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  6.1 6.0 -2.5 1.3 100.4 97.9 3.0
 THR-123   ALA-124  2.8 2.9 -10.1 -6.0 75.7 75.2 8.0
 ALA-124   PRO-125  1.0 1.5 5.0 17.5 38.0 30.6 44.7
 PRO-125   LEU-126  3.4 3.0 10.7 -5.0 75.7 81.4 27.4

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
 GLN-230   GLU-231  9.7 9.5 -5.1 -6.2 23.5 26.8 25.4
 GLU-231   PRO-232  7.8 7.5 6.4 7.4 95.3 88.0 4.6
 PRO-232   SER-233  9.3 8.4 -3.0 8.3 60.5 74.8 -13.1
 SER-233   PHE-234  6.8 5.5 8.5 -18.7 54.9 48.6 -5.3
 PHE-234   ALA-235  5.9 5.0 6.0 -11.7 118.6 122.6 31.1
 ALA-235   TYR-236  3.5 3.2 12.0 3.9 60.9 65.4 22.1
 TYR-236   VAL-237  1.8 1.8 1.2 5.4 23.3 25.7 13.4
 VAL-237   ALA-238  4.0 4.0 -14.9 -2.1 88.1 82.8 28.3

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