Iron in PDB 3e1n: Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).

The structure of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr)., PDB code: 3e1n was solved by A.Crow, T.Lawson, A.Lewin, G.R.Moore, N.Le Brun, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	32.67 / 2.80
Space group	P 42 21 2
Cell size a, b, c (Å), α, β, γ (°)	207.741, 207.741, 142.951, 90.00, 90.00, 90.00
R / Rfree (%)	25 / 26.8

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). (pdb code 3e1n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 30 binding sites of Iron where determined in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr)., PDB code: 3e1n:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe300 b:30.0 occ:1.00 OE1 A:GLU127 1.9 16.4 1.0 OE1 A:GLU18 2.1 17.6 1.0 OE2 A:GLU51 2.1 19.3 1.0 ND1 A:HIS54 2.4 12.3 1.0 OE2 A:GLU18 2.5 19.4 1.0 CD A:GLU18 2.6 17.0 1.0 CD A:GLU127 2.9 16.1 1.0 O A:UNK400 2.9 5.3 1.0 CD A:GLU51 3.0 16.4 1.0 OE2 A:GLU127 3.2 17.1 1.0 CE1 A:HIS54 3.2 13.2 1.0 CG A:HIS54 3.5 11.2 1.0 OE1 A:GLU51 3.5 19.4 1.0 FE A:FE2301 3.6 34.4 1.0 CB A:HIS54 3.8 10.1 1.0 CG A:GLU18 4.1 13.9 1.0 O A:HOH402 4.1 10.0 1.0 CG A:GLU51 4.2 12.9 1.0 CG A:GLU127 4.2 14.6 1.0 CA A:GLU51 4.3 11.5 1.0 NE2 A:HIS54 4.4 10.2 1.0 CG2 A:ILE123 4.4 7.1 1.0 CB A:GLU51 4.4 11.9 1.0 CD2 A:HIS54 4.5 10.7 1.0 CE1 A:HIS130 4.8 17.5 1.0 CB A:GLU18 4.8 11.7 1.0 CA A:GLU18 5.0 11.7 1.0

Iron binding site 2 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe301 b:34.4 occ:1.00 OE1 A:GLU51 2.0 19.4 1.0 OE2 A:GLU127 2.0 17.1 1.0 OE2 A:GLU94 2.2 19.4 1.0 OE1 A:GLU94 2.3 20.0 1.0 ND1 A:HIS130 2.4 16.5 1.0 CD A:GLU94 2.5 17.1 1.0 O A:UNK400 2.6 5.3 1.0 CD A:GLU127 3.0 16.1 1.0 CD A:GLU51 3.0 16.4 1.0 CE1 A:HIS130 3.1 17.5 1.0 OE2 A:GLU51 3.4 19.3 1.0 OE1 A:GLU127 3.5 16.4 1.0 CG A:HIS130 3.6 15.3 1.0 FE A:FE2300 3.6 30.0 1.0 CG A:GLU94 4.0 11.8 1.0 OH A:TYR25 4.0 15.1 0.3 CB A:HIS130 4.1 11.2 1.0 O A:HOH401 4.1 2.5 1.0 CG A:GLU127 4.2 14.6 1.0 CE2 A:TYR25 4.2 14.3 0.3 CA A:GLU127 4.3 11.4 1.0 CG A:GLU51 4.3 12.9 1.0 NE2 A:HIS130 4.3 17.3 1.0 OH A:TYR25 4.4 15.2 0.7 CE2 A:TYR25 4.4 14.4 0.7 CB A:GLU127 4.4 11.2 1.0 CD2 A:HIS130 4.6 17.2 1.0 CZ A:TYR25 4.7 15.0 0.3 CB A:GLU94 4.8 9.4 1.0 CZ A:TYR25 4.9 15.1 0.7

