Atomistry » Manganese » PDB 1w2c-1xie » 1woi
Atomistry »
  Manganese »
    PDB 1w2c-1xie »
      1woi »

Manganese in PDB 1woi: Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Enzymatic activity of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

All present enzymatic activity of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily:
3.5.3.11;

Protein crystallography data

The structure of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily, PDB code: 1woi was solved by H.J.Ahn, K.H.Kim, J.Lee, J.-Y.Ha, H.H.Lee, D.Kim, H.-J.Yoon, A.-R.Kwon, S.W.Suh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.99 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 81.764, 130.759, 168.746, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 24.1

Manganese Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Manganese atom in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily (pdb code 1woi). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 12 binding sites of Manganese where determined in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily, PDB code: 1woi:
Jump to Manganese binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Manganese binding site 1 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 1 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1501

b:28.2
occ:1.00
 ND1 A:HIS121 2.0 13.2 1.0
OD2 A:ASP147 2.1 22.5 1.0
OD2 A:ASP143 2.1 14.9 1.0
OD2 A:ASP229 2.2 11.7 1.0
O A:HOH1636 2.4 25.6 1.0
CE1 A:HIS121 2.9 11.5 1.0
CG A:ASP143 2.9 15.1 1.0
MN A:MN1502 3.0 21.5 1.0
OD1 A:ASP143 3.1 12.1 1.0
CG A:HIS121 3.1 13.4 1.0
CG A:ASP147 3.2 17.8 1.0
CG A:ASP229 3.3 11.3 1.0
CB A:HIS121 3.6 13.1 1.0
CB A:ASP229 3.7 9.6 1.0
OD1 A:ASP147 3.8 19.4 1.0
NE2 A:HIS121 4.0 14.0 1.0
CD2 A:HIS121 4.2 12.5 1.0
CB A:ASP143 4.3 12.1 1.0
OD1 A:ASP229 4.4 13.7 1.0
CB A:ASP147 4.4 15.6 1.0
O A:HIS145 4.7 12.1 1.0
ND1 A:HIS145 4.7 12.8 1.0
CG A:GLU274 4.7 12.8 1.0
NE2 A:GLN141 4.8 10.5 1.0
OD2 A:ASP231 4.8 15.2 1.0
CB A:HIS145 4.8 13.0 1.0
OD1 A:ASP231 4.9 9.7 1.0
O A:ASN159 4.9 10.8 1.0

Manganese binding site 2 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 2 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn1502

b:21.5
occ:1.00
 OD2 A:ASP231 2.2 15.2 1.0
OD1 A:ASP143 2.3 12.1 1.0
ND1 A:HIS145 2.3 12.8 1.0
OD2 A:ASP229 2.3 11.7 1.0
OD1 A:ASP231 2.4 9.7 1.0
O A:HOH1636 2.6 25.6 1.0
CG A:ASP231 2.6 13.3 1.0
MN A:MN1501 3.0 28.2 1.0
CG A:ASP229 3.1 11.3 1.0
CE1 A:HIS145 3.1 16.8 1.0
CG A:ASP143 3.3 15.1 1.0
CG A:HIS145 3.4 14.3 1.0
OD1 A:ASP229 3.5 13.7 1.0
OD2 A:ASP143 3.6 14.9 1.0
CB A:HIS145 3.8 13.0 1.0
N A:HIS145 3.9 11.0 1.0
N A:ALA144 4.1 10.8 1.0
CB A:ASP229 4.1 9.6 1.0
CB A:ASP231 4.2 11.0 1.0
NE2 A:HIS145 4.3 15.5 1.0
OD2 A:ASP147 4.4 22.5 1.0
CA A:HIS145 4.4 12.3 1.0
CD2 A:HIS145 4.5 13.6 1.0
CB A:ASP143 4.6 12.1 1.0
O A:HOH1520 4.7 12.0 1.0
CB A:ALA144 4.7 10.1 1.0
C A:ALA144 4.8 10.1 1.0
CA A:ALA144 4.8 11.1 1.0
CA A:ASP143 4.8 11.3 1.0
ND1 A:HIS121 4.9 13.2 1.0
C A:ASP143 4.9 10.8 1.0
OD1 A:ASP147 5.0 19.4 1.0
CG A:GLU274 5.0 12.8 1.0

