Iron in PDB 4n7n: Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.

The structure of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution., PDB code: 4n7n was solved by K.Sugiyama, N.Shibayama, S.Y.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.75
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	227.619, 56.061, 141.555, 90.00, 102.49, 90.00
R / Rfree (%)	25.1 / 28.6

Pages:

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

Binding sites:

The binding sites of Iron atom in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. (pdb code 4n7n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 12 binding sites of Iron where determined in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution., PDB code: 4n7n:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:81.6 occ:1.00 FE A:HEM201 0.0 81.6 1.0 NC A:HEM201 2.0 82.3 1.0 NA A:HEM201 2.0 87.7 1.0 NB A:HEM201 2.1 83.3 1.0 ND A:HEM201 2.1 85.8 1.0 NE2 A:HIS87 2.3 77.0 1.0 C4C A:HEM201 3.0 82.1 1.0 C1B A:HEM201 3.1 83.2 1.0 C1D A:HEM201 3.1 86.4 1.0 C4A A:HEM201 3.1 88.7 1.0 C1A A:HEM201 3.1 89.8 1.0 C1C A:HEM201 3.1 79.7 1.0 C4D A:HEM201 3.1 87.5 1.0 C4B A:HEM201 3.1 80.6 1.0 CE1 A:HIS87 3.2 76.8 1.0 CD2 A:HIS87 3.3 77.4 1.0 CHD A:HEM201 3.4 84.1 1.0 CHB A:HEM201 3.4 86.5 1.0 CHA A:HEM201 3.4 89.0 1.0 CHC A:HEM201 3.5 80.0 1.0 NE2 A:HIS58 4.1 0.7 1.0 C3C A:HEM201 4.3 79.8 1.0 C2A A:HEM201 4.3 91.0 1.0 C3A A:HEM201 4.3 90.2 1.0 C2C A:HEM201 4.3 80.0 1.0 C2D A:HEM201 4.3 87.4 1.0 ND1 A:HIS87 4.3 76.0 1.0 C2B A:HEM201 4.3 80.8 1.0 C3D A:HEM201 4.3 88.2 1.0 C3B A:HEM201 4.4 79.8 1.0 CG A:HIS87 4.4 76.7 1.0 CE1 A:HIS58 4.5 0.5 1.0 CG2 A:VAL62 4.8 96.3 1.0

Iron binding site 2 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe201 b:55.2 occ:1.00 FE B:HEM201 0.0 55.2 1.0 NC B:HEM201 2.0 54.3 1.0 NA B:HEM201 2.1 57.6 1.0 NB B:HEM201 2.1 53.3 1.0 ND B:HEM201 2.1 55.7 1.0 NE2 B:HIS92 2.2 34.6 1.0 C4C B:HEM201 3.0 54.5 1.0 CD2 B:HIS92 3.1 40.4 1.0 C1C B:HEM201 3.1 52.7 1.0 C1D B:HEM201 3.1 53.7 1.0 C1A B:HEM201 3.1 58.6 1.0 C4A B:HEM201 3.1 57.5 1.0 C1B B:HEM201 3.1 53.0 1.0 C4D B:HEM201 3.1 56.4 1.0 C4B B:HEM201 3.1 50.7 1.0 CE1 B:HIS92 3.3 41.3 1.0 CHD B:HEM201 3.4 54.8 1.0 CHB B:HEM201 3.4 55.7 1.0 CHA B:HEM201 3.5 56.3 1.0 CHC B:HEM201 3.5 51.8 1.0 NE2 B:HIS63 3.9 73.6 1.0 C3C B:HEM201 4.3 52.7 1.0 CG B:HIS92 4.3 42.0 1.0 C2C B:HEM201 4.3 52.4 1.0 C2A B:HEM201 4.3 60.3 1.0 C3A B:HEM201 4.3 59.0 1.0 C2D B:HEM201 4.3 55.8 1.0 C2B B:HEM201 4.4 52.7 1.0 ND1 B:HIS92 4.4 40.2 1.0 C3B B:HEM201 4.4 52.6 1.0 C3D B:HEM201 4.4 58.0 1.0 CE1 B:HIS63 4.4 73.0 1.0 CG2 B:VAL67 4.5 56.3 1.0

