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Iron in PDB 8cns: The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.

Enzymatic activity of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.

All present enzymatic activity of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.:
1.7.99.1;

Protein crystallography data

The structure of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution., PDB code: 8cns was solved by O.N.Lemaire, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 51.09 / 1.36
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 97.773, 102.186, 58.323, 90, 90, 90
R / Rfree (%) 12.9 / 16.6

Other elements in 8cns:

The structure of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Iron Binding Sites:

Pages:

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

Binding sites:

The binding sites of Iron atom in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. (pdb code 8cns). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution., PDB code: 8cns:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in 8cns

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Iron binding site 1 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe905

b:9.0
occ:1.00
 FE1 A:SF4905 0.0 9.0 1.0
S3 A:SF4905 2.3 10.0 1.0
S4 A:SF4905 2.3 9.6 1.0
SG A:CYS8 2.3 8.9 1.0
S2 A:SF4905 2.3 9.9 1.0
FE3 A:SF4905 2.7 9.0 1.0
FE2 A:SF4905 2.8 9.1 1.0
FE4 A:SF4905 2.8 9.3 1.0
CB A:CYS8 3.2 7.9 1.0
S1 A:SF4905 4.0 9.8 1.0
NZ A:LYS28 4.0 9.1 1.0
C A:CYS8 4.0 8.3 1.0
CG A:GLN10 4.1 8.0 1.0
O A:CYS8 4.2 9.4 1.0
CA A:CYS8 4.2 8.6 1.0
CE A:LYS28 4.2 9.5 1.0
N A:GLN10 4.2 8.3 1.0
N A:TYR9 4.4 8.3 1.0
NE2 A:GLN10 4.8 9.5 1.0
N A:CYS11 4.8 9.3 1.0
SG A:CYS20 4.8 9.9 1.0
CA A:TYR9 4.9 8.1 1.0
SG A:CYS11 4.9 9.1 1.0
SG A:CYS26 4.9 9.3 1.0
C A:TYR9 5.0 8.3 1.0
CD A:GLN10 5.0 8.9 1.0
O A:HOH1304 5.0 8.8 1.0

Iron binding site 2 out of 12 in 8cns

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Iron binding site 2 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe905

b:9.1
occ:1.00
 FE2 A:SF4905 0.0 9.1 1.0
SG A:CYS11 2.2 9.1 1.0
S4 A:SF4905 2.3 9.6 1.0
S1 A:SF4905 2.3 9.8 1.0
S3 A:SF4905 2.4 10.0 1.0
FE4 A:SF4905 2.7 9.3 1.0
FE3 A:SF4905 2.7 9.0 1.0
FE1 A:SF4905 2.8 9.0 1.0
CB A:CYS11 3.2 8.9 1.0
N A:CYS11 3.8 9.3 1.0
S2 A:SF4905 3.9 9.9 1.0
CA A:CYS11 4.0 8.3 1.0
OG1 A:THR73 4.3 8.2 1.0
CG2 A:THR73 4.5 9.8 1.0
N A:THR14 4.5 8.2 1.0
C A:CYS11 4.5 8.3 1.0
O A:CYS11 4.5 9.6 1.0
O A:HOH1139 4.5 10.6 1.0
CA A:THR14 4.6 8.0 1.0
SG A:CYS26 4.7 9.3 1.0
CB A:THR14 4.8 8.9 1.0
C A:GLU13 4.9 8.6 1.0
N A:GLN10 4.9 8.3 1.0
C A:GLN10 4.9 8.1 1.0
SG A:CYS20 4.9 9.9 1.0
SG A:CYS8 4.9 8.9 1.0
CG A:GLN10 4.9 8.0 1.0
CB A:CYS26 4.9 10.5 1.0

