Penicillin-Binding Protein 2X

(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-91   THR-92  5.8 5.6 -0.1 1.8 37.7 35.6 8.4
 THR-92   SER-93  5.2 5.1 0.6 0.8 105.3 102.7 18.8
 SER-93   TYR-94  1.8 1.6 -12.2 8.0 23.6 21.0 46.3
 TYR-94   ASN-95  0.6 0.5 -3.6 4.0 84.9 83.2 -36.5
 ASN-95   VAL-96  3.8 3.8 -6.1 3.4 20.4 23.2 19.4

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
 PHE-180   THR-181  1.3 1.3 -13.4 11.8 85.4 87.4 57.7
 THR-181   THR-182  3.8 3.8 -3.5 -4.3 34.0 30.7 71.9
 THR-182   SER-183  4.8 4.7 -7.2 7.7 45.4 46.5 -20.1

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