Iron binding site 3 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe201 b:82.9 occ:1.00 FE C:HEM201 0.0 82.9 1.0 NC C:HEM201 2.0 83.0 1.0 NB C:HEM201 2.1 83.5 1.0 NA C:HEM201 2.1 87.7 1.0 NE2 C:HIS87 2.1 68.8 1.0 ND C:HEM201 2.1 83.8 1.0 C4C C:HEM201 3.0 81.0 1.0 CE1 C:HIS87 3.0 70.1 1.0 C1B C:HEM201 3.1 85.3 1.0 C1C C:HEM201 3.1 81.5 1.0 C1D C:HEM201 3.1 83.2 1.0 CD2 C:HIS87 3.1 70.3 1.0 C4B C:HEM201 3.1 83.0 1.0 C4A C:HEM201 3.1 87.1 1.0 C1A C:HEM201 3.1 88.1 1.0 C4D C:HEM201 3.1 86.0 1.0 CHD C:HEM201 3.4 82.3 1.0 CHB C:HEM201 3.4 86.2 1.0 CHC C:HEM201 3.5 82.7 1.0 CHA C:HEM201 3.5 86.8 1.0 ND1 C:HIS87 4.2 70.2 1.0 NE2 C:HIS58 4.2 88.5 1.0 CG C:HIS87 4.2 71.7 1.0 C3C C:HEM201 4.3 79.1 1.0 C2C C:HEM201 4.3 80.0 1.0 C2B C:HEM201 4.3 85.2 1.0 C3B C:HEM201 4.3 83.5 1.0 C2D C:HEM201 4.3 83.7 1.0 C3A C:HEM201 4.4 88.7 1.0 C2A C:HEM201 4.4 90.0 1.0 C3D C:HEM201 4.4 85.4 1.0 CE1 C:HIS58 4.4 88.9 1.0 CG2 C:VAL62 4.9 91.6 1.0

Iron binding site 4 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe201 b:96.4 occ:1.00 FE D:HEM201 0.0 96.4 1.0 NC D:HEM201 2.0 96.6 1.0 NB D:HEM201 2.0 97.0 1.0 NA D:HEM201 2.0 0.9 1.0 ND D:HEM201 2.1 99.5 1.0 NE2 D:HIS92 2.4 85.6 1.0 C1B D:HEM201 3.0 97.5 1.0 C4C D:HEM201 3.1 95.5 1.0 C4A D:HEM201 3.1 0.2 1.0 C1A D:HEM201 3.1 0.6 1.0 C1C D:HEM201 3.1 95.2 1.0 C4B D:HEM201 3.1 96.0 1.0 C1D D:HEM201 3.1 98.9 1.0 C4D D:HEM201 3.1 0.3 1.0 CD2 D:HIS92 3.2 87.0 1.0 CHB D:HEM201 3.4 99.7 1.0 CHD D:HEM201 3.4 97.7 1.0 CHA D:HEM201 3.4 0.3 1.0 CHC D:HEM201 3.5 95.7 1.0 CE1 D:HIS92 3.5 86.1 1.0 NE2 D:HIS63 4.2 0.5 1.0 C2B D:HEM201 4.3 97.3 1.0 C3C D:HEM201 4.3 95.0 1.0 C3A D:HEM201 4.3 0.3 1.0 CG2 D:VAL67 4.3 0.1 1.0 C2C D:HEM201 4.3 95.1 1.0 C2A D:HEM201 4.3 0.5 1.0 C3B D:HEM201 4.3 96.4 1.0 C2D D:HEM201 4.4 99.7 1.0 C3D D:HEM201 4.4 0.4 1.0 CG D:HIS92 4.4 86.7 1.0 ND1 D:HIS92 4.6 85.9 1.0

