Bromine in PDB 1d2v: Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Enzymatic activity of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
All present enzymatic activity of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5:
1.11.1.7;
Protein crystallography data
The structure of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5, PDB code: 1d2v
was solved by
T.J.Fiedler,
C.A.Davey,
R.E.Fenna,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
30.00 /
1.75
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
111.155,
63.488,
92.476,
90.00,
97.36,
90.00
|
R / Rfree (%)
|
24.3 /
29.6
|
Other elements in 1d2v:
The structure of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 also contains other interesting chemical elements:
Bromine Binding Sites:
The binding sites of Bromine atom in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
(pdb code 1d2v). This binding sites where shown within
5.0 Angstroms radius around Bromine atom.
In total 8 binding sites of Bromine where determined in the
Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5, PDB code: 1d2v:
Jump to Bromine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Bromine binding site 1 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 1 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 1 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br601
b:6.7
occ:1.00
|
N
|
A:TRP32
|
3.3
|
4.3
|
1.0
|
O
|
A:HOH652A
|
3.3
|
2.0
|
1.0
|
N
|
C:VAL327
|
3.4
|
2.0
|
1.0
|
CB
|
C:ASN326
|
3.6
|
4.2
|
1.0
|
CH2
|
C:TRP436
|
3.6
|
4.3
|
1.0
|
N
|
C:ASN326
|
3.7
|
4.2
|
1.0
|
CZ2
|
C:TRP436
|
3.8
|
2.6
|
1.0
|
CA
|
A:ARG31
|
3.8
|
7.3
|
1.0
|
CB
|
C:VAL327
|
3.9
|
4.8
|
1.0
|
CG1
|
C:VAL327
|
3.9
|
3.6
|
1.0
|
CA
|
C:ASN326
|
4.0
|
4.7
|
1.0
|
O
|
A:VAL30
|
4.0
|
5.0
|
1.0
|
C
|
A:ARG31
|
4.0
|
6.7
|
1.0
|
N
|
A:LEU33
|
4.1
|
5.2
|
1.0
|
CD2
|
C:LEU430
|
4.1
|
6.3
|
1.0
|
C
|
C:ASN326
|
4.1
|
2.0
|
1.0
|
CD
|
A:ARG31
|
4.2
|
7.2
|
1.0
|
CA
|
A:TRP32
|
4.2
|
5.3
|
1.0
|
CB
|
A:TRP32
|
4.2
|
6.5
|
1.0
|
CA
|
C:VAL327
|
4.2
|
2.8
|
1.0
|
O
|
A:LEU33
|
4.3
|
3.7
|
1.0
|
C
|
C:ALA325
|
4.6
|
4.7
|
1.0
|
CB
|
A:ARG31
|
4.6
|
9.7
|
1.0
|
CB
|
C:ALA325
|
4.6
|
2.5
|
1.0
|
C
|
A:TRP32
|
4.7
|
6.5
|
1.0
|
NH1
|
A:ARG31
|
4.7
|
3.2
|
1.0
|
N
|
A:ARG31
|
