Ferric Vibriobactin Abc Transporter, Periplasmic Ferric Vibriobactin-Binding Protein

(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
 ILE-172   HIS-173  7.3 7.0 -2.5 13.2 118.6 121.5 16.2
 HIS-173   ASN-174  4.8 4.6 3.1 -11.7 108.5 111.9 9.4
 ASN-174   PHE-175  3.1 3.1 3.2 -3.2 144.7 144.3 1.2
 PHE-175   GLU-176  2.5 2.3 4.3 -9.5 77.9 77.6 -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


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-231   TRP-232  29.6 30.1 12.9 -15.1 32.2 29.9 10.2
 TRP-232   GLN-233  26.7 27.3 7.2 -1.4 79.8 81.0 1.7
 GLN-233   ALA-234  26.5 26.9 1.0 28.2 24.3 23.7 228.2
 ALA-234   GLY-235  26.3 26.7 -12.1 -5.8 87.6 85.7 -3.1
 GLY-235   SER-236  27.7 29.4 0.4 18.7 152.4 155.6 -139.3
 SER-236   ILE-237  28.8 31.1 -1.3 -2.0 54.8 45.8 41.9
 ILE-237   VAL-238  25.7 28.4 4.2 32.1 130.7 131.9 -233.2
 VAL-238   HIS-239  24.5 27.3 -9.9 0.6 59.3 76.0 60.1
 HIS-239   ARG-240  21.3 23.6 -17.0 -31.9 36.9 42.0 304.0
 ARG-240   ASP-241  19.9 22.1 19.7 -0.1 79.1 87.7 -6.8
 ASP-241   PHE-242  16.7 18.4 -25.0 4.5 133.1 129.1 -240.4
 PHE-242   LEU-243  17.8 18.3 2.6 8.4 72.9 65.2 11.4
 LEU-243   ARG-244  20.9 21.4 0.7 3.8 10.2 13.2 27.1

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