Atomistry » Iron » PDB 4a9v-4b2y » 4aun
Atomistry »
  Iron »
    PDB 4a9v-4b2y »
      4aun »

Iron in PDB 4aun: Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum

Enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum

All present enzymatic activity of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum:
1.11.1.6;

Protein crystallography data

The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aun was solved by Y.Yuzugullu, C.H.Trinh, M.A.Smith, A.R.Pearson, S.E.V.Phillips, D.Sutay Kocabas, U.Bakir, Z.B.Ogel, M.J.Mcpherson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 69.94 / 1.92
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 253.370, 243.290, 97.060, 90.00, 104.16, 90.00
R / Rfree (%) 16.422 / 20.054

Other elements in 4aun:

The structure of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum also contains other interesting chemical elements:

Calcium (Ca) 9 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum (pdb code 4aun). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum, PDB code: 4aun:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 1 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe900

b:16.1
occ:1.00
FE A:HDD900 0.0 16.1 1.0
ND A:HDD900 1.9 15.0 1.0
OH A:TYR369 2.0 11.0 1.0
NA A:HDD900 2.1 13.0 1.0
NC A:HDD900 2.1 13.3 1.0
NB A:HDD900 2.1 14.1 1.0
O A:HOH2085 2.3 16.1 0.3
C4D A:HDD900 2.9 16.6 1.0
C1D A:HDD900 2.9 15.5 1.0
CZ A:TYR369 3.0 10.0 1.0
C1A A:HDD900 3.1 13.4 1.0
C4C A:HDD900 3.1 13.7 1.0
C4A A:HDD900 3.1 12.4 1.0
C1C A:HDD900 3.1 12.7 1.0
C4B A:HDD900 3.1 13.5 1.0
C1B A:HDD900 3.1 13.5 1.0
CHA A:HDD900 3.3 14.0 1.0
CHD A:HDD900 3.3 13.1 1.0
CHB A:HDD900 3.5 11.6 1.0
CHC A:HDD900 3.5 12.1 1.0
CE1 A:TYR369 3.8 10.9 1.0
CE2 A:TYR369 3.9 10.5 1.0
NE A:ARG365 4.2 10.5 1.0
NH2 A:ARG365 4.2 11.0 1.0
C3D A:HDD900 4.2 19.5 1.0
C2D A:HDD900 4.3 19.2 1.0
C3C A:HDD900 4.4 12.1 1.0
O A:HOH2086 4.4 25.2 1.0
C2A A:HDD900 4.4 11.2 1.0
C3A A:HDD900 4.4 11.2 1.0
CG2 A:VAL81 4.4 11.2 1.0
C3B A:HDD900 4.4 13.8 1.0
C2C A:HDD900 4.4 13.1 1.0
C2B A:HDD900 4.5 12.4 1.0
CZ A:PHE168 4.5 9.4 1.0
CZ A:ARG365 4.6 11.6 1.0
CE1 A:HIS82 4.7 10.3 1.0
ND1 A:HIS82 4.8 11.5 1.0
O1D A:HDD900 5.0 24.2 1.0

Iron binding site 2 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 2 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe900