4.9
|
6.0
|
1.0
|
C
|
A:VAL30
|
4.9
|
5.7
|
1.0
|
CG
|
C:ASN326
|
4.9
|
4.9
|
1.0
|
CZ3
|
C:TRP436
|
4.9
|
3.4
|
1.0
|
CG
|
A:TRP32
|
4.9
|
6.7
|
1.0
|
CG
|
A:ARG31
|
5.0
|
10.4
|
1.0
|
CA
|
C:ALA325
|
5.0
|
5.2
|
1.0
|
|
Bromine binding site 2 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 2 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 2 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br758
b:16.2
occ:0.55
|
N
|
C:THR544
|
3.3
|
9.6
|
1.0
|
NH1
|
C:ARG382
|
3.5
|
17.0
|
1.0
|
CG2
|
C:ILE543
|
3.5
|
12.1
|
1.0
|
O
|
C:ASN348
|
3.5
|
22.4
|
1.0
|
N
|
C:THR545
|
3.7
|
8.3
|
1.0
|
CA
|
C:ILE543
|
3.8
|
10.4
|
1.0
|
O
|
C:HOH777A
|
3.8
|
24.7
|
1.0
|
CD
|
C:ARG382
|
3.9
|
16.3
|
1.0
|
C
|
C:ILE543
|
4.0
|
9.4
|
1.0
|
OG1
|
C:THR544
|
4.0
|
8.3
|
1.0
|
O
|
C:THR545
|
4.1
|
10.9
|
1.0
|
CB
|
C:ILE543
|
4.2
|
12.5
|
1.0
|
C
|
C:ASN348
|
4.2
|
21.0
|
1.0
|
CA
|
C:ASN348
|
4.2
|
19.9
|
1.0
|
CE1
|
C:TYR350
|
4.3
|
17.1
|
1.0
|
CA
|
C:THR544
|
4.3
|
9.9
|
1.0
|
CB
|
C:ASN348
|
4.4
|
18.9
|
1.0
|
CZ
|
C:ARG382
|
4.5
|
17.8
|
1.0
|
C
|
C:THR544
|
4.5
|
8.8
|
1.0
|
CA
|
C:THR545
|
4.6
|
11.2
|
1.0
|
CB
|
C:THR545
|
4.6
|
14.8
|
1.0
|
NE
|
C:ARG382
|
4.6
|
20.0
|
1.0
|
O
|
C:GLY542
|
4.7
|
10.7
|
1.0
|
C
|
C:THR545
|
4.8
|
10.4
|
1.0
|
CG1
|
C:ILE543
|
4.8
|
9.3
|
1.0
|
CB
|
C:THR544
|
4.8
|
10.4
|
1.0
|
CD1
|
C:TYR350
|
4.8
|
17.0
|
1.0
|
CG
|
C:ARG382
|
4.9
|
14.5
|
1.0
|
N
|
C:ILE543
|
5.0
|
9.1
|
1.0
|
|
Bromine binding site 3 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 3 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 3 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br843
b:12.7
occ:0.44
|
O
|
C:HOH957A
|
2.7
|
11.4
|
1.0
|
O
|
A:HOH844A
|
3.1
|
8.6
|
1.0
|
CG
|
C:GLU242
|
3.3
|
5.7
|
1.0
|
CE1
|
A:HIS95
|
3.5
|
5.8
|
1.0
|
NE2
|
A:HIS95
|
3.6
|
8.7
|
1.0
|
NE2
|
A:GLN91
|
3.6
|
8.4
|
1.0
|
CD
|
C:GLU242
|
3.6
|
4.2
|
1.0
|
O
|
C:HOH845A
|
3.6
|
2.0
|
1.0
|
CB
|
C:GLU242
|
3.7
|
6.3
|
1.0
|
CHB
|
A:HEM605
|
3.8
|
3.9
|
1.0
|
C1B
|
A:HEM605
|
3.9
|
5.2
|
1.0
|
OE2
|
C:GLU242
|
3.9
|
9.3
|
1.0
|
CD
|
C:ARG239
|
4.0
|
7.6
|
1.0
|
OE1
|
C:GLU242
|
4.0
|
4.9
|
1.0
|
CB
|
C:ARG239
|
4.0
|
3.3
|
1.0
|
C4A
|
A:HEM605
|
4.0
|
5.7
|
1.0
|
CG
|
C:ARG239
|
4.2
|
6.8
|
1.0
|
NB
|
A:HEM605
|
4.3
