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Nickel in PDB 4n7p: Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.

Protein crystallography data

The structure of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution., PDB code: 4n7p 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 / 2.81
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 228.331, 55.531, 139.681, 90.00, 103.08, 90.00
R / Rfree (%) 25.9 / 28.7

Other elements in 4n7p:

The structure of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. also contains other interesting chemical elements:

Iron (Fe) 6 atoms

Nickel Binding Sites:

The binding sites of Nickel atom in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. (pdb code 4n7p). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total 6 binding sites of Nickel where determined in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution., PDB code: 4n7p:
Jump to Nickel binding site number: 1; 2; 3; 4; 5; 6;

Nickel binding site 1 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 1 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ni201

b:81.2
occ:1.00
NI A:HNI201 0.0 81.2 1.0
NC A:HNI201 2.0 81.7 1.0
NA A:HNI201 2.0 82.8 1.0
NB A:HNI201 2.1 80.2 1.0
ND A:HNI201 2.1 83.0 1.0
NE2 A:HIS87 2.3 98.8 1.0
CE1 A:HIS87 3.0 99.0 1.0
C4C A:HNI201 3.0 81.7 1.0
C1B A:HNI201 3.1 81.2 1.0
C4A A:HNI201 3.1 83.1 1.0
C1D A:HNI201 3.1 84.3 1.0
C1A A:HNI201 3.1 83.4 1.0
C1C A:HNI201 3.1 81.4 1.0
C4D A:HNI201 3.1 84.6 1.0
C4B A:HNI201 3.1 79.9 1.0
CHB A:HNI201 3.4 83.2 1.0
CHD A:HNI201 3.4 82.8 1.0
CD2 A:HIS87 3.4 98.9 1.0
CHA A:HNI201 3.5 83.4 1.0
CHC A:HNI201 3.5 81.2 1.0
ND1 A:HIS87 4.1 97.9 1.0
C3A A:HNI201 4.3 82.9 1.0
C2A A:HNI201 4.3 83.1 1.0
C3C A:HNI201 4.3 82.1 1.0
C2B A:HNI201 4.3 79.7 1.0
C2D A:HNI201 4.3 85.5 1.0
C2C A:HNI201 4.3 82.0 1.0
C3B A:HNI201 4.3 78.8 1.0
C3D A:HNI201 4.4 87.3 1.0
CG A:HIS87 4.4 98.8 1.0
CE1 A:HIS58 4.8 96.7 1.0
NE2 A:HIS58 4.9 96.2 1.0
CG2 A:VAL62 4.9 89.6 1.0

Nickel binding site 2 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 2 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 2 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ni201

b:0.5
occ:1.00
NI D:HNI201 0.0 0.5 1.0
NC D:HNI201 2.0 99.8 1.0
NA D:HNI201 2.1 0.6 1.0
NB D:HNI201 2.1 99.7 1.0
ND D:HNI201 2.1 0.6 1.0
NE2 D:HIS92 2.3 0.1 1.0
C4C D:HNI201 3.0 0.1 1.0
C1B D:HNI201 3.1 0.1 1.0
CE1 D:HIS92 3.1 0.7 1.0
C4A D:HNI201 3.1 0.3 1.0
C1C D:HNI201 3.1 98.9 1.0
C1D D:HNI201 3.1 0.3 1.0
C1A D:HNI201 3.1 0.6 1.0
C4B D:HNI201 3.1 98.6 1.0
C4D D:HNI201 3.1 0.8 1.0
CD2 D:HIS92 3.4 1.0 1.0
CHD D:HNI201 3.4 0.8 1.0
CHB D:HNI201 3.4 0.7 1.0
CHA D:HNI201 3.5 0.8 1.0
CHC D:HNI201 3.5 98.8 1.0
CG2 D:VAL67 4.1 99.1 1.0
ND1 D:HIS92 4.2 0.3 1.0
C3C D:HNI201 4.3 98.9 1.0
C2C D:HNI201 4.3 98.8 1.0
C3A D:HNI201 4.3 0.6 1.0
C2B D:HNI201 4.3 98.3 1.0
C2A D:HNI201 4.3 0.9 1.0
CG D:HIS92 4.4 0.2 1.0
C2D D:HNI201 4.4 0.4 1.0
C3B D:HNI201 4.4 98.8 1.0
C3D D:HNI201 4.4 0.9 1.0
NE2 D:HIS63 4.9 0.0 1.0

