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Nickel in PDB 5x2s: Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.

Protein crystallography data

The structure of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5., PDB code: 5x2s was solved by M.Ohki, S.-Y.Park, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.99 / 2.39
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 228.603, 54.598, 138.444, 90.00, 103.18, 90.00
R / Rfree (%) 24.5 / 28.8

Other elements in 5x2s:

The structure of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. also contains other interesting chemical elements:

Iron (Fe) 6 atoms
Chlorine (Cl) 1 atom

Nickel Binding Sites:

The binding sites of Nickel atom in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. (pdb code 5x2s). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 6 binding sites of Nickel where determined in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5., PDB code: 5x2s:
Jump to Nickel binding site number: 1; 2; 3; 4; 5; 6;

Nickel binding site 1 out of 6 in 5x2s

Go back to Nickel Binding Sites List in 5x2s
Nickel binding site 1 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni201

b:70.3
occ:1.00
NI A:HNI201 0.0 70.3 1.0
NB A:HNI201 2.0 69.2 1.0
ND A:HNI201 2.0 71.4 1.0
NA A:HNI201 2.0 70.5 1.0
NC A:HNI201 2.0 70.3 1.0
NE2 A:HIS87 2.3 0.8 1.0
C4B A:HNI201 2.9 69.1 1.0
C4D A:HNI201 3.0 72.2 1.0
C1B A:HNI201 3.0 69.5 1.0
C1D A:HNI201 3.0 72.4 1.0
C1C A:HNI201 3.0 69.7 1.0
C4A A:HNI201 3.0 70.3 1.0
C1A A:HNI201 3.0 71.2 1.0
C4C A:HNI201 3.0 71.3 1.0
CE1 A:HIS87 3.2 0.3 1.0
CD2 A:HIS87 3.2 0.7 1.0
CHC A:HNI201 3.3 69.8 1.0
CHA A:HNI201 3.4 72.3 1.0
CHB A:HNI201 3.4 70.2 1.0
CHD A:HNI201 3.4 72.8 1.0
C3B A:HNI201 4.2 69.2 1.0
C2B A:HNI201 4.2 69.2 1.0
ND1 A:HIS87 4.2 0.5 1.0
C2C A:HNI201 4.2 70.7 1.0
C3A A:HNI201 4.2 71.2 1.0
CG A:HIS87 4.2 0.3 1.0
C3C A:HNI201 4.3 71.6 1.0
C3D A:HNI201 4.3 73.7 1.0
C2A A:HNI201 4.3 71.7 1.0
C2D A:HNI201 4.3 73.8 1.0
CG2 A:VAL62 4.6 67.1 1.0
NE2 A:HIS58 4.7 79.8 1.0

Nickel binding site 2 out of 6 in 5x2s

Go back to Nickel Binding Sites List in 5x2s
Nickel binding site 2 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni201

b:76.6
occ:1.00
NI D:HNI201 0.0 76.6 1.0
NC D:HNI201 2.0 75.8 1.0
NA D:HNI201 2.0 77.4 1.0
ND D:HNI201 2.0 78.3 1.0
NB D:HNI201 2.0 75.2 1.0
NE2 D:HIS92 2.2 98.7 1.0
C1C D:HNI201 3.0 74.8 1.0
C4D D:HNI201 3.0 79.8 1.0
C1D D:HNI201 3.0 79.0 1.0
C4B D:HNI201 3.0 74.8 1.0
C1A D:HNI201 3.0 78.7 1.0
C1B D:HNI201 3.0 75.5 1.0
C4C D:HNI201 3.0 76.6 1.0
C4A D:HNI201 3.0 77.0 1.0
CE1 D:HIS92 3.2 98.8 1.0
CD2 D:HIS92 3.2 99.4 1.0
CHC D:HNI201 3.3 75.0 1.0
CHA D:HNI201 3.4 80.2 1.0
CHD D:HNI201 3.4 78.6 1.0
CHB D:HNI201 3.4 76.5 1.0
C2A D:HNI201 4.2 79.3 1.0
C2C D:HNI201 4.2 75.2 1.0
C3A D:HNI201 4.2 78.2 1.0
C3C D:HNI201 4.2 76.1 1.0
C2D D:HNI201 4.2 81.1 1.0
C3D D:HNI201 4.2 81.7 1.0
C2B D:HNI201 4.3 75.1 1.0
C3B D:HNI201 4.3 74.9 1.0
CG D:HIS92 4.3 98.9 1.0
ND1 D:HIS92 4.3 0.3 1.0
CG2 D:VAL67 4.5 82.2 1.0
NE2 D:HIS63 4.8 86.7 1.0

