Zinc in PDB 2xp0: C-Terminal Cysteine-Rich Domain of Human Chfr
Protein crystallography data
The structure of C-Terminal Cysteine-Rich Domain of Human Chfr, PDB code: 2xp0
was solved by
J.Oberoi,
R.Bayliss,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
39.715 /
1.98
|
Space group
|
C 1 2 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
163.010,
52.030,
82.520,
90.00,
105.73,
90.00
|
R / Rfree (%)
|
16.07 /
20.2
|
Zinc Binding Sites:
The binding sites of Zinc atom in the C-Terminal Cysteine-Rich Domain of Human Chfr
(pdb code 2xp0). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 10 binding sites of Zinc where determined in the
C-Terminal Cysteine-Rich Domain of Human Chfr, PDB code: 2xp0:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Zinc binding site 1 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 1 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn991
b:32.7
occ:1.00
|
NE2
|
A:HIS482
|
2.1
|
29.6
|
1.0
|
SG
|
A:CYS428
|
2.3
|
31.3
|
1.0
|
SG
|
A:CYS476
|
2.3
|
34.5
|
1.0
|
SG
|
A:CYS431
|
2.4
|
33.7
|
1.0
|
CD2
|
A:HIS482
|
3.0
|
28.9
|
1.0
|
CE1
|
A:HIS482
|
3.2
|
32.0
|
1.0
|
CB
|
A:CYS428
|
3.4
|
33.4
|
1.0
|
CB
|
A:CYS476
|
3.4
|
43.3
|
1.0
|
CB
|
A:CYS431
|
3.5
|
35.3
|
1.0
|
N
|
A:CYS431
|
3.5
|
37.0
|
1.0
|
CA
|
A:CYS431
|
3.7
|
37.0
|
1.0
|
N
|
A:CYS428
|
3.7
|
32.8
|
1.0
|
CA
|
A:CYS428
|
4.0
|
32.1
|
1.0
|
C
|
A:GLN430
|
4.1
|
37.7
|
1.0
|
CG
|
A:HIS482
|
4.2
|
29.0
|
1.0
|
ND1
|
A:HIS482
|
4.2
|
33.3
|
1.0
|
O
|
A:HOH2038
|
4.3
|
35.5
|
1.0
|
C
|
A:CYS428
|
4.4
|
29.0
|
1.0
|
O
|
A:CYS428
|
4.5
|
28.4
|
1.0
|
O
|
A:GLN430
|
4.6
|
35.7
|
1.0
|
N
|
A:GLN430
|
4.6
|
33.6
|
1.0
|
CA
|
A:GLN430
|
4.8
|
31.9
|
1.0
|
CA
|
A:CYS476
|
4.8
|
44.2
|
1.0
|
C
|
A:VAL427
|
4.9
|
35.8
|
1.0
|
CD
|
A:PRO493
|
4.9
|
32.0
|
1.0
|
|
Zinc binding site 2 out
of 10 in 2xp0
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Zinc Binding Sites List in 2xp0
Zinc binding site 2 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn992
b:21.8
occ:1.00
|
SG
|
A:CYS518
|
2.3
|
23.0
|
1.0
|
SG
|
A:CYS488
|
2.4
|
23.3
|
1.0
|
SG
|
A:CYS485
|
2.4
|
20.7
|
1.0
|
SG
|
A:CYS524
|
2.4
|
20.9
|
1.0
|
CB
|
A:CYS485
|
3.1
|
18.9
|
1.0
|
CB
|
A:CYS524
|
3.2
|
17.8
|
1.0
|
CB
|
A:CYS488
|
3.4
|
21.5
|
1.0
|
CB
|
A:CYS518
|
3.5
|
23.1
