Nuclear Valosin-Containing Protein-Like

(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-683   ASP-684  30.1 27.1 24.7 -14.4 43.2 51.7 7.5
 ASP-684   ALA-685  32.3 24.4 -63.0 -116.1 65.8 90.0 -1.3
 ALA-685   LEU-686  36.1 21.7 121.9 -2.0 132.2 93.2 -70.7
 LEU-686   CYS-687  35.3 18.4 128.0 51.3 51.6 71.4 69.3
 CYS-687   PRO-688  34.2 15.5 83.2 -66.1 31.4 113.0 6.8
 ARG-700   VAL-701  40.2 9.1 -138.5 -54.5 53.6 58.5 133.9
 VAL-701   VAL-702  37.5 5.5 77.4 -72.9 55.7 72.8 3.4
 VAL-702   ASN-703  35.3 4.1 114.9 29.1 91.0 124.8 -79.2
 ASN-703   GLN-704  36.0 5.4 170.8 -13.1 151.6 63.0 39.8
 GLN-704   LEU-705  35.4 8.7 157.0 14.7 93.3 116.4 4.3
 LEU-705   LEU-706  32.0 10.1 178.5 -1.6 57.3 112.9 -70.1
 LEU-706   THR-707  31.3 13.0 146.6 -8.2 117.6 61.5 -81.4
 THR-707   GLU-708  32.8 16.2 -159.1 29.5 49.6 52.2 92.6
 GLU-708   MET-709  30.4 19.2 -37.4 15.0 111.3 48.0 10.3
 MET-709   ASP-710  27.4 21.6 11.9 -4.2 68.8 133.0 2.6
 ASP-710   GLY-711  28.4 18.9 99.1 18.0 139.0 139.6 -64.4
 GLY-711   LEU-712  29.2 18.8 164.7 20.3 117.6 119.5 81.3
 LEU-712   GLU-713  25.5 15.8 15.6 24.1 69.2 136.2 -0.5
 GLU-713   ALA-714  23.5 15.8 -163.5 -29.9 69.7 35.4 -111.7
 ALA-714   ARG-715  19.8 13.4 37.0 -13.2 163.8 111.4 -11.9
 ARG-715   GLN-716  20.9 16.7 -174.4 14.3 50.3 22.6 78.1
 GLN-716   GLN-717  21.8 18.1 129.1 -172.0 98.5 90.9 2.8
 GLN-717   VAL-718  18.2 20.1 130.8 57.2 92.2 157.1 -60.3
 VAL-718   PHE-719  20.1 22.3 -178.3 77.4 156.0 62.4 113.4
 PHE-719   ILE-720  19.2 20.0 -133.8 -12.5 96.4 65.3 -4.3
 ILE-720   MET-721  21.8 17.2 -174.1 55.6 117.0 24.5 2.5
 MET-721   ALA-722  21.4 19.2 18.4 -15.1 83.0 129.8 -3.2
 ALA-722   ALA-723  24.5 19.0 12.6 -166.1 66.0 152.2 -40.9
 ASN-725   ARG-726  29.3 23.1 87.5 58.0 18.3 61.3 -134.2
 ARG-726   PRO-727  30.0 25.8 -167.0 25.7 95.1 88.9 25.0
 PRO-727   ASP-728  27.6 29.1 -16.0 -12.6 139.6 109.9 131.8
 ASP-728   ILE-729  29.3 29.0 -24.4 41.9 77.1 169.3 -126.5
 ILE-729   ILE-730  32.6 27.5 -40.7 34.4 53.2 107.7 -3.6
 ILE-730   ASP-731  31.2 30.4 179.5 -22.9 58.5 91.4 -4.8
 ASP-731   PRO-732  31.9 32.7 -157.8 7.3 107.1 139.7 138.0
 PRO-732   ALA-733  29.1 31.5 -37.1 14.9 70.2 147.5 -6.3
 ALA-733   ILE-734  30.1 31.7 -0.2 -4.7 40.4 102.7 -6.9