Nickel binding site 3 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 3 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 3 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Ni201

b:95.8
occ:1.00
NI E:HNI201 0.0 95.8 1.0
NA E:HNI201 2.0 97.4 1.0
NC E:HNI201 2.1 95.2 1.0
NB E:HNI201 2.1 94.9 1.0
ND E:HNI201 2.1 96.8 1.0
NE2 E:HIS87 2.4 0.6 1.0
C4C E:HNI201 3.1 94.3 1.0
C1B E:HNI201 3.1 94.9 1.0
C4A E:HNI201 3.1 97.7 1.0
C1A E:HNI201 3.1 99.6 1.0
C1D E:HNI201 3.1 96.4 1.0
C1C E:HNI201 3.1 94.5 1.0
C4D E:HNI201 3.1 96.9 1.0
C4B E:HNI201 3.1 93.8 1.0
CD2 E:HIS87 3.3 0.2 1.0
CHB E:HNI201 3.4 96.7 1.0
CHD E:HNI201 3.4 96.2 1.0
CE1 E:HIS87 3.4 0.5 1.0
CHA E:HNI201 3.5 98.0 1.0
CHC E:HNI201 3.5 94.1 1.0
NE2 E:HIS58 4.2 95.5 1.0
CG2 E:VAL62 4.2 90.5 1.0
C3C E:HNI201 4.3 93.1 1.0
C3A E:HNI201 4.3 99.2 1.0
C2A E:HNI201 4.3 1.0 1.0
C2B E:HNI201 4.3 94.0 1.0
C2C E:HNI201 4.3 94.0 1.0
C2D E:HNI201 4.3 95.6 1.0
C3B E:HNI201 4.4 93.7 1.0
C3D E:HNI201 4.4 95.9 1.0
CG E:HIS87 4.5 0.9 1.0
ND1 E:HIS87 4.5 0.7 1.0
CE1 E:HIS58 5.0 95.3 1.0

Nickel binding site 4 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 4 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 4 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Ni201

b:95.1
occ:1.00
NI H:HNI201 0.0 95.1 1.0
NC H:HNI201 2.0 95.7 1.0
NA H:HNI201 2.1 98.2 1.0
NB H:HNI201 2.1 94.7 1.0
ND H:HNI201 2.1 97.9 1.0
NE2 H:HIS92 2.1 81.7 1.0
CD2 H:HIS92 3.0 82.4 1.0
C4C H:HNI201 3.1 95.3 1.0
C1B H:HNI201 3.1 94.3 1.0
C4A H:HNI201 3.1 97.6 1.0
C1A H:HNI201 3.1 100.0 1.0
C1C H:HNI201 3.1 93.5 1.0
C1D H:HNI201 3.1 98.8 1.0
C4B H:HNI201 3.1 92.3 1.0
C4D H:HNI201 3.1 99.7 1.0
CE1 H:HIS92 3.2 81.8 1.0
CHB H:HNI201 3.4 95.9 1.0
CHD H:HNI201 3.4 97.5 1.0
CHA H:HNI201 3.5 99.5 1.0
CHC H:HNI201 3.5 92.7 1.0
CG H:HIS92 4.2 82.7 1.0
ND1 H:HIS92 4.2 81.9 1.0
C3C H:HNI201 4.3 92.9 1.0
C2C H:HNI201 4.3 92.6 1.0
C2B H:HNI201 4.3 93.2 1.0
C3A H:HNI201 4.3 98.7 1.0
C2A H:HNI201 4.3 0.3 1.0
C3B H:HNI201 4.3 92.8 1.0
C2D H:HNI201 4.4 99.7 1.0
C3D H:HNI201 4.4 0.7 1.0
NE2 H:HIS63 4.4 99.4 1.0
CG2 H:VAL67 4.6 80.7 1.0

