204   ILE-205  3.0 4.8 4.6 -0.5 73.5 64.6 -2.9
 ILE-205   PRO-206  6.5 7.7 -1.8 3.0 77.1 76.5 5.0
 PRO-206   ALA-207  9.8 10.7 -1.0 3.5 137.9 134.9 2.9
 ALA-207   SER-208  11.0 11.0 -5.0 -2.6 112.0 121.6 -14.5
 SER-208   PHE-209  14.3 14.5 11.5 -0.9 38.2 39.7 32.0

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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