Iron binding site 5 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe201 b:84.9 occ:1.00 FE E:HEM201 0.0 84.9 1.0 NC E:HEM201 2.0 87.9 1.0 NA E:HEM201 2.1 90.7 1.0 NB E:HEM201 2.1 89.4 1.0 ND E:HEM201 2.1 89.3 1.0 NE2 E:HIS87 2.1 69.5 1.0 CE1 E:HIS87 2.8 70.3 1.0 C4C E:HEM201 3.0 87.2 1.0 C1B E:HEM201 3.1 88.6 1.0 C4A E:HEM201 3.1 91.5 1.0 C1C E:HEM201 3.1 87.7 1.0 C1D E:HEM201 3.1 88.9 1.0 C1A E:HEM201 3.1 90.9 1.0 C4B E:HEM201 3.1 88.9 1.0 C4D E:HEM201 3.1 88.7 1.0 CD2 E:HIS87 3.4 70.8 1.0 CHD E:HEM201 3.4 88.6 1.0 CHB E:HEM201 3.4 90.6 1.0 CHA E:HEM201 3.5 88.8 1.0 CHC E:HEM201 3.5 89.3 1.0 ND1 E:HIS87 4.1 71.9 1.0 NE2 E:HIS58 4.2 75.0 1.0 C3C E:HEM201 4.3 85.9 1.0 C2C E:HEM201 4.3 86.8 1.0 C3A E:HEM201 4.3 93.2 1.0 C2A E:HEM201 4.3 93.2 1.0 CG E:HIS87 4.3 70.6 1.0 C2B E:HEM201 4.3 87.3 1.0 C2D E:HEM201 4.4 90.2 1.0 C3B E:HEM201 4.4 88.2 1.0 C3D E:HEM201 4.4 88.9 1.0 CE1 E:HIS58 4.6 74.4 1.0

Iron binding site 6 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe201 b:53.6 occ:1.00 FE F:HEM201 0.0 53.6 1.0 NC F:HEM201 2.0 51.1 1.0 NA F:HEM201 2.0 56.0 1.0 NB F:HEM201 2.1 50.4 1.0 ND F:HEM201 2.1 57.1 1.0 NE2 F:HIS92 2.1 52.2 1.0 CE1 F:HIS92 2.9 49.6 1.0 C4C F:HEM201 3.0 52.1 1.0 C4A F:HEM201 3.0 57.0 1.0 C1B F:HEM201 3.1 49.4 1.0 C1C F:HEM201 3.1 50.7 1.0 C1A F:HEM201 3.1 58.0 1.0 C1D F:HEM201 3.1 58.0 1.0 C4D F:HEM201 3.1 60.1 1.0 C4B F:HEM201 3.1 48.7 1.0 CD2 F:HIS92 3.3 51.8 1.0 CHD F:HEM201 3.4 55.5 1.0 CHB F:HEM201 3.4 53.5 1.0 CHA F:HEM201 3.4 59.6 1.0 CHC F:HEM201 3.5 49.9 1.0 ND1 F:HIS92 4.1 50.2 1.0 NE2 F:HIS63 4.1 59.2 1.0 C3C F:HEM201 4.3 50.2 1.0 C2C F:HEM201 4.3 50.0 1.0 C3A F:HEM201 4.3 58.1 1.0 C2A F:HEM201 4.3 58.5 1.0 C2B F:HEM201 4.3 48.8 1.0 CG F:HIS92 4.3 51.4 1.0 C2D F:HEM201 4.3 61.2 1.0 C3D F:HEM201 4.4 63.7 1.0 C3B F:HEM201 4.4 47.8 1.0 CE1 F:HIS63 4.8 58.8 1.0 CG2 F:VAL67 4.8 55.5 1.0