|
6.5
|
1.0
|
NA
|
A:HEM605
|
4.4
|
6.6
|
1.0
|
C2B
|
A:HEM605
|
4.5
|
4.6
|
1.0
|
C3A
|
A:HEM605
|
4.5
|
4.7
|
1.0
|
CD
|
A:GLN91
|
4.7
|
7.8
|
1.0
|
ND1
|
A:HIS95
|
4.8
|
6.0
|
1.0
|
CD2
|
A:HIS95
|
4.9
|
8.5
|
1.0
|
C1A
|
A:HEM605
|
4.9
|
6.7
|
1.0
|
O
|
C:ARG239
|
4.9
|
2.4
|
1.0
|
CMB
|
A:HEM605
|
5.0
|
5.6
|
1.0
|
C4B
|
A:HEM605
|
5.0
|
5.3
|
1.0
|
|
Bromine binding site 4 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 4 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 4 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Br889
b:24.4
occ:0.60
|
N
|
C:PHE213
|
3.4
|
10.2
|
1.0
|
N
|
C:GLN201
|
3.4
|
12.1
|
1.0
|
OD1
|
C:ASN200
|
3.5
|
13.0
|
1.0
|
CA
|
C:PRO212
|
3.7
|
10.8
|
1.0
|
CG
|
C:ASN200
|
3.7
|
12.0
|
1.0
|
CA
|
C:ASN200
|
3.8
|
9.2
|
1.0
|
CB
|
C:PRO212
|
3.9
|
9.7
|
1.0
|
C
|
C:PRO212
|
4.0
|
9.6
|
1.0
|
ND2
|
C:ASN200
|
4.1
|
9.1
|
1.0
|
C
|
C:ASN200
|
4.1
|
9.7
|
1.0
|
CD1
|
C:PHE213
|
4.2
|
7.5
|
1.0
|
CB
|
C:PHE213
|
4.3
|
9.2
|
1.0
|
CB
|
C:ASN200
|
4.3
|
9.0
|
1.0
|
CA
|
C:PHE213
|
4.4
|
9.3
|
1.0
|
CB
|
C:GLN201
|
4.4
|
16.2
|
1.0
|
CA
|
C:GLN201
|
4.4
|
15.0
|
1.0
|
CG
|
C:PHE213
|
4.5
|
9.4
|
1.0
|
N
|
C:ARG202
|
4.6
|
15.1
|
1.0
|
O
|
C:PHE213
|
4.7
|
8.8
|
1.0
|
CG
|
C:GLN201
|
4.7
|
16.4
|
1.0
|
O
|
C:VAL199
|
4.8
|
11.5
|
1.0
|
N
|
C:ASN200
|
4.9
|
8.0
|
1.0
|
CG
|
C:ARG202
|
5.0
|
23.5
|
1.0
|
C
|
C:GLN201
|
5.0
|
16.1
|
1.0
|
|
Bromine binding site 5 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 5 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 5 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br601
b:6.7
occ:1.00
|
N
|
D:VAL327
|
3.3
|
2.0
|
1.0
|
N
|
B:TRP32
|
3.3
|
5.4
|
1.0
|
O
|
B:HOH652B
|
3.3
|
3.2
|
1.0
|
CB
|
D:ASN326
|
3.6
|
5.8
|
1.0
|
CH2
|
D:TRP436
|
3.6
|
4.2
|
1.0
|
N
|
D:ASN326
|
3.7
|
2.0
|
1.0
|
CB
|
D:VAL327
|
3.8
|
3.2
|
1.0
|
CA
|
B:ARG31
|
3.8
|
4.9
|
1.0
|
CZ2
|
D:TRP436
|
3.9
|
4.8
|
1.0
|
CG1
|
D:VAL327
|
3.9
|
2.2
|
1.0
|
CA
|
D:ASN326
|
4.0
|
3.3
|
1.0
|
O
|
B:VAL30
|
4.0
|
5.9
|
1.0
|
C
|
B:ARG31
|
4.0
|
5.9
|
1.0
|
C
|
D:ASN326
|
4.1
|
2.4
|
1.0
|
CA
|
D:VAL327
|
4.1
|
2.6
|
1.0
|
N
|
B:LEU33
|
4.1
|
6.2
|
1.0
|
CD2
|
D:LEU430
|
4.1
|
5.4
|
1.0
|
CA
|
B:TRP32
|
4.3
|
6.1
|
1.0
|
CB
|
B:TRP32
|
4.3
|
6.2
|
1.0
|
O
|
B:LEU33
|