Iron binding site 3 out of 12 in 8cns

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Iron binding site 3 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe905

b:9.0
occ:1.00
 FE3 A:SF4905 0.0 9.0 1.0
S1 A:SF4905 2.3 9.8 1.0
S2 A:SF4905 2.3 9.9 1.0
SG A:CYS20 2.3 9.9 1.0
S4 A:SF4905 2.4 9.6 1.0
FE4 A:SF4905 2.7 9.3 1.0
FE1 A:SF4905 2.7 9.0 1.0
FE2 A:SF4905 2.7 9.1 1.0
CB A:CYS20 3.3 8.9 1.0
S3 A:SF4905 3.9 10.0 1.0
N A:VAL25 4.0 10.0 1.0
CA A:THR14 4.1 8.0 1.0
OG1 A:THR14 4.1 10.0 1.0
CA A:GLY24 4.1 10.0 1.0
O A:CYS8 4.2 9.4 1.0
CB A:THR14 4.4 8.9 1.0
CA A:CYS20 4.6 9.5 1.0
C A:GLY24 4.6 9.3 1.0
N A:CYS20 4.7 9.6 1.0
CB A:CYS8 4.7 7.9 1.0
SG A:CYS11 4.7 9.1 1.0
SG A:CYS8 4.7 8.9 1.0
N A:THR14 4.7 8.2 1.0
C A:CYS8 4.8 8.3 1.0
SG A:CYS26 4.8 9.3 1.0
CB A:VAL25 4.8 11.3 1.0
N A:ALA15 4.9 8.6 1.0
N A:CYS26 4.9 9.5 1.0
CA A:VAL25 4.9 10.3 1.0

Iron binding site 4 out of 12 in 8cns

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Iron binding site 4 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe905

b:9.3
occ:1.00
 FE4 A:SF4905 0.0 9.3 1.0
S2 A:SF4905 2.3 9.9 1.0
SG A:CYS26 2.3 9.3 1.0
S1 A:SF4905 2.3 9.8 1.0
S3 A:SF4905 2.4 10.0 1.0
FE2 A:SF4905 2.7 9.1 1.0
FE3 A:SF4905 2.7 9.0 1.0
FE1 A:SF4905 2.8 9.0 1.0
CB A:CYS26 3.3 10.5 1.0
N A:CYS26 3.9 9.5 1.0
S4 A:SF4905 3.9 9.6 1.0
CA A:GLY24 4.2 10.0 1.0
O A:HOH1374 4.2 8.7 1.0
CA A:CYS26 4.3 10.2 1.0
CE A:LYS28 4.4 9.5 1.0
N A:VAL25 4.5 10.0 1.0
CB A:LYS28 4.5 10.5 1.0
SG A:CYS11 4.6 9.1 1.0
C A:GLY24 4.6 9.3 1.0
SG A:CYS20 4.8 9.9 1.0
O A:HOH1139 4.8 10.6 1.0
CG2 A:THR73 4.8 9.8 1.0
NZ A:LYS28 4.8 9.1 1.0
SG A:CYS8 4.9 8.9 1.0

Iron binding site 5 out of 12 in 8cns

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Iron binding site 5 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe906

b:15.0
occ:0.40
 FE1 A:SF3906 0.0 15.0 0.4
FE5 A:VQ8925 0.2 5.4 0.5
O10 A:VQ8925 1.9 11.8 0.5
S5 A:VQ8925 2.1 5.8 0.5
S2 A:SF3906 2.3 5.9 0.4
S1 A:SF3906 2.3 16.6 0.4
S3 A:SF3906 2.3 16.1 0.4
S6 A:VQ8925 2.4 7.9 0.5
SG A:CYS430 2.5 10.1 1.0
FE6 A:VQ8925 2.8 6.9 0.5
FE3 A:SF3906 2.8 17.5 0.4
FE4 A:SF3906 2.9 10.3 0.4
FE8 A:VQ8925 3.2 12.8 0.5
CB A:CYS430 3.5 8.8 1.0
FE7 A:VQ8925 3.6 7.0 0.5
O8 A:VQ8925 3.6 7.8 0.5
CG A:GLU267 3.6 7.5 1.0
FE7 A:SF3906 3.8 9.8 0.4
O9 A:VQ8925 4.0 6.8 0.5
CD1 A:TRP291 4.1 8.9 1.0
N A:CYS430 4.2 9.0 1.0
CD A:GLU267 4.4 7.9 1.0
CA A:CYS430 4.4 8.2 1.0
SG A:CSS402 4.5 12.6 0.6
OE2 A:GLU267 4.5 8.7 1.0
CB A:CSS402 4.6 12.2 0.6
NE1 A:TRP291 4.6 10.4 1.0
NE2 A:HIS243 4.6 8.5 1.0
CE1 A:HIS243 4.6 7.8 1.0
OG A:SER266 4.8 9.1 1.0
CB A:CSS402 4.8 7.4 0.5
CA A:CSS402 4.8 11.1 0.6
CB A:GLU267 4.9 6.7 1.0
SG A:CYS311 4.9 9.7 1.0
CA A:CSS402 4.9 7.0 0.5
SG A:CSS402 4.9 8.8 0.5

