Glutamine Abc Transporter Permease And Substrate Binding Protein 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
 TYR-111   TYR-112  8.7 8.2 13.6 -3.6 108.7 110.1 -11.7
 TYR-112   THR-113  5.3 4.7 19.0 34.8 49.0 44.1 90.7
 THR-113   SER-114  2.7 2.1 35.7 -37.0 117.6 110.4 -4.9
 SER-114   ALA-115  1.9 1.7 -51.4 6.1 127.5 112.8 -50.3
 ALA-115   LEU-116  5.4 5.0 -21.8 -3.9 54.8 53.0 48.3
 LEU-116   THR-117  8.6 8.4 2.6 2.2 91.4 91.0 7.6

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


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-205   SER-206  9.1 9.0 0.4 -13.9 84.4 85.2 0.7
 SER-206   LEU-207  5.5 5.4 -10.8 -13.2 85.5 69.3 14.1
 LEU-207   PRO-208  3.8 4.0 -8.9 -9.2 57.0 78.9 -8.4
 PRO-208   GLY-209  2.4 1.2 -158.3 -171.9 112.3 106.8 40.9
 GLY-209   GLY-210  3.8 4.5 21.0 -3.5 43.3 33.2 29.5
 GLY-210   TYR-211  3.4 3.6 8.2 8.6 56.6 52.8 28.1
 TYR-211   GLY-212  5.7 5.8 5.6 -3.8 96.6 99.0 -1.7

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