4.4
|
7.7
|
1.0
|
CD
|
B:ARG31
|
4.4
|
5.1
|
1.0
|
C
|
D:ALA325
|
4.5
|
5.0
|
1.0
|
CB
|
D:ALA325
|
4.5
|
6.9
|
1.0
|
CB
|
B:ARG31
|
4.6
|
4.7
|
1.0
|
C
|
B:TRP32
|
4.7
|
5.9
|
1.0
|
N
|
B:ARG31
|
4.8
|
6.7
|
1.0
|
C
|
B:VAL30
|
4.8
|
4.8
|
1.0
|
NH1
|
B:ARG31
|
4.9
|
3.9
|
1.0
|
CZ3
|
D:TRP436
|
4.9
|
5.0
|
1.0
|
CG
|
D:ASN326
|
4.9
|
4.9
|
1.0
|
CA
|
D:ALA325
|
4.9
|
5.6
|
1.0
|
CG
|
B:TRP32
|
4.9
|
8.8
|
1.0
|
|
Bromine binding site 6 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 6 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 6 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br758
b:18.1
occ:0.53
|
O
|
D:ASN348
|
3.3
|
29.3
|
1.0
|
N
|
D:THR544
|
3.4
|
18.3
|
1.0
|
CA
|
D:ILE543
|
3.6
|
18.3
|
1.0
|
CG2
|
D:ILE543
|
3.7
|
18.3
|
1.0
|
N
|
D:THR545
|
3.8
|
16.6
|
1.0
|
NH1
|
D:ARG382
|
3.9
|
18.0
|
1.0
|
C
|
D:ILE543
|
4.0
|
19.1
|
1.0
|
CA
|
D:ASN348
|
4.0
|
26.9
|
1.0
|
CB
|
D:ILE543
|
4.1
|
19.5
|
1.0
|
C
|
D:ASN348
|
4.1
|
27.8
|
1.0
|
OG1
|
D:THR544
|
4.2
|
22.6
|
1.0
|
CB
|
D:ASN348
|
4.3
|
28.6
|
1.0
|
O
|
D:THR545
|
4.3
|
12.9
|
1.0
|
CE1
|
D:TYR350
|
4.3
|
16.4
|
1.0
|
CG1
|
D:ILE543
|
4.3
|
19.2
|
1.0
|
CB
|
D:THR545
|
4.3
|
16.5
|
1.0
|
CD
|
D:ARG382
|
4.4
|
15.3
|
1.0
|
CA
|
D:THR544
|
4.5
|
18.3
|
1.0
|
CA
|
D:THR545
|
4.6
|
16.5
|
1.0
|
C
|
D:THR544
|
4.6
|
16.8
|
1.0
|
O
|
D:HOH1248B
|
4.7
|
23.9
|
1.0
|
N
|
D:ILE543
|
4.8
|
19.3
|
1.0
|
O
|
D:GLY542
|
4.9
|
20.1
|
1.0
|
CD1
|
D:TYR350
|
4.9
|
16.5
|
1.0
|
C
|
D:THR545
|
4.9
|
13.7
|
1.0
|
CZ
|
D:ARG382
|
4.9
|
11.8
|
1.0
|
OG1
|
D:THR545
|
5.0
|
20.1
|
1.0
|
CB
|
D:THR544
|
5.0
|
20.5
|
1.0
|
|
Bromine binding site 7 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 7 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 7 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br843
b:12.6
occ:0.44
|
O
|
D:HOH957B
|
2.9
|
15.3
|
1.0
|
O
|
B:HOH844B
|
3.2
|
21.1
|
1.0
|
CE1
|
B:HIS95
|
3.3
|
6.7
|
1.0
|
NE2
|
B:GLN91
|
3.4
|
3.2
|
1.0
|
CG
|
D:GLU242
|
3.4
|
9.3
|
1.0
|
NE2
|
B:HIS95
|
3.5
|
5.2
|
1.0
|
CD
|
D:GLU242
|
3.6
|
9.7
|
1.0
|
O
|
D:HOH845B
|
3.7
|
6.7
|
1.0
|
CB
|
D:GLU242
|
3.7
|
9.0
|
1.0
|
CHB
|
B:HEM605
|
3.8
|
5.8
|
1.0
|
OE1
|
D:GLU242
|
3.9
|
8.7
|
1.0
|
C1B
|
B:HEM605
|
3.9
|
3.8
|
1.0
|
CD
|
D:ARG239
|
4.0