b:16.9
occ:1.00
FE B:HDD900 0.0 16.9 1.0
OH B:TYR369 1.9 10.2 1.0
ND B:HDD900 1.9 15.0 1.0
NA B:HDD900 2.1 13.8 1.0
NB B:HDD900 2.1 15.2 1.0
NC B:HDD900 2.1 13.5 1.0
O B:HOH2057 2.3 11.1 0.3
C4D B:HDD900 2.9 15.7 1.0
C1D B:HDD900 3.0 16.8 1.0
CZ B:TYR369 3.0 10.1 1.0
C4C B:HDD900 3.1 14.6 1.0
C1A B:HDD900 3.1 13.3 1.0
C4A B:HDD900 3.1 12.9 1.0
C1C B:HDD900 3.1 14.2 1.0
C4B B:HDD900 3.1 14.8 1.0
C1B B:HDD900 3.1 14.3 1.0
CHA B:HDD900 3.3 14.4 1.0
CHD B:HDD900 3.4 14.2 1.0
CHB B:HDD900 3.5 12.7 1.0
CHC B:HDD900 3.5 13.6 1.0
CE1 B:TYR369 3.8 10.5 1.0
CE2 B:TYR369 3.8 10.5 1.0
NE B:ARG365 4.2 13.2 1.0
C3D B:HDD900 4.3 17.2 1.0
C2D B:HDD900 4.3 18.1 1.0
NH2 B:ARG365 4.3 12.9 1.0
C3C B:HDD900 4.4 14.2 1.0
C2A B:HDD900 4.4 12.2 1.0
C3B B:HDD900 4.4 14.3 1.0
C3A B:HDD900 4.4 12.4 1.0
C2C B:HDD900 4.4 14.4 1.0
CG2 B:VAL81 4.4 9.9 1.0
C2B B:HDD900 4.4 14.5 1.0
O B:HOH2058 4.5 20.4 1.0
CZ B:ARG365 4.7 13.5 1.0
CZ B:PHE168 4.7 10.8 1.0
CE1 B:HIS82 4.7 10.3 1.0
ND1 B:HIS82 4.8 12.1 1.0

Iron binding site 3 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 3 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe900

b:15.9
occ:1.00
FE C:HDD900 0.0 15.9 1.0
OH C:TYR369 1.9 8.3 1.0
ND C:HDD900 1.9 14.5 1.0
NA C:HDD900 2.1 12.7 1.0
NC C:HDD900 2.1 13.3 1.0
NB C:HDD900 2.1 15.0 1.0
O C:HOH2469 2.3 10.1 0.4
C4D C:HDD900 2.9 14.9 1.0
C1D C:HDD900 2.9 15.4 1.0
CZ C:TYR369 3.0 9.2 1.0
C1A C:HDD900 3.0 11.7 1.0
C4C C:HDD900 3.1 14.1 1.0
C4A C:HDD900 3.1 12.1 1.0
C1C C:HDD900 3.1 13.4 1.0
C4B C:HDD900 3.1 14.4 1.0
C1B C:HDD900 3.1 14.1 1.0
CHA C:HDD900 3.3 12.6 1.0
CHD C:HDD900 3.4 14.0 1.0
CHC C:HDD900 3.5 14.0 1.0
CHB C:HDD900 3.5 12.2 1.0
CE2 C:TYR369 3.7 8.6 1.0
CE1 C:TYR369 3.8 8.4 1.0
NE C:ARG365 4.1 10.4 1.0
NH2 C:ARG365 4.2 9.3 1.0
C3D C:HDD900 4.3 16.1 1.0
C2D C:HDD900 4.3 17.2 1.0
O C:HOH2075 4.3 17.9 1.0
C3C C:HDD900 4.4 14.0 1.0
C2A C:HDD900 4.4 10.4 1.0
C3A C:HDD900 4.4 10.8 1.0
C3B C:HDD900 4.4 14.9 1.0
C2C C:HDD900 4.4 13.8 1.0
C2B C:HDD900 4.5 13.8 1.0
CG2 C:VAL81 4.5 10.4 1.0
CZ C:ARG365 4.6 9.8 1.0
CZ C:PHE168 4.6 10.8 1.0
CE1 C:HIS82 4.8 9.6 1.0
ND1 C:HIS82 4.9 9.2 1.0
O1D C:HDD900 5.0 18.2 1.0
CD2 C:TYR369 5.0 9.1 1.0