Iron binding site 6 out of 12 in 8cns

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Iron binding site 6 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe906

b:17.5
occ:0.40
 FE3 A:SF3906 0.0 17.5 0.4
FE6 A:VQ8925 0.3 6.9 0.5
O8 A:VQ8925 1.8 7.8 0.5
S1 A:SF3906 2.3 16.6 0.4
S3 A:SF3906 2.3 16.1 0.4
S5 A:VQ8925 2.3 5.8 0.5
S6 A:VQ8925 2.4 7.9 0.5
SG A:CYS311 2.4 9.7 1.0
FE1 A:SF3906 2.8 15.0 0.4
FE8 A:VQ8925 2.8 12.8 0.5
FE5 A:VQ8925 2.8 5.4 0.5
CB A:CYS311 3.4 9.6 1.0
N A:CYS311 3.5 7.8 1.0
FE4 A:SF3906 3.7 10.3 0.4
O10 A:VQ8925 3.7 11.8 0.5
C A:ASN310 4.0 7.2 1.0
CA A:CYS311 4.0 7.8 1.0
OE2 A:GLU490 4.0 13.5 0.6
CD1 A:TRP291 4.1 8.9 1.0
O9 A:VQ8925 4.1 6.8 0.5
O A:ASN310 4.2 7.9 1.0
ND2 A:ASN310 4.3 11.8 1.0
CG A:ASN310 4.4 9.9 1.0
S2 A:SF3906 4.4 5.9 0.4
NE1 A:TRP291 4.4 10.4 1.0
CE1 A:HIS243 4.5 7.8 1.0
CB A:ASN310 4.6 8.5 1.0
CG A:TRP291 4.6 8.2 1.0
CG A:GLU490 4.7 11.7 0.4
CG A:GLU490 4.8 11.2 0.6
SG A:CYS430 4.8 10.1 1.0
OD1 A:ASN310 4.8 9.6 1.0
FE7 A:VQ8925 4.8 7.0 0.5
CD A:GLU490 4.8 12.6 0.6
CA A:ASN310 4.9 8.3 1.0
CD2 A:TYR489 5.0 9.3 1.0

Iron binding site 7 out of 12 in 8cns

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Iron binding site 7 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe906