Iron binding site 3 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe200 b:2.0 occ:0.04 FE A:HEM200 0.0 2.0 0.0 NC A:HEM200 2.0 2.0 0.0 NB A:HEM200 2.1 2.0 0.0 ND A:HEM200 2.1 2.0 0.0 NA A:HEM200 2.1 2.0 0.0 SD A:MET52 2.2 15.7 1.0 SD B:MET52 2.3 15.7 1.0 C4C A:HEM200 3.1 2.0 0.0 C1C A:HEM200 3.1 2.0 0.0 C4B A:HEM200 3.1 2.0 0.0 C1D A:HEM200 3.1 2.0 0.0 C1B A:HEM200 3.1 2.0 0.0 C4D A:HEM200 3.1 2.0 0.0 C1A A:HEM200 3.1 2.0 0.0 C4A A:HEM200 3.2 2.0 0.0 CE A:MET52 3.2 13.0 1.0 CE B:MET52 3.2 13.0 1.0 CHD A:HEM200 3.4 2.0 0.0 CHC A:HEM200 3.4 2.0 0.0 CHA A:HEM200 3.5 2.0 0.0 CHB A:HEM200 3.5 2.0 0.0 CG A:MET52 3.5 12.6 1.0 CG B:MET52 3.6 12.5 1.0 C3C A:HEM200 4.3 2.0 0.0 C2C A:HEM200 4.3 2.0 0.0 C3B A:HEM200 4.3 2.0 0.0 C2B A:HEM200 4.3 2.0 0.0 C2D A:HEM200 4.3 2.0 0.0 C3D A:HEM200 4.4 2.0 0.0 C2A A:HEM200 4.4 2.0 0.0 C3A A:HEM200 4.4 2.0 0.0 CB A:MET52 4.4 11.2 1.0 CB B:MET52 4.4 11.2 1.0

Iron binding site 4 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe300 b:29.9 occ:1.00 OE1 B:GLU127 1.9 16.4 1.0 OE1 B:GLU18 2.0 17.6 1.0 OE2 B:GLU51 2.1 19.3 1.0 ND1 B:HIS54 2.4 12.3 1.0 OE2 B:GLU18 2.5 19.4 1.0 O B:UNK400 2.5 2.0 1.0 CD B:GLU18 2.6 17.0 1.0 CD B:GLU127 2.9 16.1 1.0 CD B:GLU51 3.0 16.4 1.0 CE1 B:HIS54 3.2 13.2 1.0 OE2 B:GLU127 3.2 17.1 1.0 CG B:HIS54 3.4 11.2 1.0 OE1 B:GLU51 3.5 19.4 1.0 FE B:FE2301 3.6 34.4 1.0 CB B:HIS54 3.8 10.1 1.0 CG B:GLU18 4.1 13.9 1.0 CG B:GLU51 4.2 12.9 1.0 CG B:GLU127 4.3 14.5 1.0 CA B:GLU51 4.3 11.5 1.0 NE2 B:HIS54 4.4 10.2 1.0 CG2 B:ILE123 4.4 7.1 1.0 CB B:GLU51 4.4 11.9 1.0 CD2 B:HIS54 4.5 10.7 1.0 CE1 B:HIS130 4.8 17.5 1.0 CB B:GLU18 4.8 11.7 1.0 CA B:GLU18 4.9 11.7 1.0

Iron binding site 5 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe301 b:34.4 occ:1.00 OE1 B:GLU51 2.0 19.4 1.0 OE2 B:GLU127 2.0 17.1 1.0 OE2 B:GLU94 2.2 19.4 1.0 OE1 B:GLU94 2.4 20.0 1.0 ND1 B:HIS130 2.4 16.5 1.0 CD B:GLU94 2.6 17.1 1.0 O B:UNK400 2.7 2.0 1.0 CD B:GLU51 3.0 16.4 1.0 CD B:GLU127 3.0 16.1 1.0 CE1 B:HIS130 3.1 17.5 1.0 OE2 B:GLU51 3.4 19.3 1.0 OE1 B:GLU127 3.5 16.4 1.0 CG B:HIS130 3.6 15.3 1.0 FE B:FE2300 3.6 29.9 1.0 CG B:GLU94 4.0 11.8 1.0 OH B:TYR25 4.1 15.1 0.3 CB B:HIS130 4.1 11.2 1.0 CE2 B:TYR25 4.2 14.3 0.3 CG B:GLU127 4.2 14.5 1.0 CG B:GLU51 4.3 12.9 1.0 NE2 B:HIS130 4.3 17.3 1.0 CA B:GLU127 4.3 11.4 1.0 OH B:TYR25 4.4 15.2 0.7 CE2 B:TYR25 4.4 14.4 0.7 CB B:GLU127 4.4 11.2 1.0 CD2 B:HIS130 4.6 17.1 1.0 CZ B:TYR25 4.6 15.0 0.3 CB B:GLU94 4.9 9.4 1.0 CZ B:TYR25 4.9 15.1 0.7