|
1.0
|
N
|
A:CYS488
|
3.8
|
16.5
|
1.0
|
N
|
A:CYS518
|
4.0
|
16.2
|
1.0
|
O
|
A:HOH2047
|
4.0
|
32.9
|
1.0
|
CA
|
A:CYS524
|
4.0
|
23.4
|
1.0
|
ZN
|
A:ZN993
|
4.1
|
21.3
|
1.0
|
O
|
A:HOH2077
|
4.1
|
25.3
|
1.0
|
CA
|
A:CYS488
|
4.2
|
22.3
|
1.0
|
CA
|
A:CYS518
|
4.2
|
20.6
|
1.0
|
CB
|
A:CYS487
|
4.4
|
21.8
|
1.0
|
SG
|
A:CYS532
|
4.6
|
22.6
|
1.0
|
CA
|
A:CYS485
|
4.6
|
16.0
|
1.0
|
C
|
A:CYS518
|
4.7
|
22.5
|
1.0
|
C
|
A:CYS487
|
4.8
|
24.8
|
1.0
|
N
|
A:HIS519
|
4.8
|
16.6
|
1.0
|
SG
|
A:CYS487
|
5.0
|
20.8
|
1.0
|
C
|
A:CYS488
|
5.0
|
26.4
|
1.0
|
|
Zinc binding site 3 out
of 10 in 2xp0
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Zinc Binding Sites List in 2xp0
Zinc binding site 3 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn993
b:21.3
occ:1.00
|
SG
|
A:CYS487
|
2.3
|
20.8
|
1.0
|
SG
|
A:CYS524
|
2.4
|
20.9
|
1.0
|
SG
|
A:CYS529
|
2.4
|
22.6
|
1.0
|
SG
|
A:CYS532
|
2.4
|
22.6
|
1.0
|
CB
|
A:CYS487
|
3.1
|
21.8
|
1.0
|
CB
|
A:CYS532
|
3.1
|
17.5
|
1.0
|
CB
|
A:CYS524
|
3.2
|
17.8
|
1.0
|
CB
|
A:CYS529
|
3.4
|
27.6
|
1.0
|
ZN
|
A:ZN992
|
4.1
|
21.8
|
1.0
|
N
|
A:CYS532
|
4.1
|
18.0
|
1.0
|
CA
|
A:CYS532
|
4.2
|
19.8
|
1.0
|
O
|
A:HOH2078
|
4.3
|
32.1
|
1.0
|
CA
|
A:CYS487
|
4.5
|
24.1
|
1.0
|
CA
|
A:CYS524
|
4.6
|
23.4
|
1.0
|
CA
|
A:CYS529
|
4.6
|
30.2
|
1.0
|
N
|
A:CYS488
|
4.7
|
16.5
|
1.0
|
C
|
A:CYS487
|
4.7
|
24.8
|
1.0
|
C
|
A:CYS524
|
4.8
|
28.4
|
1.0
|
SG
|
A:CYS485
|
4.8
|
20.7
|
1.0
|
CB
|
A:CYS488
|
5.0
|
21.5
|
1.0
|
|
Zinc binding site 4 out
of 10 in 2xp0
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Zinc Binding Sites List in 2xp0
Zinc binding site 4 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn994
b:20.1
occ:1.00
|
SG
|
A:CYS510
|
2.3
|
17.5
|
1.0
|
SG
|
A:CYS601
|
2.4
|
20.1
|
1.0
|
SG
|
A:CYS604
|
2.4
|
21.2
|
1.0
|
SG
|
A:CYS513
|
2.4
|
20.0
|
1.0
|
CB
|
A:CYS510
|
3.1
|
14.2
|
1.0
|
CB
|
A:CYS604
|
3.2
|
17.8
|
1.0
|
CB
|
A:CYS513
|
3.3
|
25.8
|
1.0
|
CB
|
A:CYS601
|
3.5
|
13.6
|
1.0
|
N
|
A:CYS513
|
3.7
|
22.6
|
1.0
|
O
|
A:HOH2168
|
3.9
|
22.6
|
1.0
|
N
|
A:CYS601
|
3.9
|
16.4
|
1.0
|
CA
|
A:CYS513
|
4.1
|
22.9
|
1.0
|
N
|
A:CYS604
|
4.2
|
18.1
|
1.0
|
CA
|
A:CYS601
|
4.3
|
16.8
|
1.0
|
CA
|
A:CYS604
|
4.3
|
18.2
|
1.0
|
CA
|
A:CYS510
|
4.5
|
19.4
|
1.0
|
CB
|
A:VAL512
|
4.6
|