Manganese binding site 3 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 3 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1503

b:42.2
occ:1.00
 OD2 B:ASP147 2.1 25.1 1.0
ND1 B:HIS121 2.1 18.1 1.0
OD2 B:ASP229 2.1 14.6 1.0
OD2 B:ASP143 2.3 19.5 1.0
O B:HOH1601 2.6 31.4 1.0
MN B:MN1504 2.9 35.4 1.0
CE1 B:HIS121 3.0 15.8 1.0
CG B:ASP143 3.1 16.7 1.0
OD1 B:ASP143 3.2 16.9 1.0
CG B:HIS121 3.2 17.3 1.0
CG B:ASP147 3.2 20.1 1.0
CG B:ASP229 3.2 17.2 1.0
CB B:HIS121 3.6 16.8 1.0
CB B:ASP229 3.7 16.2 1.0
OD1 B:ASP147 3.8 22.4 1.0
NE2 B:HIS121 4.1 18.9 1.0
CD2 B:HIS121 4.2 15.7 1.0
OD1 B:ASP229 4.3 16.6 1.0
CB B:ASP147 4.4 18.3 1.0
CB B:ASP143 4.5 16.0 1.0
CG B:GLU274 4.6 15.8 1.0
O B:ASN159 4.7 14.7 1.0
OD2 B:ASP231 4.8 19.1 1.0
NE2 B:GLN141 4.8 20.6 1.0
O B:HIS145 4.8 16.8 1.0
CB B:HIS145 4.9 20.5 1.0
ND1 B:HIS145 4.9 24.7 1.0
O B:HOH1581 4.9 32.3 1.0
OD1 B:ASP231 5.0 17.8 1.0

Manganese binding site 4 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 4 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 4 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mn1504

b:35.4
occ:1.00
 OD2 B:ASP231 2.3 19.1 1.0
OD1 B:ASP143 2.4 16.9 1.0
OD2 B:ASP229 2.4 14.6 1.0
OD1 B:ASP231 2.5 17.8 1.0
ND1 B:HIS145 2.6 24.7 1.0
CG B:ASP231 2.7 16.0 1.0
O B:HOH1601 2.9 31.4 1.0
MN B:MN1503 2.9 42.2 1.0
CG B:ASP229 3.1 17.2 1.0
CG B:ASP143 3.4 16.7 1.0
CE1 B:HIS145 3.5 24.7 1.0
OD1 B:ASP229 3.5 16.6 1.0
CG B:HIS145 3.6 23.4 1.0
OD2 B:ASP143 3.7 19.5 1.0
CB B:HIS145 3.9 20.5 1.0
N B:HIS145 4.0 14.8 1.0
CB B:ASP229 4.1 16.2 1.0
N B:ALA144 4.2 14.8 1.0
CB B:ASP231 4.2 14.1 1.0
OD2 B:ASP147 4.2 25.1 1.0
CA B:HIS145 4.6 17.1 1.0
NE2 B:HIS145 4.6 24.1 1.0
CB B:ASP143 4.7 16.0 1.0
CD2 B:HIS145 4.7 22.6 1.0
O B:HOH1521 4.8 18.1 1.0
ND1 B:HIS121 4.8 18.1 1.0
CB B:ALA144 4.8 14.7 1.0
C B:ALA144 4.9 14.2 1.0
CA B:ASP143 4.9 15.8 1.0
CG B:GLU274 4.9 15.8 1.0
CA B:ALA144 4.9 13.2 1.0

Manganese binding site 5 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 5 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 5 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1505

b:36.2
occ:1.00
 ND1 C:HIS121 2.0 15.9 1.0
OD2 C:ASP229 2.1 14.6 1.0
OD2 C:ASP147 2.1 22.4 1.0
OD2 C:ASP143 2.2 18.0 1.0
O C:HOH1630 2.6 31.4 1.0
CE1 C:HIS121 2.9 12.8 1.0
MN C:MN1506 2.9 32.6 1.0
CG C:ASP143 3.0 15.6 1.0
OD1 C:ASP143 3.1 15.1 1.0
CG C:HIS121 3.1 12.2 1.0
CG C:ASP229 3.2 12.5 1.0
CG C:ASP147 3.3 20.8 1.0
CB C:HIS121 3.6 11.7 1.0
CB C:ASP229 3.6 14.1 1.0
OD1 C:ASP147 3.8 24.1 1.0
NE2 C:HIS121 4.0 15.8 1.0
CD2 C:HIS121 4.2 12.8 1.0
OD1 C:ASP229 4.3 13.8 1.0
CB C:ASP143 4.4 13.9 1.0
CB C:ASP147 4.5 18.3 1.0
CG C:GLU274 4.7 13.4 1.0
O C:HIS145 4.7 15.5 1.0
NE2 C:GLN141 4.7 21.2 1.0
OD2 C:ASP231 4.9 16.8 1.0
ND1 C:HIS145 4.9 25.5 1.0
OD1 C:ASP231 4.9 11.4 1.0
O C:HOH1611 4.9 33.8 1.0

