C1r Complement Serine Protease

(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-431   PRO-432  4.6 4.8 -18.8 31.0 76.4 79.1 -33.2
 PRO-432   VAL-433  1.3 1.3 -18.8 -13.8 30.2 26.0 138.0
 VAL-433   CYS-434  1.4 1.5 5.4 -15.2 79.1 83.6 2.7
 CYS-434   GLY-435  4.2 4.3 -11.8 35.4 47.1 36.8 -84.2
 GLY-435   LYS-436  7.4 7.4 -66.4 59.5 46.7 50.7 29.2
 LYS-436   PRO-437  7.6 7.1 -1.0 8.0 120.7 116.6 15.4
 PRO-437   VAL-438  10.6 10.4 -25.1 32.3 60.4 63.5 7.3
 VAL-438   ASN-439  12.9 12.5 -66.0 44.2 81.0 65.8 51.5
 ASN-439   PRO-440  15.7 15.8 22.5 11.2 106.8 102.1 -67.8
 PRO-440   VAL-441  15.6 15.6 -36.0 83.8 75.0 90.9 -40.3
 VAL-441   GLU-442  18.9 18.8 42.3 -129.5 144.9 153.4 385.9
 ILE-447   ILE-448  27.2 28.0 -90.6 49.7 154.5 76.3 -163.3
 ILE-448   GLY-449  28.1 31.6 -23.9 -62.8 128.8 8.4 214.3
 GLY-449   GLY-450  29.1 31.6 177.4 -143.7 15.0 100.3 121.2
 GLY-450   GLN-451  29.2 30.4 109.1 -171.0 62.8 109.2 -53.9
 GLN-451   LYS-452  28.4 28.0 -79.5 0.5 141.3 135.4 -263.2
 LYS-452   ALA-453  26.7 26.1 -32.9 39.6 75.9 68.9 4.7
 ALA-453   LYS-454  23.1 22.4 -1.9 14.8 105.8 105.3 14.0
 LYS-454   MET-455  22.0 21.5 15.1 -13.7 74.4 71.0 0.3
 MET-455   GLY-456  19.3 18.9 19.1 -26.3 135.6 135.6 21.2

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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