22.0
|
1.0
|
CE2
|
A:PHE517
|
4.6
|
21.8
|
1.0
|
C
|
A:VAL512
|
4.8
|
24.7
|
1.0
|
C
|
A:CYS601
|
4.9
|
18.1
|
1.0
|
C
|
A:CYS513
|
4.9
|
21.0
|
1.0
|
O
|
A:CYS601
|
5.0
|
13.1
|
1.0
|
|
Zinc binding site 5 out
of 10 in 2xp0
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Zinc Binding Sites List in 2xp0
Zinc binding site 5 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn995
b:14.6
occ:1.00
|
NE2
|
A:HIS655
|
2.0
|
10.8
|
1.0
|
NE2
|
A:HIS649
|
2.1
|
15.1
|
1.0
|
SG
|
A:CYS635
|
2.3
|
13.7
|
1.0
|
SG
|
A:CYS641
|
2.3
|
13.4
|
1.0
|
CD2
|
A:HIS649
|
2.9
|
14.8
|
1.0
|
CD2
|
A:HIS655
|
3.0
|
7.8
|
1.0
|
CE1
|
A:HIS655
|
3.0
|
9.8
|
1.0
|
CB
|
A:CYS641
|
3.1
|
8.5
|
1.0
|
CE1
|
A:HIS649
|
3.2
|
15.9
|
1.0
|
CB
|
A:CYS635
|
3.2
|
10.5
|
1.0
|
ND1
|
A:HIS655
|
4.1
|
11.5
|
1.0
|
CG
|
A:HIS649
|
4.1
|
13.5
|
1.0
|
CG
|
A:HIS655
|
4.1
|
7.7
|
1.0
|
ND1
|
A:HIS649
|
4.2
|
15.3
|
1.0
|
CB
|
A:THR643
|
4.6
|
16.9
|
1.0
|
O
|
A:HOH2011
|
4.6
|
40.1
|
1.0
|
CA
|
A:CYS641
|
4.6
|
13.0
|
1.0
|
CA
|
A:CYS635
|
4.6
|
16.6
|
1.0
|
CD1
|
A:TRP637
|
4.7
|
15.5
|
1.0
|
N
|
A:GLN644
|
4.7
|
13.7
|
1.0
|
CB
|
A:GLN644
|
4.8
|
22.3
|
1.0
|
CB
|
A:TRP637
|
4.9
|
11.6
|
1.0
|
OG1
|
A:THR643
|
5.0
|
15.6
|
1.0
|
CB
|
A:PHE653
|
5.0
|
11.2
|
1.0
|
|
Zinc binding site 6 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 6 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn991
b:18.6
occ:1.00
|
NE2
|
B:HIS482
|
2.1
|
13.4
|
1.0
|
SG
|
B:CYS476
|
2.2
|
18.2
|
1.0
|
SG
|
B:CYS428
|
2.3
|
16.3
|
1.0
|
SG
|
B:CYS431
|
2.4
|
21.2
|
1.0
|
CD2
|
B:HIS482
|
3.0
|
11.6
|
1.0
|
CE1
|
B:HIS482
|
3.2
|
19.4
|
1.0
|
CB
|
B:CYS476
|
3.4
|
15.1
|
1.0
|
N
|
B:CYS431
|
3.4
|
17.8
|
1.0
|
CB
|
B:CYS428
|
3.5
|
14.8
|
1.0
|
CB
|
B:CYS431
|
3.5
|
21.4
|
1.0
|
CA
|
B:CYS431
|
3.6
|
21.4
|
1.0
|
N
|
B:CYS428
|
3.8
|
14.4
|
1.0
|
C
|
B:GLN430
|
4.1
|
19.6
|
1.0
|
CA
|
B:CYS428
|
4.1
|
15.9
|
1.0
|
CG
|
B:HIS482
|
4.2
|
13.3
|
1.0
|
ND1
|
B:HIS482
|
4.2
|
16.2
|
1.0
|
O
|
B:HOH2039
|
4.3
|
20.2
|
1.0
|
O
|
B:CYS428
|
4.4
|
15.8
|
1.0
|
C
|
B:CYS428
|
4.4
|
17.6
|
1.0
|
N
|
B:GLN430
|
4.6
|
17.4
|
1.0
|
O
|
B:GLN430
|
4.7
|
19.8
|
1.0
|
CA
|
B:GLN430
|
4.7
|
20.8
|
1.0
|
CA
|
B:CYS476
|
4.7
|
18.2
|
1.0
|
CD
|
B:PRO493
|
4.9
|
17.9
|
1.0
|
C
|
B:VAL427
|
4.9
|
22.5
|
1.0
|
CB
|
