Penicillin-Binding Protein-Related Factor A

(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
 LYS-55   PRO-56  5.6 5.7 1.6 0.0 77.7 80.9 -11.5
 PRO-56   THR-57  2.2 1.9 5.7 5.7 8.0 16.6 35.0
 THR-57   PRO-58  3.1 2.2 4.4 -16.3 65.2 62.0 4.7
 PRO-58   VAL-59  0.3 0.6 0.9 -5.4 65.2 60.7 0.1
 VAL-59   GLN-60  3.9 3.9 20.6 -10.0 62.2 72.0 31.9

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


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
 TYR-78   PHE-79  7.7 7.5 -1.1 6.9 111.9 113.4 6.8
 PHE-79   ARG-80  5.2 4.7 -8.4 -6.9 44.9 48.8 46.2
 ARG-80   GLN-81  1.8 1.2 10.2 -13.8 95.7 85.9 -10.3
 GLN-81   ALA-82  3.6 2.7 5.0 6.3 44.8 53.9 0.0
 ALA-82   SER-83  5.3 4.9 0.2 0.1 112.3 122.6 13.8
 SER-83   THR-84  7.7 7.8 6.8 -8.6 54.8 58.5 21.3
 THR-84   THR-85  9.9 9.9 -7.7 -0.2 111.3 115.7 -2.2

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