Calcium in PDB 2w0c: X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
Protein crystallography data
The structure of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2, PDB code: 2w0c
was solved by
N.G.A.Abrescia,
J.M.Grimes,
H.M.Kivela,
R.Assenberg,
G.C.Sutton,
S.J.Butcher,
J.K.H.Bamford,
D.H.Bamford,
D.I.Stuart,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
96.00 /
7.00
|
|
Space group
|
C 1 2 1 24
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
946.900,
677.600,
1067.600,
90.00,
102.90,
90.00
|
|
R / Rfree (%)
|
41.9 /
n/a
|
Calcium Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
11;
Binding sites:
The binding sites of Calcium atom in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
(pdb code 2w0c). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 11 binding sites of Calcium where determined in the
X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2, PDB code: 2w0c:
Jump to Calcium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Calcium binding site 1 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 1 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 1 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Ca1270
b:40.0
occ:1.00
|
O
|
A:ALA105
|
2.5
|
40.0
|
1.0
|
|
O
|
A:PRO141
|
2.6
|
40.0
|
1.0
|
|
O
|
A:TRP143
|
2.8
|
40.0
|
1.0
|
|
O
|
A:MET103
|
3.1
|
40.0
|
1.0
|
|
CD1
|
A:LEU144
|
3.3
|
40.0
|
1.0
|
|
N
|
A:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
A:TRP143
|
3.7
|
40.0
|
1.0
|
|
C
|
A:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
A:PRO141
|
3.7
|
40.0
|
1.0
|
|
CB
|
A:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
A:PHE104
|
3.9
|
40.0
|
1.0
|
|
N
|
A:ALA105
|
3.9
|
40.0
|
1.0
|
|
C
|
A:SER142
|
3.9
|
40.0
|
1.0
|
|
C
|
A:MET103
|
3.9
|
40.0
|
1.0
|
|
CA
|
A:TRP143
|
4.1
|
40.0
|
1.0
|
|
OG
|
A:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
A:SER142
|
4.2
|
40.0
|
1.0
|
|
O
|
A:PHE104
|
4.2
|
40.0
|
1.0
|
|
CA
|
A:PHE104
|
4.2
|
40.0
|
1.0
|
|
O
|
A:ALA140
|
4.3
|
40.0
|
1.0
|
|
CA
|
A:ALA105
|
4.4
|
40.0
|
1.0
|
|
N
|
A:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
A:PHE104
|
4.4
|
40.0
|
1.0
|
|
N
|
A:GLY107
|
4.5
|
40.0
|
1.0
|
|
O
|
A:SER142
|
4.5
|
40.0
|
1.0
|
|
CB
|
A:TRP143
|
4.6
|
40.0
|
1.0
|
|
N
|
A:LEU144
|
4.7
|
40.0
|
1.0
|
|
N
|
A:LEU106
|
4.8
|
40.0
|
1.0
|
|
CG
|
A:LEU144
|
4.8
|
40.0
|
1.0
|
|
CA
|
A:PRO141
|
4.8
|
40.0
|
1.0
|
|
CA
|
A:MET103
|
5.0
|
40.0
|
1.0
|
|
O
|
A:ARG102
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 2 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 2 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 2 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Ca1270
b:40.0
occ:1.00
|
O
|
B:ALA105
|
2.6
|
40.0
|
1.0
|
|
O
|
B:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
B:PRO141
|
2.7
|
40.0
|
1.0
|
|
O
|
B:MET103
|
2.8
|
40.0
|
1.0
|
|
CD1
|
B:LEU144
|
3.1
|
40.0
|
1.0
|
|
C
|
B:TRP143
|
3.5
|
40.0