b:10.3
occ:0.40
 FE4 A:SF3906 0.0 10.3 0.4
FE8 A:VQ8925 1.7 12.8 0.5
SG A:CSS402 2.0 12.6 0.6
SD A:CSS402 2.1 11.4 0.6
S6 A:VQ8925 2.2 7.9 0.5
S3 A:SF3906 2.3 16.1 0.4
S2 A:SF3906 2.3 5.9 0.4
O10 A:VQ8925 2.5 11.8 0.5
SG A:CSS402 2.5 8.8 0.5
CB A:CSS402 2.7 12.2 0.6
FE5 A:VQ8925 2.8 5.4 0.5
FE1 A:SF3906 2.9 15.0 0.4
O9 A:VQ8925 2.9 6.8 0.5
CB A:CSS402 3.3 7.4 0.5
FE7 A:VQ8925 3.5 7.0 0.5
OE2 A:GLU490 3.6 11.6 0.4
O8 A:VQ8925 3.6 7.8 0.5
OE2 A:GLU490 3.6 13.5 0.6
FE3 A:SF3906 3.7 17.5 0.4
FE6 A:VQ8925 3.8 6.9 0.5
CA A:CSS402 3.8 11.1 0.6
FE7 A:SF3906 3.8 9.8 0.4
CA A:CSS402 3.9 7.0 0.5
CD A:GLU490 4.0 11.8 0.4
CG A:GLU490 4.1 11.7 0.4
CD A:GLU490 4.3 12.6 0.6
CG A:GLU490 4.3 11.2 0.6
SG A:CYS430 4.4 10.1 1.0
S5 A:VQ8925 4.6 5.8 0.5
N A:CSS402 4.7 7.2 0.5
N A:CSS402 4.7 10.7 0.6
S1 A:SF3906 4.7 16.6 0.4
SG A:CYS455 4.7 9.8 1.0
C A:CSS402 4.8 10.9 0.6
OE1 A:GLU490 4.8 11.1 0.4
CB A:CYS455 4.9 9.3 1.0

Iron binding site 8 out of 12 in 8cns

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Iron binding site 8 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe906

b:9.8
occ:0.40
 FE7 A:SF3906 0.0 9.8 0.4
FE7 A:VQ8925 0.3 7.0 0.5
O10 A:VQ8925 2.0 11.8 0.5
OE2 A:GLU267 2.0 8.7 1.0
NE2 A:HIS243 2.1 8.5 1.0
O9 A:VQ8925 2.3 6.8 0.5
SG A:CYS455 2.3 9.8 1.0
S2 A:SF3906 2.3 5.9 0.4
CD A:GLU267 3.0 7.9 1.0
CD2 A:HIS243 3.0 8.2 1.0
CE1 A:HIS243 3.2 7.8 1.0
CB A:CYS455 3.2 9.3 1.0
CG A:GLU267 3.3 7.5 1.0
FE8 A:VQ8925 3.7 12.8 0.5
N A:CYS455 3.7 7.8 1.0
FE1 A:SF3906 3.8 15.0 0.4
FE4 A:SF3906 3.8 10.3 0.4
FE5 A:VQ8925 3.9 5.4 0.5
CA A:CYS455 4.1 8.2 1.0
OE1 A:GLU267 4.2 8.4 1.0
CB A:GLU267 4.2 6.7 1.0
CG A:HIS243 4.2 6.9 1.0
ND1 A:HIS243 4.3 7.0 1.0
O8 A:VQ8925 4.3 7.8 0.5
NZ A:LYS492 4.5 8.2 1.0
SG A:CSS402 4.7 12.6 0.6
CA A:GLY429 4.7 8.5 1.0
S1 A:SF3906 4.7 16.6 0.4
S5 A:VQ8925 4.8 5.8 0.5
C A:GLN454 4.9 8.4 1.0
N A:CYS430 4.9 9.0 1.0

Iron binding site 9 out of 12 in 8cns

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Iron binding site 9 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe925