B:GLN430
|
4.9
|
20.7
|
1.0
|
CB
|
B:PRO493
|
4.9
|
13.7
|
1.0
|
N
|
B:PRO493
|
4.9
|
13.3
|
1.0
|
|
Zinc binding site 7 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 7 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 7 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn992
b:19.7
occ:1.00
|
SG
|
B:CYS485
|
2.3
|
18.0
|
1.0
|
SG
|
B:CYS518
|
2.3
|
19.1
|
1.0
|
SG
|
B:CYS488
|
2.4
|
20.1
|
1.0
|
SG
|
B:CYS524
|
2.4
|
16.8
|
1.0
|
CB
|
B:CYS485
|
3.0
|
14.7
|
1.0
|
CB
|
B:CYS488
|
3.3
|
17.5
|
1.0
|
CB
|
B:CYS524
|
3.3
|
18.5
|
1.0
|
CB
|
B:CYS518
|
3.5
|
13.2
|
1.0
|
N
|
B:CYS488
|
3.7
|
18.0
|
1.0
|
O
|
B:HOH2085
|
4.0
|
26.8
|
1.0
|
N
|
B:CYS518
|
4.0
|
17.8
|
1.0
|
ZN
|
B:ZN993
|
4.0
|
19.6
|
1.0
|
CA
|
B:CYS488
|
4.1
|
16.3
|
1.0
|
CA
|
B:CYS524
|
4.1
|
17.5
|
1.0
|
O
|
B:HOH2051
|
4.2
|
23.3
|
1.0
|
CA
|
B:CYS518
|
4.3
|
21.0
|
1.0
|
SG
|
B:CYS532
|
4.4
|
15.9
|
1.0
|
CA
|
B:CYS485
|
4.5
|
17.6
|
1.0
|
CB
|
B:CYS487
|
4.5
|
16.5
|
1.0
|
C
|
B:CYS518
|
4.8
|
20.1
|
1.0
|
N
|
B:HIS519
|
4.8
|
15.2
|
1.0
|
C
|
B:CYS487
|
4.8
|
25.2
|
1.0
|
SG
|
B:CYS487
|
4.9
|
21.2
|
1.0
|
C
|
B:CYS488
|
4.9
|
15.7
|
1.0
|
|
Zinc binding site 8 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 8 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 8 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn993
b:19.6
occ:1.00
|
SG
|
B:CYS487
|
2.2
|
21.2
|
1.0
|
SG
|
B:CYS532
|
2.3
|
15.9
|
1.0
|
SG
|
B:CYS529
|
2.4
|
19.6
|
1.0
|
SG
|
B:CYS524
|
2.5
|
16.8
|
1.0
|
CB
|
B:CYS532
|
3.1
|
17.9
|
1.0
|
CB
|
B:CYS487
|
3.1
|
16.5
|
1.0
|
CB
|
B:CYS524
|
3.2
|
18.5
|
1.0
|
CB
|
B:CYS529
|
3.3
|
23.6
|
1.0
|
N
|
B:CYS532
|
4.0
|
15.7
|
1.0
|
ZN
|
B:ZN992
|
4.0
|
19.7
|
1.0
|
CA
|
B:CYS532
|
4.2
|
15.1
|
1.0
|
CA
|
B:CYS487
|
4.5
|
19.5
|
1.0
|
CA
|
B:CYS529
|
4.5
|
23.9
|
1.0
|
N
|
B:CYS488
|
4.6
|
18.0
|
1.0
|
CA
|
B:CYS524
|
4.6
|
17.5
|
1.0
|
SG
|
B:CYS485
|
4.6
|
18.0
|
1.0
|
C
|
B:CYS487
|
4.7
|
25.2
|
1.0
|
O
|
B:HOH2086
|
4.8
|
44.0
|
1.0
|
C
|
B:CYS524
|
4.9
|
25.5
|
1.0
|
|
Zinc binding site 9 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 9 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 9 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn994
b:17.8
occ:1.00
|
SG
|
B:CYS601
|
2.3
|
18.2
|
1.0
|
SG
|
B:CYS604
|
2.3
|
17.9