|
1.0
|
|
N
|
B:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
B:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
B:PRO141
|
3.8
|
40.0
|
1.0
|
|
C
|
B:PHE104
|
3.8
|
40.0
|
1.0
|
|
CB
|
B:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
B:MET103
|
3.8
|
40.0
|
1.0
|
|
C
|
B:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
B:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
B:TRP143
|
4.0
|
40.0
|
1.0
|
|
O
|
B:PHE104
|
4.1
|
40.0
|
1.0
|
|
CA
|
B:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
B:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
B:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
B:PHE104
|
4.4
|
40.0
|
1.0
|
|
O
|
B:ALA140
|
4.4
|
40.0
|
1.0
|
|
CA
|
B:ALA105
|
4.4
|
40.0
|
1.0
|
|
O
|
B:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
B:SER142
|
4.4
|
40.0
|
1.0
|
|
CB
|
B:TRP143
|
4.5
|
40.0
|
1.0
|
|
N
|
B:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
B:LEU144
|
4.6
|
40.0
|
1.0
|
|
N
|
B:GLY107
|
4.6
|
40.0
|
1.0
|
|
N
|
B:LEU106
|
4.8
|
40.0
|
1.0
|
|
CA
|
B:PRO141
|
4.9
|
40.0
|
1.0
|
|
CA
|
B:LEU144
|
4.9
|
40.0
|
1.0
|
|
CA
|
B:MET103
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 3 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 3 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 3 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Ca1270
b:40.0
occ:1.00
|
O
|
C:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
C:MET103
|
2.7
|
40.0
|
1.0
|
|
O
|
C:ALA105
|
2.7
|
40.0
|
1.0
|
|
O
|
C:PRO141
|
2.7
|
40.0
|
1.0
|
|
CD1
|
C:LEU144
|
3.2
|
40.0
|
1.0
|
|
C
|
C:TRP143
|
3.5
|
40.0
|
1.0
|
|
N
|
C:TRP143
|
3.6
|
40.0
|
1.0
|
|
CZ3
|
Q:TRP30
|
3.6
|
40.0
|
1.0
|
|
C
|
C:MET103
|
3.7
|
40.0
|
1.0
|
|
C
|
C:PHE104
|
3.8
|
40.0
|
1.0
|
|
C
|
C:ALA105
|
3.8
|
40.0
|
1.0
|
|
CB
|
C:SER142
|
3.8
|
40.0
|
1.0
|
|
CH2
|
Q:TRP30
|
3.8
|
40.0
|
1.0
|
|
C
|
C:PRO141
|
3.9
|
40.0
|
1.0
|
|
C
|
C:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
C:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
C:TRP143
|
4.0
|
40.0
|
1.0
|
|
CA
|
C:PHE104
|
4.0
|
40.0
|
1.0
|
|
O
|
C:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
C:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
C:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
C:PHE104
|
4.3
|
40.0
|
1.0
|
|
O
|
C:SER142
|
4.4
|
40.0
|
1.0
|
|
CA
|
C:ALA105
|
4.4
|
40.0
|
1.0
|
|
CB
|
C:TRP143
|
4.4
|
40.0
|
1.0
|
|
N
|
C:SER142
|
4.5
|
40.0
|
1.0
|
|
O
|
C:ALA140
|
4.5
|
40.0
|
1.0
|
|
N
|
C:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
C:LEU144
|
4.6
|
40.0
|
1.0
|
|
CE3
|
Q:TRP30
|
4.7
|
40.0
|
1.0
|
|
CA
|
C:MET103
|
4.7
|
40.0
|
1.0
|
|
N
|
C:GLY107
|
4.8
|
40.0
|
1.0
|
|
N
|
C:LEU106
|
4.9
|
40.0
|
1.0
|
|
CA
|
C:LEU144
|
4.9
|
40.0
|
1.0
|
|
O
|
C:ARG102
|
5.0
|
40.0
|
1.0
|
|
CA
|
C:PRO141
|
5.0
|
40.0
|
1.0
|
|
CZ2
|
Q:TRP30