b:5.4
occ:0.53
 FE5 A:VQ8925 0.0 5.4 0.5
FE1 A:SF3906 0.2 15.0 0.4
O10 A:VQ8925 2.0 11.8 0.5
S3 A:SF3906 2.2 16.1 0.4
S5 A:VQ8925 2.3 5.8 0.5
S2 A:SF3906 2.3 5.9 0.4
S6 A:VQ8925 2.3 7.9 0.5
SG A:CYS430 2.3 10.1 1.0
S1 A:SF3906 2.5 16.6 0.4
FE6 A:VQ8925 2.8 6.9 0.5
FE4 A:SF3906 2.8 10.3 0.4
FE3 A:SF3906 2.8 17.5 0.4
FE8 A:VQ8925 3.3 12.8 0.5
CB A:CYS430 3.4 8.8 1.0
O8 A:VQ8925 3.7 7.8 0.5
FE7 A:VQ8925 3.7 7.0 0.5
CG A:GLU267 3.8 7.5 1.0
FE7 A:SF3906 3.9 9.8 0.4
CD1 A:TRP291 4.0 8.9 1.0
O9 A:VQ8925 4.1 6.8 0.5
N A:CYS430 4.1 9.0 1.0
SG A:CSS402 4.3 12.6 0.6
CB A:CSS402 4.4 12.2 0.6
CA A:CYS430 4.4 8.2 1.0
NE1 A:TRP291 4.5 10.4 1.0
CD A:GLU267 4.6 7.9 1.0
CB A:CSS402 4.6 7.4 0.5
CA A:CSS402 4.6 11.1 0.6
OE2 A:GLU267 4.6 8.7 1.0
CA A:CSS402 4.7 7.0 0.5
SG A:CSS402 4.8 8.8 0.5
N A:ASP403 4.8 9.9 0.5
NE2 A:HIS243 4.8 8.5 1.0
CE1 A:HIS243 4.9 7.8 1.0
SG A:CYS311 4.9 9.7 1.0
OG A:SER266 4.9 9.1 1.0
SD A:CSS402 4.9 11.4 0.6
N A:ASP403 4.9 7.9 0.5

Iron binding site 10 out of 12 in 8cns

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Iron binding site 10 out of 12 in the The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of The Hybrid Cluster Protein From the Thermophilic Methanogen Methanothermococcus Thermolithotrophicus in A Mixed Redox State After Soaking with Hydroxylamine, at 1.36-A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe925

b:6.9
occ:0.53
 FE6 A:VQ8925 0.0 6.9 0.5
FE3 A:SF3906 0.3 17.5 0.4
O8 A:VQ8925 2.0 7.8 0.5
S3 A:SF3906 2.2 16.1 0.4
SG A:CYS311 2.3 9.7 1.0
S1 A:SF3906 2.3 16.6 0.4
S6 A:VQ8925 2.3 7.9 0.5
S5 A:VQ8925 2.3 5.8 0.5
FE1 A:SF3906 2.8 15.0 0.4
FE5 A:VQ8925 2.8 5.4 0.5
FE8 A:VQ8925 3.0 12.8 0.5
CB A:CYS311 3.3 9.6 1.0
N A:CYS311 3.5 7.8 1.0
FE4 A:SF3906 3.8 10.3 0.4
CD1 A:TRP291 3.8 8.9 1.0
O10 A:VQ8925 3.8 11.8 0.5
CA A:CYS311 3.9 7.8 1.0
C A:ASN310 4.1 7.2 1.0
NE1 A:TRP291 4.2 10.4 1.0
OE2 A:GLU490 4.2 13.5 0.6
CG A:TRP291 4.3 8.2 1.0
O9 A:VQ8925 4.3 6.8 0.5
O A:ASN310 4.4 7.9 1.0
S2 A:SF3906 4.5 5.9 0.4
ND2 A:ASN310 4.5 11.8 1.0
CG A:ASN310 4.6 9.9 1.0
SG A:CYS430 4.7 10.1 1.0
CB A:ASN310 4.7 8.5 1.0
CE1 A:HIS243 4.7 7.8 1.0
CG A:GLU490 4.8 11.7 0.4
CG A:GLU490 4.8 11.2 0.6
CE2 A:TRP291 4.8 9.6 1.0
CB A:TRP291 4.8 8.3 1.0
CD2 A:TYR489 4.9 9.3 1.0
CD2 A:TRP291 4.9 9.4 1.0
CD A:GLU490 5.0 12.6 0.6
FE7 A:VQ8925 5.0 7.0 0.5

Reference:

O.N.Lemaire, M.Belhamri, T.Wagner. Structural and Biochemical Elucidation of Class I Hybrid Cluster Protein Natively Extracted From A Marine Methanogenic Archaeon To Be Published.
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