Iron binding site 4 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 4 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe900

b:15.2
occ:1.00
FE D:HDD900 0.0 15.2 1.0
ND D:HDD900 1.9 13.2 1.0
OH D:TYR369 2.0 9.4 1.0
NC D:HDD900 2.1 11.4 1.0
NA D:HDD900 2.1 11.3 1.0
NB D:HDD900 2.1 11.8 1.0
O D:HOH2079 2.5 7.5 0.3
C4D D:HDD900 2.9 13.4 1.0
C1D D:HDD900 2.9 14.3 1.0
CZ D:TYR369 3.0 9.3 1.0
C4C D:HDD900 3.0 11.9 1.0
C1A D:HDD900 3.1 11.4 1.0
C1C D:HDD900 3.1 11.0 1.0
C4B D:HDD900 3.1 11.3 1.0
C4A D:HDD900 3.1 10.8 1.0
C1B D:HDD900 3.1 11.1 1.0
CHA D:HDD900 3.3 12.2 1.0
CHD D:HDD900 3.4 12.3 1.0
CHC D:HDD900 3.4 10.3 1.0
CHB D:HDD900 3.4 10.5 1.0
CE1 D:TYR369 3.8 9.0 1.0
CE2 D:TYR369 3.8 9.8 1.0
NE D:ARG365 4.2 9.0 1.0
C3D D:HDD900 4.3 16.3 1.0
C2D D:HDD900 4.3 16.4 1.0
NH2 D:ARG365 4.3 9.6 1.0
C3C D:HDD900 4.4 11.7 1.0
C3B D:HDD900 4.4 11.3 1.0
C2A D:HDD900 4.4 10.1 1.0
C3A D:HDD900 4.4 10.4 1.0
C2C D:HDD900 4.4 10.8 1.0
C2B D:HDD900 4.4 10.8 1.0
CG2 D:VAL81 4.5 7.8 1.0
CZ D:PHE168 4.5 9.3 1.0
O D:HOH2080 4.6 14.7 1.0
CZ D:ARG365 4.7 9.3 1.0
CE1 D:HIS82 4.7 8.7 1.0
ND1 D:HIS82 4.8 9.3 1.0
O1D D:HDD900 5.0 18.3 1.0

Iron binding site 5 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 5 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Fe900

b:16.0
occ:1.00
FE E:HDD900 0.0 16.0 1.0
ND E:HDD900 1.9 15.2 1.0
OH E:TYR369 2.0 12.0 1.0
NA E:HDD900 2.1 12.7 1.0
NC E:HDD900 2.1 14.3 1.0
NB E:HDD900 2.1 14.3 1.0
O E:HOH2038 2.5 10.4 0.3
C4D E:HDD900 2.9 15.0 1.0
C1D E:HDD900 2.9 15.8 1.0
CZ E:TYR369 3.0 11.3 1.0
C1A E:HDD900 3.1 12.7 1.0
C4C E:HDD900 3.1 14.2 1.0
C4A E:HDD900 3.1 12.0 1.0
C4B E:HDD900 3.1 13.9 1.0
C1B E:HDD900 3.1 14.1 1.0
C1C E:HDD900 3.1 14.0 1.0
CHA E:HDD900 3.3 13.7 1.0
CHD E:HDD900 3.4 15.1 1.0
CHB E:HDD900 3.4 12.5 1.0
CHC E:HDD900 3.5 13.7 1.0
CE2 E:TYR369 3.7 11.2 1.0
CE1 E:TYR369 3.8 11.8 1.0
NE E:ARG365 4.2 12.6 1.0
NH2 E:ARG365 4.2 13.9 1.0
C3D E:HDD900 4.3 19.5 1.0
C2D E:HDD900 4.3 19.7 1.0
C2A E:HDD900 4.4 11.7 1.0
C3C E:HDD900 4.4 13.5 1.0
C3A E:HDD900 4.4 11.0 1.0
CG2 E:VAL81 4.4 10.7 1.0
C3B E:HDD900 4.4 14.2 1.0
C2B E:HDD900 4.5 13.6 1.0
C2C E:HDD900 4.5 14.0 1.0
O E:HOH2039 4.5 23.2 1.0
CZ E:PHE168 4.5 11.4 1.0
CZ E:ARG365 4.6 14.7 1.0
CE1 E:HIS82 4.7 11.9 1.0
ND1 E:HIS82 4.7 14.2 1.0
CD2 E:TYR369 5.0 11.2 1.0