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 4 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 4 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 4 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Ca1270
b:40.0
occ:1.00
|
O
|
D:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
D:MET103
|
2.7
|
40.0
|
1.0
|
|
O
|
D:ALA105
|
2.7
|
40.0
|
1.0
|
|
O
|
D:PRO141
|
2.7
|
40.0
|
1.0
|
|
CD1
|
D:LEU144
|
3.2
|
40.0
|
1.0
|
|
C
|
D:TRP143
|
3.5
|
40.0
|
1.0
|
|
N
|
D:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
D:MET103
|
3.7
|
40.0
|
1.0
|
|
C
|
D:PHE104
|
3.8
|
40.0
|
1.0
|
|
C
|
D:ALA105
|
3.8
|
40.0
|
1.0
|
|
CB
|
D:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
D:PRO141
|
3.9
|
40.0
|
1.0
|
|
C
|
D:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
D:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
D:TRP143
|
4.0
|
40.0
|
1.0
|
|
CA
|
D:PHE104
|
4.0
|
40.0
|
1.0
|
|
O
|
D:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
D:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
D:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
D:PHE104
|
4.3
|
40.0
|
1.0
|
|
O
|
D:SER142
|
4.4
|
40.0
|
1.0
|
|
CA
|
D:ALA105
|
4.4
|
40.0
|
1.0
|
|
CB
|
D:TRP143
|
4.4
|
40.0
|
1.0
|
|
N
|
D:SER142
|
4.5
|
40.0
|
1.0
|
|
O
|
D:ALA140
|
4.5
|
40.0
|
1.0
|
|
N
|
D:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
D:LEU144
|
4.6
|
40.0
|
1.0
|
|
CA
|
D:MET103
|
4.7
|
40.0
|
1.0
|
|
N
|
D:GLY107
|
4.8
|
40.0
|
1.0
|
|
N
|
D:LEU106
|
4.9
|
40.0
|
1.0
|
|
CA
|
D:LEU144
|
4.9
|
40.0
|
1.0
|
|
O
|
D:ARG102
|
5.0
|
40.0
|
1.0
|
|
CA
|
D:PRO141
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 5 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 5 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 5 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:Ca1270
b:40.0
occ:1.00
|
O
|
E:ALA105
|
2.5
|
40.0
|
1.0
|
|
O
|
E:PRO141
|
2.6
|
40.0
|
1.0
|
|
O
|
E:TRP143
|
2.8
|
40.0
|
1.0
|
|
CH2
|
R:TRP30
|
2.8
|
40.0
|
1.0
|
|
CZ3
|
R:TRP30
|
2.9
|
40.0
|
1.0
|
|
O
|
E:MET103
|
3.1
|
40.0
|
1.0
|
|
CD1
|
E:LEU144
|
3.3
|
40.0
|
1.0
|
|
N
|
E:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
E:TRP143
|
3.7
|
40.0
|
1.0
|
|
C
|
E:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
E:PRO141
|
3.7
|
40.0
|
1.0
|
|
CB
|
E:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
E:PHE104
|
3.9
|
40.0
|
1.0
|
|
N
|
E:ALA105
|
3.9
|
40.0
|
1.0
|
|
C
|
E:SER142
|
3.9
|
40.0
|
1.0
|
|
C
|
E:MET103
|
3.9
|
40.0
|
1.0
|
|
CZ2
|
R:TRP30
|
4.1
|
40.0
|
1.0
|
|
CA
|
E:TRP143
|
4.1
|
40.0
|
1.0
|
|
OG
|
E:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
E:SER142
|
4.2
|
40.0
|
1.0
|
|
O
|
E:PHE104
|
4.2
|
40.0
|
1.0
|
|
CA
|
E:PHE104
|
4.2
|
40.0
|
1.0
|
|
O
|
E:ALA140
|
4.3
|
40.0
|
1.0
|
|
CE3
|
R:TRP30
|
4.3
|
40.0
|
1.0
|
|
CA
|
E:ALA105
|
4.4
|
40.0
|
1.0
|
|
N
|
E:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
E:PHE104
|
4.4
|
40.0
|
1.0
|
|
N
|
E:GLY107
|
4.5
|
40.0
|
1.0
|
|
O
|
E:SER142
|
4.5
|
40.0
|
