Alpha-1-Antichymotrypsin

(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
 ALA-151   ALA-152  10.4 9.2 -15.6 12.2 147.3 147.3 -7.0
 ALA-152   ALA-153  10.1 8.6 -21.9 21.4 124.8 129.3 -1.1
 ALA-153   LYS-154  6.4 4.9 -17.0 26.5 125.5 129.3 8.4
 LYS-154   LYS-155  7.9 6.8 -40.9 31.5 141.2 143.4 -12.4
 LYS-155   LEU-156  10.4 9.3 -4.7 6.4 139.5 134.9 -0.5
 LEU-156   ILE-157  8.3 7.0 -9.5 9.7 126.3 131.0 0.9
 ILE-157   ASN-158  5.9 4.8 -7.2 8.1 123.5 127.9 -0.5
 ASN-158   ASP-159  9.4 8.3 -0.3 7.5 142.0 137.2 6.3
 ASP-159   TYR-160  10.2 9.0 -21.8 24.1 135.4 140.0 0.0
 TYR-160   VAL-161  6.8 5.7 -13.7 49.4 123.3 123.0 24.4

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


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
 MET-182   VAL-183  4.9 5.4 -5.1 -9.5 58.4 63.4 14.2
 VAL-183   LEU-184  4.7 4.9 7.1 -16.8 161.8 162.7 14.7
 LEU-184   VAL-185  6.0 6.1 -26.2 28.7 57.5 56.1 -6.4

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