Iron binding site 7 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ G:Fe201 b:67.6 occ:1.00 FE G:HEM201 0.0 67.6 1.0 NC G:HEM201 2.0 71.7 1.0 NB G:HEM201 2.1 71.7 1.0 NA G:HEM201 2.1 74.0 1.0 ND G:HEM201 2.1 70.9 1.0 NE2 G:HIS87 2.2 68.8 1.0 C4C G:HEM201 3.0 70.6 1.0 C1B G:HEM201 3.0 74.1 1.0 C4A G:HEM201 3.1 74.4 1.0 C1D G:HEM201 3.1 70.5 1.0 C1C G:HEM201 3.1 70.6 1.0 C1A G:HEM201 3.1 73.0 1.0 C4D G:HEM201 3.1 71.9 1.0 C4B G:HEM201 3.1 72.2 1.0 CE1 G:HIS87 3.1 71.7 1.0 CD2 G:HIS87 3.2 71.4 1.0 CHB G:HEM201 3.4 74.4 1.0 CHD G:HEM201 3.4 72.1 1.0 CHA G:HEM201 3.5 71.8 1.0 CHC G:HEM201 3.5 71.4 1.0 NE2 G:HIS58 4.2 71.4 1.0 ND1 G:HIS87 4.3 73.1 1.0 C3C G:HEM201 4.3 69.4 1.0 C2C G:HEM201 4.3 70.0 1.0 C2B G:HEM201 4.3 74.5 1.0 C3A G:HEM201 4.3 74.8 1.0 C2D G:HEM201 4.3 69.5 1.0 C2A G:HEM201 4.3 74.8 1.0 CG G:HIS87 4.3 71.1 1.0 C3D G:HEM201 4.3 72.4 1.0 C3B G:HEM201 4.3 72.7 1.0 CE1 G:HIS58 4.4 71.2 1.0 CG2 G:VAL62 4.6 70.9 1.0

Iron binding site 8 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ H:Fe201 b:83.3 occ:1.00 FE H:HEM201 0.0 83.3 1.0 NC H:HEM201 2.0 87.1 1.0 NB H:HEM201 2.1 87.2 1.0 NA H:HEM201 2.1 91.0 1.0 NE2 H:HIS92 2.1 76.7 1.0 ND H:HEM201 2.1 90.4 1.0 CE1 H:HIS92 3.0 78.7 1.0 C4C H:HEM201 3.0 86.6 1.0 C1B H:HEM201 3.0 87.2 1.0 CD2 H:HIS92 3.1 79.3 1.0 C1C H:HEM201 3.1 85.9 1.0 C4A H:HEM201 3.1 90.2 1.0 C1D H:HEM201 3.1 89.3 1.0 C4B H:HEM201 3.1 85.8 1.0 C1A H:HEM201 3.1 93.1 1.0 C4D H:HEM201 3.2 92.4 1.0 CHB H:HEM201 3.4 89.3 1.0 CHD H:HEM201 3.4 88.3 1.0 CHC H:HEM201 3.5 86.5 1.0 CHA H:HEM201 3.5 93.2 1.0 ND1 H:HIS92 4.1 79.2 1.0 CG H:HIS92 4.2 80.7 1.0 C3C H:HEM201 4.3 86.5 1.0 C2C H:HEM201 4.3 86.3 1.0 C2B H:HEM201 4.3 86.7 1.0 NE2 H:HIS63 4.3 78.9 1.0 C3B H:HEM201 4.3 86.0 1.0 C3A H:HEM201 4.3 91.9 1.0 C2D H:HEM201 4.4 91.7 1.0 C2A H:HEM201 4.4 94.3 1.0 C3D H:HEM201 4.4 93.8 1.0 CE1 H:HIS63 4.7 76.5 1.0 CG2 H:VAL67 4.8 82.2 1.0