Manganese binding site 6 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 6 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 6 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Mn1506

b:32.6
occ:1.00
 OD2 C:ASP229 2.2 14.6 1.0
OD1 C:ASP143 2.3 15.1 1.0
OD2 C:ASP231 2.3 16.8 1.0
ND1 C:HIS145 2.5 25.5 1.0
OD1 C:ASP231 2.5 11.4 1.0
O C:HOH1630 2.7 31.4 1.0
CG C:ASP231 2.7 12.6 1.0
MN C:MN1505 2.9 36.2 1.0
CG C:ASP229 3.0 12.5 1.0
CG C:ASP143 3.2 15.6 1.0
CE1 C:HIS145 3.3 25.6 1.0
OD1 C:ASP229 3.5 13.8 1.0
CG C:HIS145 3.5 24.0 1.0
OD2 C:ASP143 3.6 18.0 1.0
CB C:HIS145 3.9 22.0 1.0
N C:HIS145 3.9 15.4 1.0
CB C:ASP229 4.0 14.1 1.0
N C:ALA144 4.1 14.7 1.0
OD2 C:ASP147 4.2 22.4 1.0
CB C:ASP231 4.3 12.1 1.0
NE2 C:HIS145 4.5 27.5 1.0
CA C:HIS145 4.5 17.5 1.0
CB C:ASP143 4.5 13.9 1.0
CD2 C:HIS145 4.6 26.3 1.0
CA C:ASP143 4.7 14.1 1.0
O C:HOH1517 4.8 12.5 1.0
ND1 C:HIS121 4.8 15.9 1.0
O C:HIS145 4.8 15.5 1.0
CB C:ALA144 4.8 15.4 1.0
C C:ALA144 4.9 15.9 1.0
OD1 C:ASP147 4.9 24.1 1.0
CA C:ALA144 4.9 14.3 1.0
C C:ASP143 4.9 14.1 1.0
CG C:GLU274 5.0 13.4 1.0
CG C:ASP147 5.0 20.8 1.0

Manganese binding site 7 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 7 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 7 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn1507

b:42.7
occ:1.00
 ND1 D:HIS121 2.0 13.7 1.0
OD2 D:ASP147 2.1 25.8 1.0
OD2 D:ASP143 2.2 18.0 1.0
OD2 D:ASP229 2.2 15.3 1.0
O D:HOH1600 2.8 33.6 1.0
CE1 D:HIS121 2.9 13.2 1.0
CG D:ASP143 3.0 16.5 1.0
MN D:MN1508 3.1 28.9 1.0
OD1 D:ASP143 3.1 14.0 1.0
CG D:HIS121 3.1 13.8 1.0
CG D:ASP147 3.2 20.6 1.0
CG D:ASP229 3.3 15.7 1.0
CB D:HIS121 3.6 14.1 1.0
CB D:ASP229 3.7 14.9 1.0
OD1 D:ASP147 3.8 19.0 1.0
NE2 D:HIS121 4.0 13.4 1.0
CD2 D:HIS121 4.1 13.6 1.0
OD1 D:ASP229 4.4 12.9 1.0
CB D:ASP143 4.4 16.0 1.0
CB D:ASP147 4.4 18.7 1.0
O D:ASN159 4.7 14.8 1.0
NE2 D:GLN141 4.7 17.1 1.0
CG D:GLU274 4.7 14.8 1.0
O D:HIS145 4.8 17.6 1.0
OD2 D:ASP231 4.9 18.0 1.0
ND1 D:HIS145 4.9 26.0 1.0
OD1 D:ASP231 4.9 16.3 1.0

Manganese binding site 8 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 8 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 8 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Mn1508

b:28.9
occ:1.00
 OD2 D:ASP231 2.2 18.0 1.0
OD2 D:ASP229 2.3 15.3 1.0
OD1 D:ASP143 2.3 14.0 1.0
ND1 D:HIS145 2.4 26.0 1.0
OD1 D:ASP231 2.5 16.3 1.0
CG D:ASP231 2.7 13.8 1.0
O D:HOH1600 3.1 33.6 1.0
CG D:ASP229 3.1 15.7 1.0
MN D:MN1507 3.1 42.7 1.0
CE1 D:HIS145 3.2 26.9 1.0
CG D:ASP143 3.3 16.5 1.0
CG D:HIS145 3.5 24.3 1.0
OD1 D:ASP229 3.5 12.9 1.0
OD2 D:ASP143 3.7 18.0 1.0
CB D:HIS145 3.9 20.8 1.0
N D:HIS145 4.0 15.8 1.0
CB D:ASP229 4.1 14.9 1.0
N D:ALA144 4.1 15.2 1.0
CB D:ASP231 4.2 12.9 1.0
OD2 D:ASP147 4.2 25.8 1.0
NE2 D:HIS145 4.4 25.8 1.0
CA D:HIS145 4.5 18.0 1.0
CD2 D:HIS145 4.6 25.1 1.0
CB D:ASP143 4.6 16.0 1.0
O D:HOH1524 4.7 15.5 1.0
CB D:ALA144 4.7 14.6 1.0
CA D:ASP143 4.8 16.3 1.0
C D:ALA144 4.8 16.2 1.0
CA D:ALA144 4.8 15.0 1.0
OD1 D:ASP147 4.9 19.0 1.0
ND1 D:HIS121 4.9 13.7 1.0
C D:ASP143 4.9 16.1 1.0