|
1.0
|
SG
|
B:CYS510
|
2.4
|
14.0
|
1.0
|
SG
|
B:CYS513
|
2.4
|
17.5
|
1.0
|
CB
|
B:CYS510
|
3.1
|
12.3
|
1.0
|
CB
|
B:CYS604
|
3.1
|
15.5
|
1.0
|
CB
|
B:CYS513
|
3.2
|
22.4
|
1.0
|
CB
|
B:CYS601
|
3.5
|
9.7
|
1.0
|
N
|
B:CYS513
|
3.7
|
16.1
|
1.0
|
N
|
B:CYS601
|
4.0
|
14.2
|
1.0
|
CA
|
B:CYS513
|
4.0
|
21.2
|
1.0
|
N
|
B:CYS604
|
4.2
|
12.6
|
1.0
|
CA
|
B:CYS604
|
4.3
|
17.7
|
1.0
|
CA
|
B:CYS601
|
4.3
|
15.5
|
1.0
|
O
|
B:HOH2075
|
4.3
|
31.0
|
1.0
|
O
|
B:HOH2188
|
4.4
|
48.5
|
1.0
|
CA
|
B:CYS510
|
4.5
|
12.9
|
1.0
|
CB
|
B:VAL512
|
4.7
|
15.4
|
1.0
|
C
|
B:VAL512
|
4.8
|
19.6
|
1.0
|
C
|
B:CYS513
|
4.9
|
22.8
|
1.0
|
C
|
B:CYS601
|
5.0
|
18.1
|
1.0
|
O
|
B:CYS601
|
5.0
|
12.8
|
1.0
|
N
|
B:LEU514
|
5.0
|
17.5
|
1.0
|
|
Zinc binding site 10 out
of 10 in 2xp0
Go back to
Zinc Binding Sites List in 2xp0
Zinc binding site 10 out
of 10 in the C-Terminal Cysteine-Rich Domain of Human Chfr
Mono view
Stereo pair view
|
A full contact list of Zinc with other atoms in the Zn binding
site number 10 of C-Terminal Cysteine-Rich Domain of Human Chfr within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn995
b:17.2
occ:1.00
|
NE2
|
B:HIS655
|
2.2
|
11.1
|
1.0
|
NE2
|
B:HIS649
|
2.2
|
21.4
|
1.0
|
SG
|
B:CYS635
|
2.3
|
17.9
|
1.0
|
SG
|
B:CYS641
|
2.3
|
14.1
|
1.0
|
CD2
|
B:HIS655
|
3.0
|
12.1
|
1.0
|
CD2
|
B:HIS649
|
3.0
|
17.8
|
1.0
|
CB
|
B:CYS641
|
3.1
|
9.3
|
1.0
|
CB
|
B:CYS635
|
3.2
|
9.6
|
1.0
|
CE1
|
B:HIS655
|
3.2
|
13.5
|
1.0
|
CE1
|
B:HIS649
|
3.2
|
31.2
|
1.0
|
CG
|
B:HIS655
|
4.2
|
13.0
|
1.0
|
CG
|
B:HIS649
|
4.2
|
20.2
|
1.0
|
ND1
|
B:HIS655
|
4.3
|
15.1
|
1.0
|
ND1
|
B:HIS649
|
4.3
|
26.5
|
1.0
|
O
|
B:HOH2251
|
4.4
|
45.5
|
1.0
|
CD1
|
B:TRP637
|
4.5
|
30.9
|
1.0
|
CA
|
B:CYS641
|
4.5
|
15.7
|
1.0
|
CA
|
B:CYS635
|
4.6
|
20.3
|
1.0
|
CB
|
B:TRP637
|
4.7
|
12.9
|
1.0
|
N
|
B:GLN644
|
4.7
|
16.2
|
1.0
|
CB
|
B:GLN644
|
4.8
|
15.8
|
1.0
|
CB
|
B:THR643
|
4.9
|
18.3
|
1.0
|
|
Reference:
J.Oberoi,
M.W.Richards,
S.Crumpler,
N.Brown,
J.Blagg,
R.Bayliss.
Structural Basis of Poly(Adp-Ribose) Recognition By the Multizinc Binding Domain of Checkpoint with Forkhead-Associated and Ring Domains (Chfr). J.Biol.Chem. V. 285 39348 2010.
ISSN: ISSN 0021-9258
PubMed: 20880844
DOI: 10.1074/JBC.M110.159855
Page generated: Thu Oct 17 05:26:17 2024
|