Iron binding site 6 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 6 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Fe900

b:15.1
occ:1.00
FE F:HDD900 0.0 15.1 1.0
ND F:HDD900 1.9 14.4 1.0
OH F:TYR369 2.0 9.8 1.0
NA F:HDD900 2.1 11.7 1.0
NC F:HDD900 2.1 12.3 1.0
NB F:HDD900 2.1 13.1 1.0
O F:HOH2380 2.5 10.0 0.4
C4D F:HDD900 2.9 13.6 1.0
C1D F:HDD900 3.0 14.8 1.0
CZ F:TYR369 3.0 9.8 1.0
C4C F:HDD900 3.0 12.7 1.0
C1A F:HDD900 3.1 11.6 1.0
C4A F:HDD900 3.1 10.6 1.0
C4B F:HDD900 3.1 12.2 1.0
C1C F:HDD900 3.1 11.5 1.0
C1B F:HDD900 3.1 12.0 1.0
CHA F:HDD900 3.3 13.0 1.0
CHD F:HDD900 3.4 13.0 1.0
CHB F:HDD900 3.5 10.7 1.0
CHC F:HDD900 3.5 11.3 1.0
CE1 F:TYR369 3.8 9.8 1.0
CE2 F:TYR369 3.8 10.1 1.0
NE F:ARG365 4.2 10.8 1.0
NH2 F:ARG365 4.2 11.3 1.0
O F:HOH2052 4.2 28.3 1.0
C3D F:HDD900 4.3 15.7 1.0
C2D F:HDD900 4.3 16.5 1.0
C3C F:HDD900 4.4 12.1 1.0
C2A F:HDD900 4.4 10.8 1.0
C3B F:HDD900 4.4 11.9 1.0
C3A F:HDD900 4.4 10.5 1.0
CG2 F:VAL81 4.4 9.1 1.0
C2C F:HDD900 4.4 11.9 1.0
C2B F:HDD900 4.5 12.0 1.0
CE1 F:HIS82 4.6 8.6 1.0
CZ F:PHE168 4.6 7.7 1.0
CZ F:ARG365 4.6 12.4 1.0
ND1 F:HIS82 4.7 9.0 1.0

Iron binding site 7 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 7 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Fe900

b:16.6
occ:1.00
FE G:HDD900 0.0 16.6 1.0
OH G:TYR369 1.9 11.5 1.0
ND G:HDD900 1.9 14.7 1.0
NA G:HDD900 2.1 13.2 1.0
NC G:HDD900 2.1 14.0 1.0
NB G:HDD900 2.1 14.0 1.0
O G:HOH2057 2.5 8.7 0.3
C4D G:HDD900 2.9 14.9 1.0
C1D G:HDD900 2.9 15.6 1.0
CZ G:TYR369 3.0 11.0 1.0
C1A G:HDD900 3.1 13.1 1.0
C4C G:HDD900 3.1 14.3 1.0
C4A G:HDD900 3.1 12.6 1.0
C1C G:HDD900 3.1 14.3 1.0
C4B G:HDD900 3.1 14.4 1.0
C1B G:HDD900 3.1 13.6 1.0
CHA G:HDD900 3.3 13.9 1.0
CHD G:HDD900 3.3 14.0 1.0
CHB G:HDD900 3.4 12.1 1.0
CHC G:HDD900 3.5 13.6 1.0
CE1 G:TYR369 3.8 11.4 1.0
CE2 G:TYR369 3.8 11.7 1.0
NE G:ARG365 4.2 12.5 1.0
NH2 G:ARG365 4.2 12.4 1.0
C3D G:HDD900 4.3 16.3 1.0
C2D G:HDD900 4.3 17.4 1.0
C3C G:HDD900 4.4 14.9 1.0
C2A G:HDD900 4.4 11.3 1.0
C3A G:HDD900 4.4 11.6 1.0
C3B G:HDD900 4.4 13.9 1.0
O G:HOH2058 4.4 15.2 1.0
C2C G:HDD900 4.4 14.7 1.0
CG2 G:VAL81 4.5 10.2 1.0
C2B G:HDD900 4.5 12.8 1.0
CZ G:PHE168 4.6 13.9 1.0
CZ G:ARG365 4.6 13.2 1.0
CE1 G:HIS82 4.6 12.0 1.0
ND1 G:HIS82 4.8 13.5 1.0
O1D G:HDD900 5.0 19.1 1.0

