Fluorine in PDB 1njt: Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Enzymatic activity of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
All present enzymatic activity of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor:
3.4.21.97;
Protein crystallography data
The structure of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor, PDB code: 1njt
was solved by
R.Khayat,
R.Batra,
C.Qian,
T.Halmos,
M.Bailey,
L.Tong,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
19.95 /
2.50
|
Space group
|
P 21 21 2
|
Cell size a, b, c (Å), α, β, γ (°)
|
107.072,
213.306,
52.795,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
22.8 /
27.1
|
Other elements in 1njt:
The structure of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor also contains other interesting chemical elements:
Fluorine Binding Sites:
Pages:
>>> Page 1 <<<
Page 2, Binding sites: 11 -
12;
Binding sites:
The binding sites of Fluorine atom in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
(pdb code 1njt). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the
Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor, PDB code: 1njt:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
9;
10;
Fluorine binding site 1 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 1 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F265
b:29.1
occ:1.00
|
FB1
|
E:CFT265
|
0.0
|
29.1
|
1.0
|
C1
|
E:CFT265
|
1.3
|
27.3
|
1.0
|
FB3
|
E:CFT265
|
2.1
|
27.2
|
1.0
|
FB2
|
E:CFT265
|
2.1
|
27.7
|
1.0
|
C
|
E:ALA264
|
2.4
|
26.5
|
1.0
|
CA
|
E:ALA264
|
2.8
|
27.7
|
1.0
|
O
|
E:ALA264
|
2.9
|
25.3
|
1.0
|
CG
|
A:ARG165
|
3.3
|
25.7
|
1.0
|
O
|
E:DMH263
|
3.3
|
31.9
|
1.0
|
CB
|
A:ARG165
|
3.6
|
23.9
|
1.0
|
OG
|
A:SER132
|
3.6
|
24.2
|
1.0
|
N
|
E:ALA264
|
3.7
|
29.4
|
1.0
|
NE
|
A:ARG165
|
3.8
|
29.8
|
1.0
|
C
|
E:DMH263
|
3.8
|
31.2
|
1.0
|
N
|
A:ARG165
|
3.9
|
22.6
|
1.0
|
CB
|
E:ALA264
|
4.1
|
28.4
|
1.0
|
CD
|
A:ARG165
|
4.1
|
27.7
|
1.0
|
CA
|
A:ARG165
|
4.3
|
23.9
|
1.0
|
CB
|
A:SER132
|
4.5
|
21.8
|
1.0
|
C
|
A:GLY164
|
4.8
|
21.2
|
1.0
|
NE2
|
A:HIS63
|
4.8
|
20.4
|
1.0
|
CZ
|
A:ARG165
|
4.9
|
31.5
|
1.0
|
|
Fluorine binding site 2 out
of 12 in 1njt
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Fluorine Binding Sites List in 1njt
Fluorine binding site 2 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F265
b:27.7
occ:1.00
|
FB2
|
E:CFT265
|
0.0
|
27.7
|
1.0
|
C1
|
E:CFT265
|
1.3
|
27.3
|
1.0
|
FB3
|
E:CFT265
|
2.1
|
27.2
|
1.0
|
FB1
|
E:CFT265
|
2.1
|
29.1
|
1.0
|
C
|
E:ALA264
|
2.4
|
26.5
|
1.0
|
O
|
E:ALA264
|
2.7
|
25.3
|
1.0
|
OG
|
A:SER132
|
3.0
|
24.2
|
1.0
|
CB
|
A:SER132
|
3.2
|
21.8
|
1.0
|
CA
|
E:ALA264
|
3.7
|
27.7
|
1.0
|
SG
|
A:CYS161
|
3.8
|
23.4
|
1.0
|
O
|
A:VAL163
|
3.9
|
18.6
|
1.0
|
NE2
|
A:HIS63
|
4.2
|
20.4
|
1.0
|
CA
|
A:GLY164
|
4.3
|
20.3
|
1.0
|
N
|
A:ARG165
|
4.3
|
22.6
|
1.0
|
CD2
|
A:HIS63
|
4.3
|
20.0
|
1.0
|
CB
|
A:CYS161
|
4.4
|
19.6
|
1.0
|
N
|
E:ALA264
|
4.4
|
29.4
|
1.0
|
OD1
|
A:ASN62
|
4.6
|
18.6
|
1.0
|
CA
|
A:SER132
|
4.7
|
20.1
|
1.0
|
C
|
A:GLY164
|
4.7
|
21.2
|
1.0
|
CB
|
E:ALA264
|
4.8
|
28.4
|
1.0
|
O
|
E:DMH263
|
4.8
|
31.9
|
1.0
|
C
|
A:VAL163
|
4.9
|
19.1
|
1.0
|
C
|
E:DMH263
|
4.9
|
31.2
|
1.0
|
CG
|
A:ARG165
|
4.9
|
25.7
|
1.0
|
|
Fluorine binding site 3 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 3 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
E:F265
b:27.2
occ:1.00
|
FB3
|
E:CFT265
|
0.0
|
27.2
|
1.0
|
C1
|
E:CFT265
|
1.3
|
27.3
|
1.0
|
FB1
|
E:CFT265
|
2.1
|
29.1
|
1.0
|
FB2
|
E:CFT265
|
2.1
|
27.7
|
1.0
|
C
|
E:ALA264
|
2.4
|
26.5
|
1.0
|
OG
|
A:SER132
|
2.7
|
24.2
|
1.0
|
NE2
|
A:HIS63
|
2.9
|
20.4
|
1.0
|
CA
|
E:ALA264
|
3.0
|
27.7
|
1.0
|
CD2
|
A:HIS63
|
3.0
|
20.0
|
1.0
|
N
|
E:ALA264
|
3.1
|
29.4
|
1.0
|
O
|
E:DMH263
|
3.2
|
31.9
|
1.0
|
C
|
E:DMH263
|
3.2
|
31.2
|
1.0
|
O
|
E:ALA264
|
3.5
|
25.3
|
1.0
|
CB
|
A:SER132
|
3.7
|
21.8
|
1.0
|
CB
|
E:DMH263
|
3.9
|
30.9
|
1.0
|
CE1
|
A:HIS63
|
4.1
|
20.2
|
1.0
|
CA
|
E:DMH263
|
4.1
|
31.8
|
1.0
|
CG
|
A:HIS63
|
4.3
|
20.4
|
1.0
|
CB
|
E:ALA264
|
4.5
|
28.4
|
1.0
|
ND1
|
A:HIS63
|
4.8
|
19.6
|
1.0
|
OD1
|
A:ASN62
|
5.0
|
18.6
|
1.0
|
|
Fluorine binding site 4 out
of 12 in 1njt
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Fluorine Binding Sites List in 1njt
Fluorine binding site 4 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:F565
b:25.9
occ:1.00
|
FB1
|
F:CFT565
|
0.0
|
25.9
|
1.0
|
C1
|
F:CFT565
|
1.3
|
24.3
|
1.0
|
FB2
|
F:CFT565
|
2.1
|
24.3
|
1.0
|
FB3
|
F:CFT565
|
2.1
|
23.0
|
1.0
|
C
|
F:ALA564
|
2.4
|
24.3
|
1.0
|
O
|
F:ALA564
|
2.9
|
24.0
|
1.0
|
CA
|
F:ALA564
|
2.9
|
25.2
|
1.0
|
CG
|
B:ARG465
|
3.2
|
20.9
|
1.0
|
O
|
F:DMH563
|
3.4
|
28.4
|
1.0
|
NE
|
B:ARG465
|
3.5
|
22.3
|
1.0
|
CB
|
B:ARG465
|
3.5
|
21.2
|
1.0