Iron binding site 9 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ I:Fe201 b:0.7 occ:1.00 FE I:HEM201 0.0 0.7 1.0 NC I:HEM201 2.1 0.1 1.0 NA I:HEM201 2.1 0.8 1.0 NB I:HEM201 2.1 0.9 1.0 ND I:HEM201 2.1 0.3 1.0 NE2 I:HIS87 2.3 93.8 1.0 CD2 I:HIS87 3.0 96.5 1.0 C1B I:HEM201 3.1 0.0 1.0 C4C I:HEM201 3.1 0.7 1.0 C4A I:HEM201 3.1 0.8 1.0 C1D I:HEM201 3.1 0.2 1.0 C1C I:HEM201 3.1 0.8 1.0 C1A I:HEM201 3.1 0.7 1.0 C4D I:HEM201 3.1 0.4 1.0 C4B I:HEM201 3.1 0.2 1.0 CE1 I:HIS87 3.4 96.2 1.0 CHB I:HEM201 3.4 0.1 1.0 CHD I:HEM201 3.4 0.7 1.0 CHA I:HEM201 3.5 0.0 1.0 CHC I:HEM201 3.5 0.3 1.0 CE1 I:HIS58 4.0 1.0 1.0 NE2 I:HIS58 4.1 0.5 1.0 CG I:HIS87 4.2 97.9 1.0 C3C I:HEM201 4.3 0.0 1.0 C3A I:HEM201 4.3 0.1 1.0 C2C I:HEM201 4.3 0.7 1.0 C2B I:HEM201 4.3 0.9 1.0 C2A I:HEM201 4.4 0.1 1.0 C2D I:HEM201 4.4 0.6 1.0 C3B I:HEM201 4.4 0.8 1.0 C3D I:HEM201 4.4 1.0 1.0 ND1 I:HIS87 4.4 97.0 1.0 CG2 I:VAL62 4.5 0.8 1.0

Iron binding site 10 out of 12 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Full-Liganded Human Haemoglobin with Phosphate at 2.75 A Resolution. within 5.0Å range: probe atom residue distance (Å) B Occ J:Fe201 b:0.8 occ:1.00 FE J:HEM201 0.0 0.8 1.0 NC J:HEM201 2.0 1.0 1.0 NA J:HEM201 2.1 0.8 1.0 NB J:HEM201 2.1 0.6 1.0 ND J:HEM201 2.1 0.3 1.0 NE2 J:HIS92 2.3 0.8 1.0 CE1 J:HIS92 3.0 0.5 1.0 C4C J:HEM201 3.0 1.0 1.0 C1B J:HEM201 3.1 0.4 1.0 C4A J:HEM201 3.1 0.1 1.0 C1C J:HEM201 3.1 0.9 1.0 C1A J:HEM201 3.1 0.5 1.0 C4B J:HEM201 3.1 0.4 1.0 C1D J:HEM201 3.1 0.2 1.0 C4D J:HEM201 3.1 0.5 1.0 CHB J:HEM201 3.4 0.2 1.0 CD2 J:HIS92 3.4 0.7 1.0 CHD J:HEM201 3.4 0.9 1.0 CHA J:HEM201 3.5 0.7 1.0 CHC J:HEM201 3.5 0.3 1.0 NE2 J:HIS63 4.2 0.7 1.0 ND1 J:HIS92 4.2 0.0 1.0 CG2 J:VAL67 4.3 0.4 1.0 C3C J:HEM201 4.3 0.2 1.0 C2C J:HEM201 4.3 0.8 1.0 C3A J:HEM201 4.3 0.9 1.0 C2B J:HEM201 4.3 0.9 1.0 C2A J:HEM201 4.3 0.0 1.0 C3B J:HEM201 4.3 0.1 1.0 C2D J:HEM201 4.4 0.4 1.0 C3D J:HEM201 4.4 0.5 1.0 CG J:HIS92 4.4 0.9 1.0 CE1 J:HIS63 4.5 0.6 1.0

N.Shibayama, K.Sugiyama, J.R.Tame, S.Y.Park. Capturing the Hemoglobin Allosteric Transition in A Single Crystal Form J.Am.Chem.Soc. V. 136 5097 2014.
ISSN: ISSN 0002-7863
PubMed: 24635037
DOI: 10.1021/JA500380E