Nickel binding site 3 out of 6 in 5x2s

Go back to Nickel Binding Sites List in 5x2s
Nickel binding site 3 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ni201

b:69.2
occ:1.00
NI E:HNI201 0.0 69.2 1.0
NB E:HNI201 2.0 67.9 1.0
NC E:HNI201 2.0 69.1 1.0
ND E:HNI201 2.0 70.8 1.0
NA E:HNI201 2.0 69.6 1.0
CE1 E:HIS87 2.5 85.1 1.0
C4B E:HNI201 2.9 67.7 1.0
C1C E:HNI201 3.0 68.3 1.0
C4D E:HNI201 3.0 71.9 1.0
C1D E:HNI201 3.0 71.9 1.0
C1B E:HNI201 3.0 68.0 1.0
C1A E:HNI201 3.0 70.6 1.0
C4C E:HNI201 3.0 70.1 1.0
C4A E:HNI201 3.0 69.0 1.0
CHC E:HNI201 3.3 68.3 1.0
NE2 E:HIS87 3.3 85.3 1.0
CHA E:HNI201 3.3 72.1 1.0
CHB E:HNI201 3.4 68.8 1.0
CHD E:HNI201 3.4 72.0 1.0
ND1 E:HIS87 3.5 86.7 1.0
C2C E:HNI201 4.2 69.1 1.0
C3B E:HNI201 4.2 67.7 1.0
C2A E:HNI201 4.2 71.0 1.0
C3C E:HNI201 4.2 70.1 1.0
C2B E:HNI201 4.2 67.6 1.0
C3D E:HNI201 4.3 73.9 1.0
C2D E:HNI201 4.3 73.9 1.0
C3A E:HNI201 4.3 70.0 1.0
NE2 E:HIS58 4.3 77.7 1.0
CD2 E:HIS87 4.5 86.5 1.0
CG E:HIS87 4.6 85.7 1.0
CD1 E:LEU91 4.9 87.5 1.0
CG2 E:VAL62 4.9 61.6 1.0
CE1 E:HIS58 4.9 78.1 1.0

Nickel binding site 4 out of 6 in 5x2s

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Nickel binding site 4 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 4 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Ni201

b:68.4
occ:1.00
NI H:HNI201 0.0 68.4 1.0
NA H:HNI201 2.0 69.3 1.0
NB H:HNI201 2.0 67.3 1.0
NC H:HNI201 2.0 67.9 1.0
ND H:HNI201 2.0 69.8 1.0
NE2 H:HIS92 2.0 61.1 1.0
C1B H:HNI201 2.9 67.8 1.0
C4A H:HNI201 3.0 69.1 1.0
CE1 H:HIS92 3.0 61.0 1.0
C1A H:HNI201 3.0 70.2 1.0
C1D H:HNI201 3.0 70.5 1.0
C4C H:HNI201 3.0 68.7 1.0
C4B H:HNI201 3.0 67.0 1.0
C4D H:HNI201 3.0 70.9 1.0
C1C H:HNI201 3.0 67.1 1.0
CD2 H:HIS92 3.1 61.8 1.0
CHB H:HNI201 3.3 68.9 1.0
CHA H:HNI201 3.4 71.3 1.0
CHD H:HNI201 3.4 70.4 1.0
CHC H:HNI201 3.4 67.3 1.0
ND1 H:HIS92 4.1 62.4 1.0
CG H:HIS92 4.2 61.0 1.0
C2A H:HNI201 4.2 71.0 1.0
C3A H:HNI201 4.2 70.4 1.0
C2B H:HNI201 4.2 67.5 1.0
C3C H:HNI201 4.3 68.7 1.0
C2C H:HNI201 4.3 67.8 1.0
C3B H:HNI201 4.3 67.2 1.0
C2D H:HNI201 4.3 72.1 1.0
C3D H:HNI201 4.3 72.4 1.0
NE2 H:HIS63 4.5 75.1 1.0
CG2 H:VAL67 4.6 71.5 1.0