1.0
|
|
CB
|
E:TRP143
|
4.6
|
40.0
|
1.0
|
|
N
|
E:LEU144
|
4.7
|
40.0
|
1.0
|
|
N
|
E:LEU106
|
4.8
|
40.0
|
1.0
|
|
CG
|
E:LEU144
|
4.8
|
40.0
|
1.0
|
|
CA
|
E:PRO141
|
4.8
|
40.0
|
1.0
|
|
CA
|
E:MET103
|
5.0
|
40.0
|
1.0
|
|
O
|
E:ARG102
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 6 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 6 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 6 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:Ca1270
b:40.0
occ:1.00
|
O
|
F:ALA105
|
2.6
|
40.0
|
1.0
|
|
O
|
F:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
F:PRO141
|
2.7
|
40.0
|
1.0
|
|
O
|
F:MET103
|
2.8
|
40.0
|
1.0
|
|
CD1
|
F:LEU144
|
3.1
|
40.0
|
1.0
|
|
C
|
F:TRP143
|
3.5
|
40.0
|
1.0
|
|
N
|
F:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
F:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
F:PRO141
|
3.8
|
40.0
|
1.0
|
|
C
|
F:PHE104
|
3.8
|
40.0
|
1.0
|
|
CB
|
F:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
F:MET103
|
3.8
|
40.0
|
1.0
|
|
C
|
F:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
F:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
F:TRP143
|
4.0
|
40.0
|
1.0
|
|
O
|
F:PHE104
|
4.1
|
40.0
|
1.0
|
|
CA
|
F:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
F:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
F:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
F:PHE104
|
4.4
|
40.0
|
1.0
|
|
O
|
F:ALA140
|
4.4
|
40.0
|
1.0
|
|
CA
|
F:ALA105
|
4.4
|
40.0
|
1.0
|
|
O
|
F:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
F:SER142
|
4.4
|
40.0
|
1.0
|
|
CB
|
F:TRP143
|
4.5
|
40.0
|
1.0
|
|
N
|
F:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
F:LEU144
|
4.6
|
40.0
|
1.0
|
|
N
|
F:GLY107
|
4.6
|
40.0
|
1.0
|
|
N
|
F:LEU106
|
4.8
|
40.0
|
1.0
|
|
CA
|
F:PRO141
|
4.9
|
40.0
|
1.0
|
|
CA
|
F:LEU144
|
4.9
|
40.0
|
1.0
|
|
CA
|
F:MET103
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 7 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 7 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 7 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:Ca1270
b:40.0
occ:1.00
|
O
|
G:ALA105
|
2.5
|
40.0
|
1.0
|
|
O
|
G:PRO141
|
2.6
|
40.0
|
1.0
|
|
O
|
G:TRP143
|
2.8
|
40.0
|
1.0
|
|
O
|
G:MET103
|
3.1
|
40.0
|
1.0
|
|
CD1
|
G:LEU144
|
3.3
|
40.0
|
1.0
|
|
CZ3
|
P:TRP30
|
3.6
|
40.0
|
1.0
|
|
CH2
|
P:TRP30
|
3.6
|
40.0
|
1.0
|
|
N
|
G:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
G:TRP143
|
3.7
|
40.0
|
1.0
|
|
C
|
G:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
G:PRO141
|
3.7
|
40.0
|
1.0
|
|
CB
|
G:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
G:PHE104
|
3.9
|
40.0
|
1.0
|
|
C
|
G:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
G:ALA105
|
3.9
|
40.0
|
1.0
|
|
C
|
G:MET103
|
3.9
|
40.0
|
1.0
|
|
CA
|
G:TRP143
|
4.1
|
40.0
|
1.0
|
|
CA
|
G:SER142
|
4.2
|
40.0
|
1.0
|
|
OG
|
G:SER142
|
4.2
|
40.0
|
1.0
|
|
O
|
G:PHE104
|
4.2
|
40.0
|
1.0
|
|
CA
|
G:PHE104