Iron binding site 6 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe300 b:30.0 occ:1.00 OE1 C:GLU127 1.9 16.4 1.0 OE1 C:GLU18 2.0 17.6 1.0 OE2 C:GLU51 2.1 19.3 1.0 ND1 C:HIS54 2.4 12.3 1.0 OE2 C:GLU18 2.5 19.4 1.0 CD C:GLU18 2.6 17.0 1.0 O C:UNK400 2.6 2.0 1.0 CD C:GLU127 2.9 16.1 1.0 CD C:GLU51 3.0 16.4 1.0 OE2 C:GLU127 3.2 17.1 1.0 CE1 C:HIS54 3.3 13.2 1.0 OE1 C:GLU51 3.5 19.4 1.0 CG C:HIS54 3.5 11.2 1.0 FE C:FE2301 3.6 34.4 1.0 CB C:HIS54 3.9 10.1 1.0 CG C:GLU18 4.1 13.9 1.0 CG C:GLU51 4.2 12.9 1.0 CG C:GLU127 4.2 14.5 1.0 CA C:GLU51 4.3 11.5 1.0 CB C:GLU51 4.4 11.9 1.0 NE2 C:HIS54 4.4 10.2 1.0 CG2 C:ILE123 4.5 7.1 1.0 O C:HOH414 4.5 13.5 1.0 CD2 C:HIS54 4.6 10.7 1.0 CE1 C:HIS130 4.8 17.5 1.0 CB C:GLU18 4.8 11.7 1.0 CA C:GLU18 4.9 11.8 1.0

Iron binding site 7 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe301 b:34.4 occ:1.00 OE2 C:GLU127 1.9 17.1 1.0 OE1 C:GLU51 2.0 19.4 1.0 OE2 C:GLU94 2.2 19.4 1.0 OE1 C:GLU94 2.4 20.0 1.0 ND1 C:HIS130 2.4 16.5 1.0 CD C:GLU94 2.6 17.1 1.0 O C:UNK400 2.9 2.0 1.0 CD C:GLU127 2.9 16.1 1.0 CD C:GLU51 3.0 16.4 1.0 CE1 C:HIS130 3.1 17.5 1.0 OE2 C:GLU51 3.4 19.3 1.0 OE1 C:GLU127 3.4 16.4 1.0 FE C:FE2300 3.6 30.0 1.0 CG C:HIS130 3.6 15.3 1.0 CB C:HIS130 4.1 11.2 1.0 CG C:GLU94 4.1 11.8 1.0 OH C:TYR25 4.1 15.1 0.3 CG C:GLU127 4.2 14.5 1.0 CA C:GLU127 4.3 11.4 1.0 CE2 C:TYR25 4.3 14.3 0.3 NE2 C:HIS130 4.3 17.3 1.0 CG C:GLU51 4.3 12.9 1.0 CB C:GLU127 4.4 11.2 1.0 OH C:TYR25 4.4 15.2 0.7 CE2 C:TYR25 4.5 14.4 0.7 CD2 C:HIS130 4.6 17.2 1.0 CZ C:TYR25 4.7 15.0 0.3 CB C:GLU94 4.9 9.4 1.0 O C:GLU127 5.0 10.7 1.0

Iron binding site 8 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe300 b:30.0 occ:1.00 OE1 D:GLU127 1.9 16.4 1.0 OE2 D:GLU51 2.0 19.2 1.0 OE1 D:GLU18 2.0 17.6 1.0 ND1 D:HIS54 2.4 12.3 1.0 OE2 D:GLU18 2.6 19.4 1.0 CD D:GLU18 2.6 17.0 1.0 CD D:GLU127 2.9 16.1 1.0 O D:UNK400 2.9 2.0 1.0 CD D:GLU51 2.9 16.5 1.0 OE2 D:GLU127 3.2 17.1 1.0 CE1 D:HIS54 3.2 13.2 1.0 OE1 D:GLU51 3.4 19.4 1.0 CG D:HIS54 3.5 11.2 1.0 FE D:FE2301 3.6 34.4 1.0 CB D:HIS54 3.8 10.1 1.0 CG D:GLU18 4.1 13.9 1.0 CG D:GLU51 4.2 12.9 1.0 O D:HOH405 4.3 8.6 1.0 CG D:GLU127 4.3 14.5 1.0 CA D:GLU51 4.3 11.5 1.0 CB D:GLU51 4.4 11.9 1.0 NE2 D:HIS54 4.4 10.3 1.0 CG2 D:ILE123 4.5 7.1 1.0 CD2 D:HIS54 4.5 10.8 1.0 CE1 D:HIS130 4.7 17.5 1.0 CB D:GLU18 4.8 11.7 1.0 CA D:GLU18 4.9 11.8 1.0 ND1 D:HIS130 5.0 16.5 1.0