Nickel binding site 5 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 5 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 5 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
I:Ni201

b:0.1
occ:1.00
NI I:HNI201 0.0 0.1 1.0
NC I:HNI201 2.0 0.1 1.0
NA I:HNI201 2.1 0.3 1.0
NB I:HNI201 2.1 0.7 1.0
ND I:HNI201 2.1 0.8 1.0
NE2 I:HIS87 2.1 0.6 1.0
CD2 I:HIS87 3.0 0.6 1.0
C4C I:HNI201 3.0 0.8 1.0
C1B I:HNI201 3.1 0.2 1.0
C4A I:HNI201 3.1 0.1 1.0
C1D I:HNI201 3.1 0.7 1.0
C1A I:HNI201 3.1 0.9 1.0
C1C I:HNI201 3.1 0.4 1.0
C4D I:HNI201 3.1 0.2 1.0
C4B I:HNI201 3.1 0.2 1.0
CE1 I:HIS87 3.2 1.0 1.0
CHB I:HNI201 3.4 0.3 1.0
CHD I:HNI201 3.4 0.3 1.0
CHA I:HNI201 3.5 0.3 1.0
CHC I:HNI201 3.5 0.9 1.0
CE1 I:HIS58 4.2 0.8 1.0
CG I:HIS87 4.2 0.9 1.0
ND1 I:HIS87 4.2 0.8 1.0
C3C I:HNI201 4.3 0.2 1.0
C2B I:HNI201 4.3 0.6 1.0
NE2 I:HIS58 4.3 0.0 1.0
C3A I:HNI201 4.3 1.0 1.0
C2A I:HNI201 4.3 0.9 1.0
C2C I:HNI201 4.3 0.9 1.0
C2D I:HNI201 4.4 0.4 1.0
C3B I:HNI201 4.4 0.7 1.0
C3D I:HNI201 4.4 0.3 1.0
CG2 I:VAL62 4.7 94.9 1.0

Nickel binding site 6 out of 6 in 4n7p

Go back to Nickel Binding Sites List in 4n7p
Nickel binding site 6 out of 6 in the Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution.


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 6 of Capturing the Haemoglobin Allosteric Transition in A Single Crystal Form; Crystal Structure of Half-Liganded Human Haemoglobin Without Phosphate at 2.8 A Resolution. within 5.0Å range:
probe atom residue distance (Å) B Occ
L:Ni201

b:0.2
occ:1.00
NI L:HNI201 0.0 0.2 1.0
NC L:HNI201 2.0 0.9 1.0
NA L:HNI201 2.1 0.2 1.0
NB L:HNI201 2.1 0.2 1.0
ND L:HNI201 2.1 0.0 1.0
NE2 L:HIS92 2.4 0.4 1.0
C4C L:HNI201 3.1 0.5 1.0
C1B L:HNI201 3.1 0.4 1.0
C4A L:HNI201 3.1 0.5 1.0
C1D L:HNI201 3.1 0.3 1.0
CE1 L:HIS92 3.1 0.4 1.0
C1A L:HNI201 3.1 0.9 1.0
C1C L:HNI201 3.1 0.0 1.0
C4D L:HNI201 3.1 0.4 1.0
C4B L:HNI201 3.1 0.9 1.0
CHD L:HNI201 3.4 0.8 1.0
CHB L:HNI201 3.4 0.6 1.0
CHA L:HNI201 3.5 0.8 1.0
CHC L:HNI201 3.5 0.7 1.0
CD2 L:HIS92 3.6 1.0 1.0
NE2 L:HIS63 4.2 0.0 1.0
C3C L:HNI201 4.3 0.4 1.0
C2B L:HNI201 4.3 0.3 1.0
C2C L:HNI201 4.3 0.5 1.0
ND1 L:HIS92 4.3 0.6 1.0
C3A L:HNI201 4.3 0.9 1.0
C2A L:HNI201 4.3 0.1 1.0
C2D L:HNI201 4.4 0.6 1.0
C3B L:HNI201 4.4 0.2 1.0
C3D L:HNI201 4.4 0.5 1.0
CG2 L:VAL67 4.4 99.3 1.0
CG L:HIS92 4.6 0.4 1.0
CD2 L:HIS63 4.8 1.0 1.0

Reference:

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
Page generated: Wed Oct 9 18:33:47 2024

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