|
4.2
|
40.0
|
1.0
|
|
O
|
G:ALA140
|
4.3
|
40.0
|
1.0
|
|
CA
|
G:ALA105
|
4.4
|
40.0
|
1.0
|
|
N
|
G:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
G:PHE104
|
4.4
|
40.0
|
1.0
|
|
N
|
G:GLY107
|
4.5
|
40.0
|
1.0
|
|
O
|
G:SER142
|
4.5
|
40.0
|
1.0
|
|
CB
|
G:TRP143
|
4.6
|
40.0
|
1.0
|
|
N
|
G:LEU144
|
4.7
|
40.0
|
1.0
|
|
N
|
G:LEU106
|
4.8
|
40.0
|
1.0
|
|
CG
|
G:LEU144
|
4.8
|
40.0
|
1.0
|
|
CA
|
G:PRO141
|
4.8
|
40.0
|
1.0
|
|
CE3
|
P:TRP30
|
4.9
|
40.0
|
1.0
|
|
CZ2
|
P:TRP30
|
4.9
|
40.0
|
1.0
|
|
CA
|
G:MET103
|
5.0
|
40.0
|
1.0
|
|
O
|
G:ARG102
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 8 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 8 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 8 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:Ca1270
b:40.0
occ:1.00
|
O
|
H:ALA105
|
2.6
|
40.0
|
1.0
|
|
O
|
H:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
H:PRO141
|
2.7
|
40.0
|
1.0
|
|
O
|
H:MET103
|
2.8
|
40.0
|
1.0
|
|
CD1
|
H:LEU144
|
3.1
|
40.0
|
1.0
|
|
C
|
H:TRP143
|
3.5
|
40.0
|
1.0
|
|
N
|
H:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
H:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
H:PRO141
|
3.8
|
40.0
|
1.0
|
|
C
|
H:PHE104
|
3.8
|
40.0
|
1.0
|
|
CB
|
H:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
H:MET103
|
3.8
|
40.0
|
1.0
|
|
C
|
H:SER142
|
3.9
|
40.0
|
1.0
|
|
N
|
H:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
H:TRP143
|
4.0
|
40.0
|
1.0
|
|
CA
|
H:PHE104
|
4.1
|
40.0
|
1.0
|
|
O
|
H:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
H:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
H:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
H:PHE104
|
4.4
|
40.0
|
1.0
|
|
O
|
H:ALA140
|
4.4
|
40.0
|
1.0
|
|
CA
|
H:ALA105
|
4.4
|
40.0
|
1.0
|
|
O
|
H:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
H:SER142
|
4.4
|
40.0
|
1.0
|
|
CB
|
H:TRP143
|
4.5
|
40.0
|
1.0
|
|
N
|
H:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
H:LEU144
|
4.6
|
40.0
|
1.0
|
|
N
|
H:GLY107
|
4.6
|
40.0
|
1.0
|
|
N
|
H:LEU106
|
4.8
|
40.0
|
1.0
|
|
CA
|
H:PRO141
|
4.9
|
40.0
|
1.0
|
|
CA
|
H:LEU144
|
4.9
|
40.0
|
1.0
|
|
CA
|
H:MET103
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 9 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 9 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 9 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
I:Ca1270
b:40.0
occ:1.00
|
O
|
I:TRP143
|
2.6
|
40.0
|
1.0
|
|
O
|
I:MET103
|
2.7
|
40.0
|
1.0
|
|
O
|
I:ALA105
|
2.7
|
40.0
|
1.0
|
|
O
|
I:PRO141
|
2.7
|
40.0
|
1.0
|
|
CD1
|
I:LEU144
|
3.2
|
40.0
|
1.0
|
|
C
|
I:TRP143
|
3.5
|
40.0
|
1.0
|
|
CZ3
|
S:TRP30
|
3.5
|
40.0
|
1.0
|
|
N
|
I:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
I:MET103
|
3.7
|
40.0
|
1.0
|
|
C
|
I:PHE104
|
3.8
|
40.0
|
1.0
|
|
C
|
I:ALA105
|
3.8
|
40.0
|
1.0
|
|
CB
|
I:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
I:SER142
|
3.9
|
40.0
|
1.0
|
|
C
|