Iron binding site 9 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe301 b:34.4 occ:1.00 OE2 D:GLU127 2.0 17.1 1.0 OE1 D:GLU51 2.0 19.4 1.0 OE2 D:GLU94 2.2 19.4 1.0 OE1 D:GLU94 2.3 20.0 1.0 ND1 D:HIS130 2.4 16.5 1.0 CD D:GLU94 2.6 17.1 1.0 O D:UNK400 2.9 2.0 1.0 CD D:GLU127 2.9 16.1 1.0 CD D:GLU51 3.0 16.5 1.0 CE1 D:HIS130 3.1 17.5 1.0 OE2 D:GLU51 3.4 19.2 1.0 OE1 D:GLU127 3.5 16.4 1.0 FE D:FE2300 3.6 30.0 1.0 CG D:HIS130 3.6 15.3 1.0 CG D:GLU94 4.1 11.8 1.0 CB D:HIS130 4.1 11.2 1.0 OH D:TYR25 4.1 15.1 0.3 CG D:GLU127 4.2 14.5 1.0 CE2 D:TYR25 4.3 14.3 0.3 CA D:GLU127 4.3 11.4 1.0 CG D:GLU51 4.4 12.9 1.0 NE2 D:HIS130 4.4 17.3 1.0 CB D:GLU127 4.4 11.2 1.0 OH D:TYR25 4.4 15.2 0.7 CE2 D:TYR25 4.5 14.4 0.7 CD2 D:HIS130 4.6 17.2 1.0 CZ D:TYR25 4.7 15.0 0.3 CB D:GLU94 4.9 9.4 1.0

Iron binding site 10 out of 30 in the Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr).


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of E. Coli Bacterioferritin (Bfr) After A 65 Minute (Aerobic) Exposure to Fe(II) Revealing A Possible Mu-Oxo Bridge/Mu-Hydroxy Bridged Diiron Intermediate at the Ferroxidase Centre. (Fe(III)-O-Fe(III)- Bfr). within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe200 b:2.0 occ:0.04 FE D:HEM200 0.0 2.0 0.0 NC D:HEM200 2.1 2.0 0.0 NA D:HEM200 2.1 2.0 0.0 NB D:HEM200 2.1 2.0 0.0 ND D:HEM200 2.1 2.0 0.0 SD C:MET52 2.2 15.7 1.0 SD D:MET52 2.3 15.7 1.0 C4C D:HEM200 3.1 2.0 0.0 C1A D:HEM200 3.1 2.0 0.0 C4A D:HEM200 3.1 2.0 0.0 C1C D:HEM200 3.1 2.0 0.0 C1D D:HEM200 3.1 2.0 0.0 C4D D:HEM200 3.1 2.0 0.0 CE C:MET52 3.1 13.0 1.0 C1B D:HEM200 3.1 2.0 0.0 C4B D:HEM200 3.1 2.0 0.0 CE D:MET52 3.3 13.0 1.0 CHD D:HEM200 3.4 2.0 0.0 CHA D:HEM200 3.5 2.0 0.0 CHB D:HEM200 3.5 2.0 0.0 CHC D:HEM200 3.5 2.0 0.0 CG D:MET52 3.6 12.5 1.0 CG C:MET52 3.6 12.6 1.0 C3C D:HEM200 4.3 2.0 0.0 C2A D:HEM200 4.3 2.0 0.0 C3A D:HEM200 4.3 2.0 0.0 C2C D:HEM200 4.3 2.0 0.0 C2B D:HEM200 4.3 2.0 0.0 C3B D:HEM200 4.3 2.0 0.0 C2D D:HEM200 4.3 2.0 0.0 C3D D:HEM200 4.4 2.0 0.0 CB D:MET52 4.4 11.2 1.0 CB C:MET52 4.5 11.2 1.0

A.Crow, T.L.Lawson, A.Lewin, G.R.Moore, N.E.Le Brun. Structural Basis For Iron Mineralization By Bacterioferritin J.Am.Chem.Soc. V. 131 6808 2009.
ISSN: ISSN 0002-7863
PubMed: 19391621
DOI: 10.1021/JA8093444