Cytochrome B6-F Complex Iron-Sulfur Subunit
(All numbering and residues are taken from first PDB file)
Bending Residue Dihedral Analysis
Residue
iResidue
i+1Distance of hinge axis to residue i in
(A) Distance of hinge axis to residue i in
(A) Change in
(deg) Change in
(deg) Angle of psi(i) axis to hinge axis
(deg) Angle of psi(i) axis to hinge axis
(deg) Percentage Progress
VAL-39
LYS-40
13.6
13.7
1.5
-0.7
131.6
131.7
-2.8
LYS-40
TYR-41
13.0
13.1
-0.8
-0.6
93.2
92.6
5.0
TYR-41
PHE-42
9.6
9.7
3.4
-1.2
125.7
125.1
-5.3
PHE-42
ILE-43
8.2
8.3
-2.1
-0.1
15.7
15.6
17.7
ILE-43
PRO-44
9.1
9.1
-9.5
36.9
77.9
84.3
-159.6
PRO-44
PRO-45
6.5
6.2
50.9
-17.0
111.8
85.3
-175.3
PRO-45
SER-46
8.6
7.6
-42.7
82.8
27.6
22.8
-439.7
SER-46
GLY-47
9.3
9.7
59.1
-33.1
84.4
104.3
107.1
GLY-47
GLY-48
12.0
10.7
75.5
155.9
151.8
107.6
1050.5
GLY-48
ALA-49
14.0
14.1
-127.1
111.3
38.6
2.7
161.2
ALA-49
VAL-50
12.3
15.1
110.8
-28.1
118.8
109.9
-594.7
VAL-50
GLY-51
10.5
16.9
7.6
-70.0
90.4
59.3
-326.9
GLY-51
GLY-52
11.4
15.2
-95.7
104.0
139.6
104.3
102.7
GLY-52
GLY-53
9.5
12.0
150.9
159.3
107.4
108.0
123.2
GLY-53
THR-54
10.4
10.3
-20.4
2.5
7.9
7.7
241.2
THR-54
THR-55
11.2
11.2
0.0
0.3
57.9
58.7
-10.0
THR-55
ALA-56
14.2
14.2
0.0
0.5
72.5
72.0
7.6
ALA-56
LYS-57
12.3
12.3
1.1
-1.4
45.3
44.9
-1.5
LYS-57
ASP-58
12.9
12.9
-1.3
1.6
80.5
81.0
6.9
ASP-58
LYS-59
13.3
13.3
-1.3
0.7
145.2
145.5
4.3
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