|
5.5
|
1.0
|
C4A
|
B:HEM605
|
4.0
|
8.5
|
1.0
|
CB
|
D:ARG239
|
4.0
|
5.8
|
1.0
|
OE2
|
D:GLU242
|
4.1
|
8.6
|
1.0
|
CG
|
D:ARG239
|
4.3
|
8.2
|
1.0
|
NB
|
B:HEM605
|
4.3
|
5.5
|
1.0
|
NA
|
B:HEM605
|
4.4
|
8.4
|
1.0
|
C2B
|
B:HEM605
|
4.4
|
2.9
|
1.0
|
CD
|
B:GLN91
|
4.6
|
4.9
|
1.0
|
C3A
|
B:HEM605
|
4.6
|
6.6
|
1.0
|
ND1
|
B:HIS95
|
4.6
|
4.2
|
1.0
|
CMB
|
B:HEM605
|
4.8
|
3.3
|
1.0
|
CD2
|
B:HIS95
|
4.8
|
5.0
|
1.0
|
NE
|
D:ARG239
|
4.9
|
5.1
|
1.0
|
C4B
|
B:HEM605
|
4.9
|
4.2
|
1.0
|
O
|
D:ARG239
|
4.9
|
5.3
|
1.0
|
C1A
|
B:HEM605
|
5.0
|
7.5
|
1.0
|
C3B
|
B:HEM605
|
5.0
|
3.7
|
1.0
|
FE
|
B:HEM605
|
5.0
|
9.3
|
1.0
|
CG
|
B:GLN91
|
5.0
|
6.1
|
1.0
|
|
Bromine binding site 8 out
of 8 in 1d2v
Go back to
Bromine Binding Sites List in 1d2v
Bromine binding site 8 out
of 8 in the Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5
Mono view
Stereo pair view
|
A full contact list of Bromine with other atoms in the Br binding
site number 8 of Crystal Structure of Bromide-Bound Human Myeloperoxidase Isoform C at pH 5.5 within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Br889
b:23.4
occ:0.60
|
N
|
D:PHE213
|
3.4
|
11.5
|
1.0
|
N
|
D:GLN201
|
3.5
|
19.1
|
1.0
|
ND2
|
D:ASN200
|
3.7
|
14.5
|
1.0
|
CA
|
D:ASN200
|
3.8
|
16.4
|
1.0
|
CG
|
D:ASN200
|
3.8
|
15.5
|
1.0
|
CA
|
D:PRO212
|
3.9
|
13.8
|
1.0
|
OD1
|
D:ASN200
|
4.1
|
14.7
|
1.0
|
C
|
D:ASN200
|
4.2
|
16.8
|
1.0
|
C
|
D:PRO212
|
4.2
|
12.3
|
1.0
|
CD1
|
D:PHE213
|
4.2
|
10.7
|
1.0
|
CB
|
D:PRO212
|
4.2
|
17.1
|
1.0
|
CB
|
D:PHE213
|
4.2
|
10.6
|
1.0
|
CG
|
D:ARG202
|
4.3
|
32.6
|
1.0
|
CB
|
D:ASN200
|
4.4
|
14.9
|
1.0
|
CA
|
D:PHE213
|
4.4
|
11.7
|
1.0
|
CA
|
D:GLN201
|
4.4
|
23.5
|
1.0
|
CB
|
D:GLN201
|
4.4
|
23.9
|
1.0
|
CG
|
D:PHE213
|
4.5
|
8.0
|
1.0
|
O
|
D:VAL199
|
4.7
|
15.2
|
1.0
|
N
|
D:ARG202
|
4.8
|
25.2
|
1.0
|
C
|
D:GLN201
|
4.9
|
25.5
|
1.0
|
N
|
D:ASN200
|
4.9
|
16.1
|
1.0
|
CG
|
D:GLN201
|
4.9
|
28.9
|
1.0
|
O
|
D:PHE213
|
4.9
|
15.4
|
1.0
|
|
Reference:
T.J.Fiedler,
C.A.Davey,
R.E.Fenna.
X-Ray Crystal Structure and Characterization of Halide-Binding Sites of Human Myeloperoxidase at 1.8 A Resolution. J.Biol.Chem. V. 275 11964 2000.
ISSN: ISSN 0021-9258
PubMed: 10766826
DOI: 10.1074/JBC.275.16.11964
Page generated: Wed Jul 10 16:22:12 2024
|