Iron binding site 8 out of 8 in 4aun

Go back to Iron Binding Sites List in 4aun
Iron binding site 8 out of 8 in the Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure, Recombinant Expression and Mutagenesis Studies of the Bifunctional Catalase-Phenol Oxidase From Scytalidium Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Fe900

b:16.5
occ:1.00
FE H:HDD900 0.0 16.5 1.0
ND H:HDD900 1.9 13.7 1.0
OH H:TYR369 2.0 11.3 1.0
NA H:HDD900 2.1 12.2 1.0
NB H:HDD900 2.1 13.7 1.0
NC H:HDD900 2.1 12.9 1.0
O H:HOH2349 2.6 11.7 0.3
C4D H:HDD900 2.9 16.0 1.0
C1D H:HDD900 2.9 15.6 1.0
CZ H:TYR369 3.0 10.3 1.0
C4C H:HDD900 3.1 13.2 1.0
C1A H:HDD900 3.1 12.4 1.0
C4B H:HDD900 3.1 13.0 1.0
C4A H:HDD900 3.1 11.4 1.0
C1C H:HDD900 3.1 12.8 1.0
C1B H:HDD900 3.1 12.7 1.0
CHA H:HDD900 3.3 13.6 1.0
CHD H:HDD900 3.4 13.1 1.0
CHB H:HDD900 3.4 11.4 1.0
CHC H:HDD900 3.5 13.1 1.0
CE2 H:TYR369 3.8 10.4 1.0
CE1 H:TYR369 3.8 10.7 1.0
NE H:ARG365 4.1 10.9 1.0
NH2 H:ARG365 4.2 10.8 1.0
C3D H:HDD900 4.2 19.2 1.0
C2D H:HDD900 4.3 18.8 1.0
O H:HOH2030 4.4 25.3 1.0
C3C H:HDD900 4.4 12.7 1.0
C2A H:HDD900 4.4 10.8 1.0
C3B H:HDD900 4.4 13.6 1.0
C3A H:HDD900 4.4 10.4 1.0
C2B H:HDD900 4.4 12.9 1.0
C2C H:HDD900 4.4 13.0 1.0
CG2 H:VAL81 4.5 8.7 1.0
CZ H:ARG365 4.6 10.8 1.0
CZ H:PHE168 4.6 12.7 1.0
CE1 H:HIS82 4.7 9.4 1.0
ND1 H:HIS82 4.7 10.5 1.0
O1D H:HDD900 5.0 23.5 1.0
CD2 H:TYR369 5.0 9.6 1.0

Reference:

Y.Yuzugullu, C.H.Trinh, M.A.Smith, A.R.Pearson, S.E.V.Phillips, D.Sutay Kocabas, U.Bakir, Z.B.Ogel, M.J.Mcpherson. Structure, Recombinant Expression and Mutagenesis Studies of the Catalase with Oxidase Activity From Scytalidium Thermophilum Acta Crystallogr.,Sect.D V. 69 398 2013.
ISSN: ISSN 0907-4449
PubMed: 23519415
DOI: 10.1107/S0907444912049001
Page generated: Sun Aug 4 23:45:52 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy