Lipoprotein

(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
 PRO-122   THR-123  5.8 5.7 -8.1 10.5 100.5 103.0 12.6
 THR-123   ALA-124  2.5 2.8 -1.4 -13.2 73.2 73.2 10.1
 ALA-124   PRO-125  1.4 1.9 -3.4 27.8 139.0 147.8 40.5
 PRO-125   LEU-126  3.5 3.2 -1.9 2.8 102.7 101.3 32.5

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
 PHE-229   GLN-230  13.4 13.2 8.2 -12.3 97.0 95.3 3.1
 GLN-230   GLU-231  9.7 9.6 -1.0 -11.0 21.5 28.1 29.1
 GLU-231   PRO-232  8.0 7.6 0.2 4.5 96.0 84.3 -4.7
 PRO-232   SER-233  9.2 8.6 2.4 6.9 122.4 115.4 -3.1
 SER-233   PHE-234  6.7 5.9 11.7 -27.6 57.9 54.2 -17.6
 PHE-234   ALA-235  5.6 4.8 4.2 -11.3 120.9 124.4 40.7
 ALA-235   TYR-236  3.1 3.0 11.7 7.0 62.9 68.3 18.4
 TYR-236   VAL-237  1.2 1.4 -0.1 2.9 154.5 152.0 17.9

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