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:
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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