Fusion Protein Beta-2 Adrenergic Receptor/lysozyme

(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-222   PHE-223  4.5 4.1 1.0 1.6 139.1 120.0 2.3
 PHE-223   GLN-224  6.4 5.5 -1.3 16.8 45.6 45.9 -10.1
 GLN-224   GLU-225  3.6 2.9 8.7 -4.1 77.9 65.2 0.3
 GLU-225   ALA-226  0.9 0.8 -24.7 16.1 93.7 104.8 -0.4
 ALA-226   LYS-227  4.7 4.2 -9.4 65.2 25.7 37.2 -34.9
 LEU-266   LYS-267  17.6 4.6 45.0 -7.0 24.7 56.1 -211.4
 LYS-267   GLU-268  15.9 7.1 9.5 0.0 93.5 108.3 -3.4
 GLU-268   HIS-269  12.7 9.7 162.6 -79.7 91.2 125.0 207.4
 HIS-269   LYS-270  15.0 12.5 -123.4 1.2 149.0 99.3 -44.5
 LYS-270   ALA-271  16.9 16.3 -14.5 28.9 132.8 159.3 9.2
 ALA-271   LEU-272  13.4 16.6 -19.3 17.9 67.2 113.1 -2.0
 LEU-272   LYS-273  12.4 14.6 -20.8 9.3 91.8 63.5 -6.6
 LYS-273   THR-274  16.1 16.7 -12.0 -20.3 146.4 115.5 -19.9
 THR-274   LEU-275  14.8 20.0 33.5 -4.2 93.3 13.2 11.9
 LEU-275   GLY-276  12.6 18.7 -21.8 0.3 59.3 92.7 -1.8
 GLY-276   ILE-277  15.7 18.7 -4.9 -10.3 129.7 72.7 -5.1
 ILE-277   ILE-278  18.1 21.9 13.9 -54.2 59.5 58.3 -32.5
 ILE-278   MET-279  15.8 24.0 31.0 159.5 114.3 6.6 61.0
 MET-279   GLY-280  16.1 22.3 171.8 -34.3 106.8 67.0 -169.9
 GLY-280   THR-281  19.4 21.3 -167.6 -66.4 132.9 155.5 91.0
 THR-281   PHE-282  21.6 23.7 152.7 -11.8 67.2 62.9 -40.0
 PHE-282   THR-283  20.5 22.9 29.7 -46.0 126.5 59.2 9.1
 THR-283   LEU-284  21.9 26.3 -161.8 -2.3 85.8 52.1 99.8

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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