|
OG
|
B:SER432
|
3.6
|
22.5
|
1.0
|
N
|
F:ALA564
|
3.7
|
26.4
|
1.0
|
N
|
B:ARG465
|
3.8
|
20.0
|
1.0
|
CD
|
B:ARG465
|
3.9
|
21.3
|
1.0
|
C
|
F:DMH563
|
3.9
|
27.4
|
1.0
|
CB
|
F:ALA564
|
4.1
|
25.9
|
1.0
|
CA
|
B:ARG465
|
4.3
|
21.0
|
1.0
|
CB
|
B:SER432
|
4.4
|
20.2
|
1.0
|
CZ
|
B:ARG465
|
4.6
|
22.4
|
1.0
|
C
|
B:GLY464
|
4.7
|
19.3
|
1.0
|
NH2
|
B:ARG465
|
4.8
|
22.3
|
1.0
|
NE2
|
B:HIS363
|
4.8
|
17.3
|
1.0
|
CA
|
B:GLY464
|
4.9
|
18.5
|
1.0
|
|
Fluorine binding site 5 out
of 12 in 1njt
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Fluorine Binding Sites List in 1njt
Fluorine binding site 5 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:F565
b:24.3
occ:1.00
|
FB2
|
F:CFT565
|
0.0
|
24.3
|
1.0
|
C1
|
F:CFT565
|
1.3
|
24.3
|
1.0
|
FB1
|
F:CFT565
|
2.1
|
25.9
|
1.0
|
FB3
|
F:CFT565
|
2.1
|
23.0
|
1.0
|
C
|
F:ALA564
|
2.4
|
24.3
|
1.0
|
O
|
F:ALA564
|
2.7
|
24.0
|
1.0
|
OG
|
B:SER432
|
2.9
|
22.5
|
1.0
|
CB
|
B:SER432
|
3.2
|
20.2
|
1.0
|
CA
|
F:ALA564
|
3.7
|
25.2
|
1.0
|
SG
|
B:CYS461
|
3.8
|
22.2
|
1.0
|
O
|
B:VAL463
|
4.0
|
17.0
|
1.0
|
NE2
|
B:HIS363
|
4.0
|
17.3
|
1.0
|
CD2
|
B:HIS363
|
4.3
|
15.8
|
1.0
|
CA
|
B:GLY464
|
4.3
|
18.5
|
1.0
|
N
|
B:ARG465
|
4.3
|
20.0
|
1.0
|
CB
|
B:CYS461
|
4.3
|
18.7
|
1.0
|
N
|
F:ALA564
|
4.4
|
26.4
|
1.0
|
ND2
|
B:ASN362
|
4.5
|
24.5
|
1.0
|
CA
|
B:SER432
|
4.6
|
18.3
|
1.0
|
C
|
B:GLY464
|
4.7
|
19.3
|
1.0
|
CB
|
F:ALA564
|
4.8
|
25.9
|
1.0
|
O
|
F:DMH563
|
4.8
|
28.4
|
1.0
|
C
|
B:VAL463
|
4.9
|
17.1
|
1.0
|
CG
|
B:ARG465
|
4.9
|
20.9
|
1.0
|
C
|
F:DMH563
|
4.9
|
27.4
|
1.0
|
|
Fluorine binding site 6 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 6 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
F:F565
b:23.0
occ:1.00
|
FB3
|
F:CFT565
|
0.0
|
23.0
|
1.0
|
C1
|
F:CFT565
|
1.3
|
24.3
|
1.0
|
FB2
|
F:CFT565
|
2.1
|
24.3
|
1.0
|
FB1
|
F:CFT565
|
2.1
|
25.9
|
1.0
|
C
|
F:ALA564
|
2.4
|
24.3
|
1.0
|
OG
|
B:SER432
|
2.8
|
22.5
|
1.0
|
NE2
|
B:HIS363
|
2.9
|
17.3
|
1.0
|
CA
|
F:ALA564
|
3.0
|
25.2
|
1.0
|
CD2
|
B:HIS363
|
3.1
|
15.8
|
1.0
|
N
|
F:ALA564
|
3.1
|
26.4
|
1.0
|
O
|
F:DMH563
|
3.1
|
28.4
|
1.0
|
C
|
F:DMH563
|
3.2
|
27.4
|
1.0
|
O
|
F:ALA564
|
3.6
|
24.0
|
1.0
|
CB
|
B:SER432
|
3.8
|
20.2
|
1.0
|
CB
|
F:DMH563
|
3.9
|
25.3
|
1.0
|
CE1
|
B:HIS363
|
4.1
|
16.4
|
1.0
|
CA
|
F:DMH563
|
4.2
|
27.3
|
1.0
|
CG
|
B:HIS363
|
4.3
|
18.2
|
1.0
|
CB
|
F:ALA564
|
4.5
|
25.9
|
1.0
|
ND2
|
B:ASN362
|
4.7
|
24.5
|
1.0
|
ND1
|
B:HIS363
|
4.8
|
17.6
|
1.0
|
NE
|
B:ARG465
|
4.9
|
22.3
|
1.0
|
|
Fluorine binding site 7 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 7 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F1265
b:26.2
occ:1.00
|
FB1
|
G:CFT1265
|
0.0
|
26.2
|
1.0
|
C1
|
G:CFT1265
|
1.3
|
27.2
|
1.0
|
FB2
|
G:CFT1265
|
2.1
|
28.6
|
1.0
|
FB3
|
G:CFT1265
|
2.1
|
27.2
|
1.0
|
C
|
G:ALA1264
|
2.4
|
26.4
|
1.0
|
O
|
G:ALA1264
|
2.9
|
26.3
|
1.0
|
CA
|
G:ALA1264
|
3.0
|
27.4
|
1.0
|
CG
|
C:ARG1165
|
3.1
|
26.7
|
1.0
|
NE
|
C:ARG1165
|
3.5
|
32.7
|
1.0
|
O
|
G:DMH1263
|
3.6
|
30.3
|
1.0
|
CB
|
C:ARG1165
|
3.6
|
24.7
|
1.0
|
OG
|
C:SER1132
|
3.6
|
25.1
|
1.0
|
CD
|
C:ARG1165
|
3.8
|
29.6
|
1.0
|
N
|
C:ARG1165
|
3.8
|
22.5
|
1.0
|
N
|
G:ALA1264
|
3.8
|
28.7
|
1.0
|
C
|
G:DMH1263
|
4.1
|
30.0
|
1.0
|
CB
|
G:ALA1264
|
4.2
|
27.3
|
1.0
|
CA
|
C:ARG1165
|
4.3
|
23.1
|
1.0
|
CB
|
C:SER1132
|
4.4
|
22.4
|
1.0
|
C
|
C:GLY1164
|
4.6
|
21.2
|
1.0
|
CZ
|
C:ARG1165
|
4.7
|
34.3
|
1.0
|
NE2
|
C:HIS1063
|
4.8
|
21.4
|
1.0
|
CA
|
C:GLY1164
|
4.8
|
20.2
|
1.0
|
O
|
C:VAL1163
|
4.9
|
15.6
|
1.0
|
|
Fluorine binding site 8 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 8 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 8 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F1265
b:28.6
occ:1.00
|
FB2
|
G:CFT1265
|
0.0
|
28.6
|
1.0
|
C1
|
G:CFT1265
|
1.3
|
27.2
|
1.0
|
FB3
|
G:CFT1265
|
2.1
|
27.2
|
1.0
|
FB1
|
G:CFT1265
|
2.1
|
26.2
|
1.0
|
C
|
G:ALA1264
|
2.4
|
26.4
|
1.0
|
O
|
G:ALA1264
|
2.8
|
26.3
|
1.0
|
OG
|
C:SER1132
|
2.9
|
25.1
|
1.0
|
CB
|
C:SER1132
|
3.1
|
22.4
|
1.0
|
CA
|
G:ALA1264
|
3.8
|
27.4
|
1.0
|
SG
|
C:CYS1161
|
3.8
|
25.9
|
1.0
|
NE2
|
C:HIS1063
|
3.8
|
21.4
|
1.0
|
CD2
|
C:HIS1063
|
4.1
|
20.0
|
1.0
|
O
|
C:VAL1163
|
4.1
|
15.6
|
1.0
|
CB
|
C:CYS1161
|
4.3
|
20.5
|
1.0
|
OD1
|
C:ASN1062
|
4.3
|
24.1
|
1.0
|
N
|
G:ALA1264
|
4.4
|
28.7
|
1.0
|
CA
|
C:GLY1164
|
4.5
|
20.2
|
1.0
|
N
|
C:ARG1165
|
4.5
|
22.5
|
1.0
|
CA
|
C:SER1132
|
4.6
|
21.0
|
1.0
|
O
|
G:DMH1263
|
4.9
|
30.3
|
1.0
|
CB
|
G:ALA1264
|
4.9
|
27.3
|
1.0
|
C
|
G:DMH1263
|
4.9
|
30.0
|
1.0
|
C
|
C:GLY1164
|
4.9
|
21.2
|
1.0
|
|
Fluorine binding site 9 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 9 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 9 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
G:F1265
b:27.2
occ:1.00
|
FB3
|
G:CFT1265
|
0.0
|
27.2
|
1.0
|
C1
|
G:CFT1265
|
1.3
|
27.2
|
1.0
|
FB2
|
G:CFT1265
|
2.1
|
28.6
|
1.0
|
FB1
|
G:CFT1265
|
2.1
|
26.2
|
1.0
|
C
|
G:ALA1264
|
2.4
|
26.4
|
1.0
|
NE2
|
C:HIS1063
|
2.8
|
21.4
|
1.0
|
OG
|
C:SER1132
|
2.8
|
25.1
|
1.0
|
CA
|
G:ALA1264
|
3.0
|
27.4
|
1.0
|
N
|
G:ALA1264
|
3.0
|
28.7
|
1.0
|
O
|
G:DMH1263
|
3.0
|
30.3
|
1.0
|
C
|
G:DMH1263
|
3.1
|
30.0
|
1.0
|
CD2
|
C:HIS1063
|
3.1
|
20.0
|
1.0
|
O
|
G:ALA1264
|
3.6
|
26.3
|
1.0
|
CB
|
C:SER1132
|
3.8
|
22.4
|
1.0
|
CB
|
G:DMH1263
|
3.9
|
30.3
|
1.0
|
CE1
|
C:HIS1063
|
4.0
|
21.1
|
1.0
|
CA
|
G:DMH1263
|
4.1
|
30.9
|
1.0
|
CG
|
C:HIS1063
|
4.3
|
20.9
|
1.0
|
CB
|
G:ALA1264
|
4.4
|
27.3
|
1.0
|
ND1
|
C:HIS1063
|
4.7
|
21.6
|
1.0
|
NE
|
C:ARG1165
|
4.8
|
32.7
|
1.0
|
|
Fluorine binding site 10 out
of 12 in 1njt
Go back to
Fluorine Binding Sites List in 1njt
Fluorine binding site 10 out
of 12 in the Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor
Mono view
Stereo pair view
|
A full contact list of Fluorine with other atoms in the F binding
site number 10 of Complex Structure of Hcmv Protease and A Peptidomimetic Inhibitor within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
H:F1565
b:23.3
occ:1.00
|
FB1
|
H:CFT1565
|
0.0
|
23.3
|
1.0
|
C1
|
H:CFT1565
|
1.3
|
24.8
|
1.0
|
FB3
|
H:CFT1565
|
2.1
|
23.0
|
1.0
|
FB2
|
H:CFT1565
|
2.1
|
26.2
|
1.0
|
C
|
H:ALA1564
|
2.5
|
25.2
|
1.0
|
O
|
H:ALA1564
|
3.0
|
23.7
|
1.0
|
CA
|
H:ALA1564
|
3.0
|
26.6
|
1.0
|
CG
|
D:ARG1465
|
3.2
|
25.5
|
1.0
|
O
|
H:DMH1563
|
3.5
|
29.9
|
1.0
|
NE
|
D:ARG1465
|
3.6
|
29.6
|
1.0
|
OG
|
D:SER1432
|
3.7
|
23.2
|
1.0
|
CB
|
D:ARG1465
|
3.7
|
24.0
|
1.0
|
N
|
H:ALA1564
|
3.8
|
28.7
|
1.0
|
CD
|
D:ARG1465
|
3.9
|
27.0
|
1.0
|
N
|
D:ARG1465
|
4.0
|
22.2
|
1.0
|
C
|
H:DMH1563
|
4.0
|
29.9
|
1.0
|
CB
|
H:ALA1564
|
4.3
|
27.3
|
1.0
|
CA
|
D:ARG1465
|
4.4
|
23.8
|
1.0
|
CB
|
D:SER1432
|
4.5
|
21.1
|
1.0
|
NE2
|
D:HIS1363
|
4.7
|
20.2
|
1.0
|
CZ
|
D:ARG1465
|
4.8
|
31.1
|
1.0
|
C
|
D:GLY1464
|
4.8
|
20.2
|
1.0
|
O
|
D:VAL1463
|
5.0
|
20.6
|
1.0
|
|
Reference:
R.Khayat,
R.Batra,
C.Qian,
T.Halmos,
M.Bailey,
L.Tong.
Structural and Biochemical Studies of Inhibitor Binding to Human Cytomegalovirus Protease Biochemistry V. 42 885 2003.
ISSN: ISSN 0006-2960
PubMed: 12549906
DOI: 10.1021/BI027045S
Page generated: Wed Jul 31 12:08:18 2024
|