 ILE-734   LEU-735  28.2 35.4 -19.4 44.0 107.0 101.2 11.3
 LEU-735   ARG-736  25.2 36.4 -33.4 -25.1 118.9 165.0 -36.2
 ARG-736   PRO-737  25.2 35.1 173.2 19.2 119.3 50.1 -11.6
 PRO-737   GLY-738  22.5 35.5 161.4 -158.8 142.4 52.2 -0.6
 GLY-738   ARG-739  22.9 38.9 -41.0 34.3 48.0 130.9 2.6
 ARG-739   LEU-740  24.2 38.9 94.5 6.3 92.8 56.5 -107.4
 LEU-740   ASP-741  22.7 35.4 -88.1 -43.1 150.6 135.2 114.5
 ASP-741   LYS-742  20.6 35.3 18.4 -26.7 80.9 62.3 0.0
 LYS-742   THR-743  17.8 39.0 -45.4 38.0 72.1 95.5 10.5
 THR-743   LEU-744  19.4 39.9 162.2 72.8 97.9 77.6 -16.7
 LEU-744   PHE-745  17.9 43.1 -160.0 43.7 91.9 42.9 -62.6
 PHE-745   VAL-746  19.8 44.5 -163.1 21.8 50.5 64.2 85.2
 ALA-752   ASP-753  16.1 47.0 -10.4 -16.2 70.0 88.8 -10.1
 ASP-753   ARG-754  17.1 49.6 47.2 -70.6 132.1 162.2 12.4
 ARG-754   LEU-755  20.3 49.7 -159.1 -68.7 22.5 63.9 144.3
 LEU-755   ALA-756  18.3 50.8 115.6 -72.4 113.0 165.2 -22.2
 ALA-756   ILE-757  16.1 48.7 -168.3 -15.5 71.0 78.3 -42.6
 ILE-757   LEU-758  19.6 46.5 139.0 -19.3 151.8 99.2 -75.2
 LEU-758   LYS-759  20.7 42.8 157.1 33.6 141.8 111.1 65.4
 LYS-759   THR-760  17.4 40.3 159.7 -23.7 107.4 45.8 18.2
 THR-760   ILE-761  18.5 39.3 -8.9 -34.5 64.1 62.1 23.3
 ILE-761   THR-762  22.2 37.4 177.5 -44.9 160.6 127.3 -74.4
 THR-762   LYS-763  21.4 34.4 120.1 -154.2 122.2 118.9 9.5
 LYS-763   ASN-764  18.3 32.8 97.3 172.1 108.9 115.1 12.8
 ASN-764   GLY-765  16.4 29.4 69.2 -161.1 140.2 139.5 62.7
 GLY-765   THR-766  19.2 28.4 144.4 -111.8 157.6 100.8 -14.8
 THR-766   LYS-767  19.0 25.0 -151.4 42.3 85.0 84.2 8.8
 LYS-767   PRO-768  22.0 22.4 69.6 30.2 32.2 36.4 -57.7
 PRO-768   PRO-769  24.1 20.7 -14.0 160.2 75.1 93.4 -4.2
 PRO-769   LEU-770  22.4 17.7 -112.7 18.2 111.5 80.4 -0.5
 LEU-770   ASP-771  23.1 19.6 -156.9 178.5 56.7 151.4 -3.5
 ASP-771   ALA-772  24.0 19.6 -132.0 -6.8 127.8 117.4 106.2
 ALA-772   ASP-773  23.0 23.2 -28.3 29.0 140.2 172.6 2.5
 ASP-773   VAL-774  26.2 22.2 -35.4 27.7 147.2 118.0 -6.0
 VAL-774   ASN-775  24.8 20.2 -170.6 63.6 116.5 93.7 -33.3
 ASN-775   LEU-776  22.6 23.2 -132.5 -22.5 140.2 132.8 -85.1
 LEU-776   GLU-777  21.5 25.2 -38.1 17.7 155.5 160.0 -11.4

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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