Penicillin-Binding Protein 3

(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
 VAL-75   SER-76  18.6 18.3 18.1 0.9 91.3 85.8 -13.7
 SER-76   THR-77  15.1 14.7 26.2 -10.8 64.9 45.4 -34.4
 THR-77   PRO-78  12.9 12.1 2.5 -19.1 88.6 100.7 -14.8
 PRO-78   VAL-79  9.1 8.3 5.1 2.6 30.6 46.4 29.1
 VAL-79   THR-80  7.4 7.3 5.9 -28.8 102.6 114.4 148.4
 THR-80   THR-81  4.1 5.2 3.1 22.4 77.3 87.6 51.9
 THR-81   LEU-82  6.3 7.7 -42.1 17.0 85.1 96.4 65.6
 LEU-82   TRP-83  7.1 7.5 -50.0 51.7 63.2 70.2 -104.0

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
 SER-147   ILE-148  4.1 4.2 0.8 6.5 27.9 21.9 20.9
 ILE-148   GLU-149  2.8 3.7 -37.4 11.0 74.6 71.0 129.1
 GLU-149   GLU-150  3.5 3.4 -9.5 6.0 116.1 117.8 -35.4
 GLU-150   PHE-151  7.1 7.2 -10.9 0.8 81.5 71.3 119.4
 PHE-151   ARG-152  10.5 10.2 25.1 -28.1 117.1 113.3 58.6

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