Nickel binding site 5 out of 6 in 5x2s

Go back to Nickel Binding Sites List in 5x2s
Nickel binding site 5 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 5 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Ni201

b:76.4
occ:1.00
NI I:HNI201 0.0 76.4 1.0
ND I:HNI201 2.0 77.8 1.0
NA I:HNI201 2.0 77.0 1.0
NB I:HNI201 2.0 75.2 1.0
NC I:HNI201 2.0 76.2 1.0
CE1 I:HIS87 2.9 81.1 1.0
C4D I:HNI201 2.9 78.8 1.0
C1B I:HNI201 3.0 75.5 1.0
C1D I:HNI201 3.0 78.6 1.0
C4A I:HNI201 3.0 76.7 1.0
C4B I:HNI201 3.0 75.0 1.0
C1A I:HNI201 3.0 78.0 1.0
C4C I:HNI201 3.0 77.1 1.0
C1C I:HNI201 3.1 75.4 1.0
NE2 I:HIS87 3.2 81.4 1.0
CHB I:HNI201 3.3 76.4 1.0
CHA I:HNI201 3.3 79.2 1.0
CHD I:HNI201 3.4 78.8 1.0
CHC I:HNI201 3.4 75.5 1.0
ND1 I:HIS87 4.1 82.2 1.0
CG1 I:VAL62 4.2 74.5 1.0
C3A I:HNI201 4.2 77.9 1.0
C2A I:HNI201 4.2 78.6 1.0
C2B I:HNI201 4.2 75.1 1.0
C3D I:HNI201 4.2 80.3 1.0
C2D I:HNI201 4.2 80.1 1.0
C3B I:HNI201 4.2 75.0 1.0
CE1 I:HIS58 4.3 93.6 1.0
C3C I:HNI201 4.3 77.2 1.0
C2C I:HNI201 4.3 76.2 1.0
NE2 I:HIS58 4.5 94.6 1.0
CD2 I:HIS87 4.6 81.7 1.0
CD1 I:LEU91 5.0 86.3 1.0
CG I:HIS87 5.0 80.5 1.0

Nickel binding site 6 out of 6 in 5x2s

Go back to Nickel Binding Sites List in 5x2s
Nickel binding site 6 out of 6 in the Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 6 of Direct Observation of Conformational Population Shifts in Hemoglobin: Crystal Structure of Half-Liganded Hemoglobin After Adding 4 Mm Bezafibrate pH 6.5. within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ni201

b:84.0
occ:1.00
NI L:HNI201 0.0 84.0 1.0
NB L:HNI201 2.0 82.3 1.0
NC L:HNI201 2.0 83.6 1.0
ND L:HNI201 2.0 85.8 1.0
NA L:HNI201 2.0 84.6 1.0
CE1 L:HIS92 2.2 91.7 1.0
NE2 L:HIS92 2.7 92.1 1.0
C1D L:HNI201 3.0 86.9 1.0
C4B L:HNI201 3.0 81.8 1.0
C1B L:HNI201 3.0 82.6 1.0
C1C L:HNI201 3.0 82.5 1.0
C4D L:HNI201 3.0 87.1 1.0
C4C L:HNI201 3.0 84.8 1.0
C1A L:HNI201 3.1 85.9 1.0
C4A L:HNI201 3.1 84.1 1.0
ND1 L:HIS92 3.3 92.8 1.0
CHC L:HNI201 3.4 82.3 1.0
CHD L:HNI201 3.4 86.8 1.0
CHB L:HNI201 3.4 83.7 1.0
CHA L:HNI201 3.4 87.3 1.0
CD2 L:HIS92 4.0 93.0 1.0
CG2 L:VAL67 4.2 85.7 1.0
C2C L:HNI201 4.2 83.4 1.0
C2B L:HNI201 4.2 82.0 1.0
C2D L:HNI201 4.2 88.9 1.0
C3C L:HNI201 4.2 84.7 1.0
C3B L:HNI201 4.3 81.7 1.0
CG L:HIS92 4.3 91.5 1.0
C3D L:HNI201 4.3 89.1 1.0
C2A L:HNI201 4.3 86.5 1.0
C3A L:HNI201 4.3 85.5 1.0
CE1 L:HIS63 4.7 98.9 1.0
CE1 L:PHE103 4.9 80.8 1.0

Reference:

N.Shibayama, M.Ohki, J.R.H.Tame, S.Y.Park. Direct Observation of Conformational Population Shifts in Crystalline Human Hemoglobin. J. Biol. Chem. V. 292 18258 2017.
ISSN: ESSN 1083-351X
PubMed: 28931607
DOI: 10.1074/JBC.M117.781146
Page generated: Thu Oct 10 08:10:18 2024

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