I:PRO141
|
3.9
|
40.0
|
1.0
|
|
N
|
I:ALA105
|
3.9
|
40.0
|
1.0
|
|
CA
|
I:TRP143
|
4.0
|
40.0
|
1.0
|
|
CA
|
I:PHE104
|
4.0
|
40.0
|
1.0
|
|
CH2
|
S:TRP30
|
4.1
|
40.0
|
1.0
|
|
O
|
I:PHE104
|
4.1
|
40.0
|
1.0
|
|
OG
|
I:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
I:SER142
|
4.2
|
40.0
|
1.0
|
|
N
|
I:PHE104
|
4.3
|
40.0
|
1.0
|
|
CE3
|
S:TRP30
|
4.3
|
40.0
|
1.0
|
|
O
|
I:SER142
|
4.4
|
40.0
|
1.0
|
|
CA
|
I:ALA105
|
4.4
|
40.0
|
1.0
|
|
CB
|
I:TRP143
|
4.4
|
40.0
|
1.0
|
|
N
|
I:SER142
|
4.5
|
40.0
|
1.0
|
|
O
|
I:ALA140
|
4.5
|
40.0
|
1.0
|
|
N
|
I:LEU144
|
4.6
|
40.0
|
1.0
|
|
CG
|
I:LEU144
|
4.6
|
40.0
|
1.0
|
|
CA
|
I:MET103
|
4.7
|
40.0
|
1.0
|
|
N
|
I:GLY107
|
4.8
|
40.0
|
1.0
|
|
N
|
I:LEU106
|
4.9
|
40.0
|
1.0
|
|
CA
|
I:LEU144
|
4.9
|
40.0
|
1.0
|
|
O
|
I:ARG102
|
5.0
|
40.0
|
1.0
|
|
CA
|
I:PRO141
|
5.0
|
40.0
|
1.0
|
|
Calcium binding site 10 out
of 11 in 2w0c
Go back to
Calcium Binding Sites List in 2w0c
Calcium binding site 10 out
of 11 in the X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2
 Mono view
 Stereo pair view
|
|
A full contact list of Calcium with other atoms in the Ca binding
site number 10 of X-Ray Structure of the Entire Lipid-Containing Bacteriophage PM2 within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
J:Ca1270
b:40.0
occ:1.00
|
O
|
J:ALA105
|
2.5
|
40.0
|
1.0
|
|
O
|
J:PRO141
|
2.6
|
40.0
|
1.0
|
|
O
|
J:TRP143
|
2.8
|
40.0
|
1.0
|
|
O
|
J:MET103
|
3.1
|
40.0
|
1.0
|
|
CD1
|
J:LEU144
|
3.3
|
40.0
|
1.0
|
|
N
|
J:TRP143
|
3.6
|
40.0
|
1.0
|
|
C
|
J:TRP143
|
3.7
|
40.0
|
1.0
|
|
C
|
J:ALA105
|
3.7
|
40.0
|
1.0
|
|
C
|
J:PRO141
|
3.7
|
40.0
|
1.0
|
|
CB
|
J:SER142
|
3.8
|
40.0
|
1.0
|
|
C
|
J:PHE104
|
3.9
|
40.0
|
1.0
|
|
N
|
J:ALA105
|
3.9
|
40.0
|
1.0
|
|
C
|
J:SER142
|
3.9
|
40.0
|
1.0
|
|
C
|
J:MET103
|
3.9
|
40.0
|
1.0
|
|
CA
|
J:TRP143
|
4.1
|
40.0
|
1.0
|
|
OG
|
J:SER142
|
4.2
|
40.0
|
1.0
|
|
CA
|
J:SER142
|
4.2
|
40.0
|
1.0
|
|
O
|
J:PHE104
|
4.2
|
40.0
|
1.0
|
|
CA
|
J:PHE104
|
4.2
|
40.0
|
1.0
|
|
O
|
J:ALA140
|
4.3
|
40.0
|
1.0
|
|
CA
|
J:ALA105
|
4.4
|
40.0
|
1.0
|
|
N
|
J:SER142
|
4.4
|
40.0
|
1.0
|
|
N
|
J:PHE104
|
4.4
|
40.0
|
1.0
|
|
N
|
J:GLY107
|
4.5
|
40.0
|
1.0
|
|
O
|
J:SER142
|
4.5
|
40.0
|
1.0
|
|
CB
|
J:TRP143
|
4.6
|
40.0
|
1.0
|
|
N
|
J:LEU144
|
4.7
|
40.0
|
1.0
|
|
N
|
J:LEU106
|
4.8
|
40.0
|
1.0
|
|
CG
|
J:LEU144
|
4.8
|
40.0
|
1.0
|
|
CA
|
J:PRO141
|
4.8
|
40.0
|
1.0
|
|
CA
|
J:MET103
|
5.0
|
40.0
|
1.0
|
|
O
|
J:ARG102
|
5.0
|
40.0
|
1.0
|
|
Reference:
N.G.A.Abrescia,
J.M.Grimes,
H.M.Kivela,
R.Assenberg,
G.C.Sutton,
S.J.Butcher,
J.K.H.Bamford,
D.H.Bamford,
D.I.Stuart.
Insights Into Virus Evolution and Membrane Biogenesis From the Structure of the Marine Lipid-Containing Bacteriophage PM2 Mol.Cell V. 31 749 2008.
ISSN: ISSN 1097-2765
PubMed: 18775333
DOI: 10.1016/J.MOLCEL.2008.06.026
Page generated: Fri Jul 12 18:18:45 2024
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