Complement Control 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
 CYS-182   GLN-183  3.1 3.4 -7.2 17.0 126.0 119.4 22.2
 GLN-183   ILE-184  1.1 1.4 -9.9 -1.6 53.8 47.2 28.4
 ILE-184   VAL-185  4.3 4.5 18.9 0.4 73.3 80.8 31.0

Downloading Image

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


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
 TYR-205   SER-206  9.9 9.9 -6.9 -9.0 47.6 45.8 52.1
 SER-206   TYR-207  6.5 6.7 -38.4 -6.1 59.0 52.5 66.4
 TYR-207   ASN-208  6.4 5.7 -23.8 -45.1 66.7 97.3 37.6
 ASN-208   ASP-209  9.7 9.0 24.9 44.9 87.7 44.4 149.8
 ASP-209   ASN-210  12.6 11.6 123.0 23.4 126.3 113.9 -229.4
 ASN-210   VAL-211  16.3 15.2 -57.4 -4.9 124.0 113.7 -171.2
 VAL-211   ASP-212  17.8 17.7 -22.4 -41.7 89.8 54.4 62.2
 ASP-212   PHE-213  21.4 20.9 33.9 9.4 64.8 55.3 75.7
 PHE-213   LYS-214  23.7 23.2 4.3 -15.2 63.1 75.8 1.6
 LYS-214   CYS-215  26.7 26.5 7.2 -3.7 106.9 88.3 8.4

Downloading Image

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