Manganese binding site 9 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 9 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 9 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn1509

b:73.8
occ:1.00
 OD2 E:ASP147 2.1 28.9 1.0
ND1 E:HIS121 2.1 17.1 1.0
OD2 E:ASP229 2.2 19.6 1.0
O E:HOH1616 2.4 27.7 1.0
OD2 E:ASP143 2.4 22.1 1.0
MN E:MN1510 3.0 37.5 1.0
CE1 E:HIS121 3.1 12.2 1.0
CG E:HIS121 3.1 16.2 1.0
CG E:ASP147 3.2 25.8 1.0
CG E:ASP143 3.2 20.3 1.0
OD1 E:ASP143 3.3 17.2 1.0
CG E:ASP229 3.4 19.6 1.0
CB E:HIS121 3.5 16.5 1.0
OD1 E:ASP147 3.7 26.3 1.0
CB E:ASP229 3.9 18.5 1.0
NE2 E:HIS121 4.2 17.2 1.0
CD2 E:HIS121 4.2 14.7 1.0
CB E:ASP147 4.3 22.1 1.0
OD1 E:ASP229 4.4 16.6 1.0
CB E:ASP143 4.6 17.2 1.0
O E:ASN159 4.6 16.5 1.0
CG E:GLU274 4.7 18.2 1.0
OD2 E:ASP231 4.8 21.9 1.0
NE2 E:GLN141 4.9 23.4 1.0
O E:HIS145 4.9 23.3 1.0
ND1 E:HIS145 5.0 33.0 1.0
CA E:HIS121 5.0 14.6 1.0

Manganese binding site 10 out of 12 in 1woi

Go back to Manganese Binding Sites List in 1woi
Manganese binding site 10 out of 12 in the Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 10 of Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mn1510

b:37.5
occ:1.00
 OD2 E:ASP231 2.3 21.9 1.0
OD1 E:ASP143 2.4 17.2 1.0
OD2 E:ASP229 2.5 19.6 1.0
ND1 E:HIS145 2.5 33.0 1.0
O E:HOH1616 2.5 27.7 1.0
OD1 E:ASP231 2.6 19.1 1.0
CG E:ASP231 2.8 18.7 1.0
MN E:MN1509 3.0 73.8 1.0
CG E:ASP229 3.2 19.6 1.0
CE1 E:HIS145 3.3 34.3 1.0
CG E:ASP143 3.4 20.3 1.0
CG E:HIS145 3.5 31.1 1.0
OD1 E:ASP229 3.6 16.6 1.0
OD2 E:ASP143 3.7 22.1 1.0
CB E:HIS145 3.9 26.7 1.0
N E:HIS145 4.1 22.0 1.0
OD2 E:ASP147 4.1 28.9 1.0
CB E:ASP229 4.3 18.5 1.0
N E:ALA144 4.3 20.6 1.0
CB E:ASP231 4.3 18.4 1.0
NE2 E:HIS145 4.4 33.7 1.0
CD2 E:HIS145 4.5 32.0 1.0
CA E:HIS145 4.6 23.1 1.0
O E:HOH1582 4.7 20.0 1.0
CB E:ASP143 4.7 17.2 1.0
CB E:ALA144 4.8 20.5 1.0
OD1 E:ASP147 4.8 26.3 1.0
CG E:ASP147 4.9 25.8 1.0
C E:ALA144 4.9 21.3 1.0
ND1 E:HIS121 4.9 17.1 1.0
CA E:ALA144 4.9 20.6 1.0
CG E:GLU274 5.0 18.2 1.0

Reference:

H.J.Ahn, K.H.Kim, J.Lee, J.-Y.Ha, H.H.Lee, D.Kim, H.-J.Yoon, A.-R.Kwon, S.W.Suh. Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily J.Biol.Chem. V. 279 50505 2004.
ISSN: ISSN 0021-9258
PubMed: 15355972
DOI: 10.1074/JBC.M409246200
Page generated: Sat Oct 5 12:56:56 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy