Fluorine in PDB 8vrg: E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
Enzymatic activity of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
All present enzymatic activity of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines:
5.2.1.8;
Protein crystallography data
The structure of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines, PDB code: 8vrg
was solved by
R.L.Frkic,
C.J.Jackson,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
40.75 /
1.22
|
|
Space group
|
P 1 21 1
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
34.691,
50.675,
40.767,
90,
91.53,
90
|
|
R / Rfree (%)
|
16.2 /
19.1
|
Fluorine Binding Sites:
The binding sites of Fluorine atom in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
(pdb code 8vrg). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total 7 binding sites of Fluorine where determined in the
E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines, PDB code: 8vrg:
Jump to Fluorine binding site number:
1;
2;
3;
4;
5;
6;
7;
Fluorine binding site 1 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 1 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 1 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F28
b:24.1
occ:0.60
|
F1
|
A:LEF28
|
0.0
|
24.1
|
0.6
|
|
HD12
|
A:LEF28
|
1.1
|
26.7
|
0.4
|
|
CD1
|
A:LEF28
|
1.4
|
20.8
|
0.6
|
|
CD1
|
A:LEF28
|
1.9
|
22.3
|
0.4
|
|
HD12
|
A:LEF28
|
2.0
|
25.0
|
0.6
|
|
HD13
|
A:LEF28
|
2.0
|
25.0
|
0.6
|
|
HD21
|
A:LEF28
|
2.2
|
23.6
|
0.4
|
|
HD21
|
A:LEF28
|
2.3
|
22.1
|
0.6
|
|
HG
|
A:LEF28
|
2.3
|
21.1
|
0.4
|
|
CG
|
A:LEF28
|
2.4
|
17.6
|
0.4
|
|
CG
|
A:LEF28
|
2.4
|
16.3
|
0.6
|
|
F1
|
A:LEF28
|
2.7
|
22.3
|
0.4
|
|
CD2
|
A:LEF28
|
2.7
|
19.7
|
0.4
|
|
HG
|
A:LEF28
|
2.7
|
19.5
|
0.6
|
|
HD13
|
A:LEF28
|
2.8
|
26.7
|
0.4
|
|
CD2
|
A:LEF28
|
2.8
|
18.4
|
0.6
|
|
O
|
A:HOH338
|
2.9
|
28.8
|
1.0
|
|
HG13
|
A:VAL24
|
2.9
|
21.1
|
1.0
|
|
HG12
|
A:VAL24
|
3.1
|
21.1
|
1.0
|
|
HD23
|
A:LEF28
|
3.2
|
23.6
|
0.4
|
|
CG1
|
A:VAL24
|
3.3
|
17.6
|
1.0
|
|
HG11
|
A:VAL24
|
3.4
|
21.1
|
1.0
|
|
HG21
|
A:THR15
|
3.5
|
23.5
|
1.0
|
|
HD23
|
A:LEF28
|
3.5
|
22.1
|
0.6
|
|
HD22
|
A:LEF28
|
3.6
|
23.6
|
0.4
|
|
HD22
|
A:LEF28
|
3.6
|
22.1
|
0.6
|
|
CB
|
A:LEF28
|
3.7
|
20.2
|
0.6
|
|
OG1
|
A:THR15
|
3.7
|
22.2
|
1.0
|
|
CB
|
A:LEF28
|
3.8
|
18.1
|
0.4
|
|
HB2
|
A:LEF28
|
3.9
|
24.3
|
0.6
|
|
HB3
|
A:LEF28
|
3.9
|
24.3
|
0.6
|
|
OD2
|
A:ASP17
|
4.1
|
43.9
|
1.0
|
|
HB3
|
A:LEF28
|
4.1
|
21.7
|
0.4
|
|
HG1
|
A:THR15
|
4.2
|
26.6
|
1.0
|
|
CG2
|
A:THR15
|
4.3
|
19.6
|
1.0
|
|
HB2
|
A:LEF28
|
4.3
|
21.7
|
0.4
|
|
O
|
A:HOH380
|
4.3
|
35.8
|
1.0
|
|
OD1
|
A:ASP17
|
4.3
|
42.2
|
1.0
|
|
HB
|
A:THR15
|
4.4
|
22.8
|
1.0
|
|
CB
|
A:THR15
|
4.4
|
19.0
|
1.0
|
|
O
|
A:VAL24
|
4.4
|
16.7
|
1.0
|
|
HG23
|
A:THR15
|
4.6
|
23.5
|
1.0
|
|
CG
|
A:ASP17
|
4.6
|
38.8
|
1.0
|
|
HG23
|
A:VAL2
|
4.7
|
39.4
|
1.0
|
|
HD2
|
A:PHE27
|
4.7
|
20.5
|
1.0
|
|
HA
|
A:LEF28
|
4.8
|
20.8
|
0.4
|
|
CB
|
A:VAL24
|
4.8
|
16.7
|
1.0
|
|
CA
|
A:LEF28
|
4.9
|
17.4
|
0.4
|
|
O
|
A:HOH412
|
4.9
|
32.5
|
1.0
|
|
HG11
|
A:VAL162
|
4.9
|
38.1
|
1.0
|
|
CA
|
A:LEF28
|
4.9
|
17.2
|
0.6
|
|
C
|
A:VAL24
|
4.9
|
17.0
|
1.0
|
|
HG21
|
A:VAL2
|
5.0
|
39.4
|
1.0
|
|
Fluorine binding site 2 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 2 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 2 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F28
b:22.3
occ:0.40
|
F1
|
A:LEF28
|
0.0
|
22.3
|
0.4
|
|
HD13
|
A:LEF28
|
0.8
|
25.0
|
0.6
|
|
CD1
|
A:LEF28
|
1.4
|
22.3
|
0.4
|
|
CD1
|
A:LEF28
|
1.7
|
20.8
|
0.6
|
|
HD12
|
A:LEF28
|
2.0
|
25.0
|
0.6
|
|
HD13
|
A:LEF28
|
2.0
|
26.7
|
0.4
|
|
HD12
|
A:LEF28
|
2.0
|
26.7
|
0.4
|
|
CG
|
A:LEF28
|
2.4
|
17.6
|
0.4
|
|
HB3
|
A:LEF28
|
2.4
|
24.3
|
0.6
|
|
O
|
A:HOH412
|
2.4
|
32.5
|
1.0
|
|
HB3
|
A:LEF28
|
2.5
|
21.7
|
0.4
|
|
O
|
A:HOH380
|
2.6
|
35.8
|
1.0
|
|
HG
|
A:LEF28
|
2.6
|
21.1
|
0.4
|
|
F1
|
A:LEF28
|
2.7
|
24.1
|
0.6
|
|
CG
|
A:LEF28
|
2.7
|
16.3
|
0.6
|
|
HG12
|
A:VAL24
|
2.8
|
21.1
|
1.0
|
|
CB
|
A:LEF28
|
2.9
|
18.1
|
0.4
|
|
CB
|
A:LEF28
|
2.9
|
20.2
|
0.6
|
|
HA
|
A:LYS25
|
3.0
|
20.2
|
0.7
|
|
HA
|
A:LYS25
|
3.0
|
20.3
|
0.3
|
|
HG
|
A:LEF28
|
3.1
|
19.5
|
0.6
|
|
HB2
|
A:LEF28
|
3.2
|
21.7
|
0.4
|
|
HB2
|
A:LEF28
|
3.2
|
24.3
|
0.6
|
|
O
|
A:VAL24
|
3.4
|
16.7
|
1.0
|
|
HG13
|
A:VAL24
|
3.6
|
21.1
|
1.0
|
|
CG1
|
A:VAL24
|
3.6
|
17.6
|
1.0
|
|
CD2
|
A:LEF28
|
3.7
|
19.7
|
0.4
|
|
HD21
|
A:LEF28
|
3.8
|
23.6
|
0.4
|
|
CA
|
A:LYS25
|
3.8
|
16.9
|
0.7
|
|
CA
|
A:LYS25
|
3.8
|
16.9
|
0.3
|
|
C
|
A:VAL24
|
3.8
|
17.0
|
1.0
|
|
O
|
A:HOH258
|
4.0
|
33.0
|
1.0
|
|
N
|
A:LYS25
|
4.0
|
17.3
|
0.3
|
|
N
|
A:LYS25
|
4.0
|
17.3
|
0.7
|
|
HG11
|
A:VAL24
|
4.1
|
21.1
|
1.0
|
|
CD2
|
A:LEF28
|
4.1
|
18.4
|
0.6
|
|
HD22
|
A:LEF28
|
4.2
|
23.6
|
0.4
|
|
HD21
|
A:LEF28
|
4.2
|
22.1
|
0.6
|
|
HG3
|
A:LYS25
|
4.2
|
22.3
|
0.3
|
|
CA
|
A:LEF28
|
4.3
|
17.4
|
0.4
|
|
CA
|
A:LEF28
|
4.3
|
17.2
|
0.6
|
|
O
|
A:HOH375
|
4.4
|
29.6
|
1.0
|
|
HD23
|
A:LEF28
|
4.4
|
23.6
|
0.4
|
|
OD2
|
A:ASP17
|
4.5
|
43.9
|
1.0
|
|
HD22
|
A:LEF28
|
4.5
|
22.1
|
0.6
|
|
HG2
|
A:LYS25
|
4.5
|
22.3
|
0.3
|
|
H
|
A:LEF28
|
4.6
|
19.0
|
0.6
|
|
H
|
A:LEF28
|
4.6
|
18.9
|
0.4
|
|
H
|
A:LYS25
|
4.6
|
20.8
|
0.3
|
|
HB2
|
A:LYS25
|
4.6
|
23.4
|
0.7
|
|
H
|
A:LYS25
|
4.6
|
20.8
|
0.7
|
|
O
|
A:LYS25
|
4.6
|
16.8
|
0.3
|
|
N
|
A:LEF28
|
4.6
|
15.8
|
0.4
|
|
N
|
A:LEF28
|
4.6
|
15.8
|
0.6
|
|
O
|
A:LYS25
|
4.7
|
16.9
|
0.7
|
|
C
|
A:LYS25
|
4.7
|
17.4
|
0.3
|
|
C
|
A:LYS25
|
4.7
|
17.4
|
0.7
|
|
CB
|
A:VAL24
|
4.7
|
16.7
|
1.0
|
|
CG
|
A:LYS25
|
4.7
|
18.6
|
0.3
|
|
HA
|
A:LEF28
|
4.7
|
20.8
|
0.4
|
|
O
|
A:HOH298
|
4.8
|
32.7
|
1.0
|
|
CB
|
A:LYS25
|
4.8
|
19.5
|
0.7
|
|
HD23
|
A:LEF28
|
4.8
|
22.1
|
0.6
|
|
CB
|
A:LYS25
|
4.8
|
19.4
|
0.3
|
|
HB
|
A:VAL24
|
4.8
|
20.0
|
1.0
|
|
CA
|
A:VAL24
|
4.8
|
14.4
|
1.0
|
|
HG3
|
A:LYS25
|
4.9
|
28.8
|
0.7
|
|
HA
|
A:LEF28
|
5.0
|
20.7
|
0.6
|
|
Fluorine binding site 3 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 3 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 3 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F76
b:23.7
occ:1.00
|
F1
|
A:LEF76
|
0.0
|
23.7
|
1.0
|
|
CD1
|
A:LEF76
|
1.4
|
19.0
|
1.0
|
|
HD13
|
A:LEF76
|
2.0
|
22.8
|
1.0
|
|
HD12
|
A:LEF76
|
2.0
|
22.8
|
1.0
|
|
CG
|
A:LEF76
|
2.4
|
17.5
|
1.0
|
|
HD23
|
A:LEF76
|
2.4
|
32.8
|
1.0
|
|
HB2
|
A:LYS19
|
2.6
|
29.6
|
1.0
|
|
HG
|
A:LEF76
|
2.6
|
21.0
|
1.0
|
|
CD2
|
A:LEF76
|
2.9
|
27.3
|
1.0
|
|
HB3
|
A:PHE16
|
2.9
|
24.6
|
1.0
|
|
HB3
|
A:LYS19
|
2.9
|
29.6
|
1.0
|
|
HG3
|
A:LYS19
|
3.0
|
44.4
|
1.0
|
|
CB
|
A:LYS19
|
3.1
|
24.7
|
1.0
|
|
HD1
|
A:PHE16
|
3.1
|
22.9
|
1.0
|
|
CD1
|
A:PHE16
|
3.3
|
19.0
|
1.0
|
|
HB2
|
A:PHE16
|
3.4
|
24.6
|
1.0
|
|
CB
|
A:PHE16
|
3.4
|
20.5
|
1.0
|
|
HD21
|
A:LEF76
|
3.4
|
32.8
|
1.0
|
|
CG
|
A:PHE16
|
3.4
|
23.3
|
1.0
|
|
CG
|
A:LYS19
|
3.5
|
37.0
|
1.0
|
|
CB
|
A:LEF76
|
3.7
|
16.3
|
1.0
|
|
HD22
|
A:LEF76
|
3.8
|
32.8
|
1.0
|
|
HB3
|
A:LEF76
|
3.9
|
19.6
|
1.0
|
|
HB2
|
A:LEF76
|
3.9
|
19.6
|
1.0
|
|
HZ3
|
A:LYS19
|
3.9
|
65.6
|
1.0
|
|
CE1
|
A:PHE16
|
4.1
|
19.4
|
1.0
|
|
HD21
|
A:ASN74
|
4.2
|
17.6
|
1.0
|
|
HG2
|
A:LYS19
|
4.2
|
44.4
|
1.0
|
|
HG12
|
A:VAL122
|
4.2
|
16.1
|
1.0
|
|
ND2
|
A:ASN74
|
4.3
|
14.7
|
1.0
|
|
CD2
|
A:PHE16
|
4.4
|
38.5
|
1.0
|
|
HD22
|
A:ASN74
|
4.4
|
17.6
|
1.0
|
|
HE1
|
A:PHE16
|
4.4
|
23.3
|
1.0
|
|
HD2
|
A:LYS19
|
4.4
|
51.9
|
1.0
|
|
CA
|
A:LYS19
|
4.5
|
21.6
|
1.0
|
|
O
|
A:VAL122
|
4.5
|
14.3
|
1.0
|
|
CD
|
A:LYS19
|
4.5
|
43.2
|
1.0
|
|
O
|
A:HOH374
|
4.6
|
29.3
|
1.0
|
|
NZ
|
A:LYS19
|
4.7
|
54.7
|
1.0
|
|
CG
|
A:ASN74
|
4.7
|
14.2
|
1.0
|
|
H
|
A:LYS19
|
4.7
|
29.8
|
1.0
|
|
HE2
|
A:LYS19
|
4.8
|
72.6
|
1.0
|
|
C
|
A:LYS19
|
4.8
|
20.5
|
1.0
|
|
HA
|
A:PHE123
|
4.8
|
14.1
|
1.0
|
|
HD2
|
A:PHE16
|
4.8
|
46.2
|
1.0
|
|
HB2
|
A:ASN74
|
4.8
|
19.3
|
1.0
|
|
CA
|
A:PHE16
|
4.9
|
19.1
|
1.0
|
|
HB2
|
A:ALA20
|
4.9
|
18.2
|
1.0
|
|
CZ
|
A:PHE16
|
4.9
|
28.9
|
1.0
|
|
CA
|
A:LEF76
|
4.9
|
13.6
|
1.0
|
|
CE
|
A:LYS19
|
4.9
|
60.5
|
1.0
|
|
HA
|
A:LEF76
|
5.0
|
16.3
|
1.0
|
|
Fluorine binding site 4 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 4 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 4 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F83
b:15.0
occ:1.00
|
F1
|
A:LEF83
|
0.0
|
15.0
|
1.0
|
|
CD1
|
A:LEF83
|
1.4
|
12.0
|
1.0
|
|
HD12
|
A:LEF83
|
2.0
|
14.4
|
1.0
|
|
HD13
|
A:LEF83
|
2.0
|
14.4
|
1.0
|
|
CG
|
A:LEF83
|
2.4
|
12.0
|
1.0
|
|
HB3
|
A:LEF83
|
2.6
|
13.4
|
1.0
|
|
HD23
|
A:LEF83
|
2.6
|
15.7
|
1.0
|
|
HB3
|
A:ALA124
|
2.9
|
18.5
|
1.0
|
|
HG12
|
A:ILE13
|
2.9
|
25.6
|
1.0
|
|
CD2
|
A:LEF83
|
2.9
|
13.1
|
1.0
|
|
CB
|
A:LEF83
|
2.9
|
11.2
|
1.0
|
|
HA
|
A:GLU125
|
2.9
|
17.6
|
1.0
|
|
HG23
|
A:ILE13
|
3.2
|
26.5
|
1.0
|
|
N
|
A:GLU125
|
3.3
|
14.9
|
1.0
|
|
HG
|
A:LEF83
|
3.3
|
14.4
|
1.0
|
|
HD22
|
A:LEF83
|
3.3
|
15.7
|
1.0
|
|
C
|
A:GLU125
|
3.3
|
13.9
|
1.0
|
|
CA
|
A:GLU125
|
3.3
|
14.6
|
1.0
|
|
HG23
|
A:VAL126
|
3.3
|
18.1
|
1.0
|
|
HG21
|
A:ILE13
|
3.4
|
26.5
|
1.0
|
|
C
|
A:ALA124
|
3.4
|
12.4
|
1.0
|
|
N
|
A:LEF83
|
3.4
|
10.6
|
1.0
|
|
N
|
A:VAL126
|
3.5
|
15.7
|
1.0
|
|
O
|
A:ALA124
|
3.6
|
12.5
|
1.0
|
|
H
|
A:VAL126
|
3.6
|
18.8
|
1.0
|
|
CB
|
A:ALA124
|
3.6
|
15.4
|
1.0
|
|
H
|
A:GLU125
|
3.6
|
17.9
|
1.0
|
|
HB1
|
A:ALA124
|
3.6
|
18.5
|
1.0
|
|
CG2
|
A:ILE13
|
3.7
|
22.1
|
1.0
|
|
CA
|
A:LEF83
|
3.7
|
10.0
|
1.0
|
|
HG22
|
A:VAL126
|
3.7
|
18.1
|
1.0
|
|
CG1
|
A:ILE13
|
3.8
|
21.3
|
1.0
|
|
O
|
A:GLU125
|
3.8
|
15.7
|
1.0
|
|
HB2
|
A:LEF83
|
3.9
|
13.4
|
1.0
|
|
HD21
|
A:LEF83
|
3.9
|
15.7
|
1.0
|
|
CG2
|
A:VAL126
|
4.0
|
15.0
|
1.0
|
|
O
|
A:GLY81
|
4.0
|
14.9
|
1.0
|
|
H
|
A:LEF83
|
4.0
|
12.7
|
1.0
|
|
HA
|
A:LEF83
|
4.1
|
12.0
|
1.0
|
|
CA
|
A:ALA124
|
4.1
|
13.4
|
1.0
|
|
HA
|
A:THR82
|
4.1
|
14.2
|
1.0
|
|
C
|
A:THR82
|
4.2
|
10.5
|
1.0
|
|
HA
|
A:VAL126
|
4.2
|
16.7
|
1.0
|
|
HG12
|
A:ILE100
|
4.2
|
14.2
|
1.0
|
|
CB
|
A:ILE13
|
4.3
|
17.4
|
1.0
|
|
HD13
|
A:ILE13
|
4.3
|
27.9
|
1.0
|
|
HG13
|
A:ILE13
|
4.3
|
25.6
|
1.0
|
|
CA
|
A:VAL126
|
4.4
|
13.9
|
1.0
|
|
HA
|
A:ILE13
|
4.4
|
20.4
|
1.0
|
|
HB2
|
A:ALA124
|
4.4
|
18.5
|
1.0
|
|
HG22
|
A:ILE13
|
4.5
|
26.5
|
1.0
|
|
CD1
|
A:ILE13
|
4.6
|
23.3
|
1.0
|
|
HG21
|
A:VAL126
|
4.7
|
18.1
|
1.0
|
|
CA
|
A:THR82
|
4.7
|
11.8
|
1.0
|
|
H
|
A:ALA124
|
4.8
|
16.2
|
1.0
|
|
HD11
|
A:ILE13
|
4.8
|
27.9
|
1.0
|
|
CB
|
A:VAL126
|
4.8
|
15.5
|
1.0
|
|
CB
|
A:GLU125
|
4.8
|
22.0
|
1.0
|
|
O
|
A:THR82
|
4.8
|
11.4
|
1.0
|
|
HA
|
A:ALA124
|
4.9
|
16.1
|
1.0
|
|
HG23
|
A:ILE100
|
4.9
|
15.0
|
1.0
|
|
CA
|
A:ILE13
|
4.9
|
16.9
|
1.0
|
|
N
|
A:ALA124
|
4.9
|
13.5
|
1.0
|
|
C
|
A:LEF83
|
4.9
|
9.7
|
1.0
|
|
Fluorine binding site 5 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 5 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 5 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F108
b:12.6
occ:0.61
|
F1
|
A:LEF108
|
0.0
|
12.6
|
0.6
|
|
F1
|
A:LEF108
|
1.1
|
11.0
|
0.4
|
|
CD1
|
A:LEF108
|
1.4
|
9.6
|
0.6
|
|
HD12
|
A:LEF108
|
1.4
|
11.7
|
0.4
|
|
CD1
|
A:LEF108
|
1.5
|
9.7
|
0.4
|
|
HD13
|
A:LEF108
|
2.0
|
11.5
|
0.6
|
|
HD12
|
A:LEF108
|
2.0
|
11.5
|
0.6
|
|
HE1
|
A:PHE48
|
2.3
|
13.1
|
1.0
|
|
HD13
|
A:LEF108
|
2.4
|
11.7
|
0.4
|
|
CG
|
A:LEF108
|
2.4
|
11.2
|
0.6
|
|
HD23
|
A:LEF108
|
2.5
|
13.4
|
0.6
|
|
CG
|
A:LEF108
|
2.6
|
8.5
|
0.4
|
|
HG
|
A:LEF108
|
2.6
|
10.2
|
0.4
|
|
HG
|
A:LEF108
|
2.6
|
13.4
|
0.6
|
|
CD2
|
A:LEF108
|
2.9
|
11.2
|
0.6
|
|
CE1
|
A:PHE48
|
3.0
|
10.9
|
1.0
|
|
HB3
|
A:ASN105
|
3.1
|
14.8
|
1.0
|
|
HE2
|
A:PHE99
|
3.2
|
11.6
|
1.0
|
|
HD23
|
A:LEF108
|
3.3
|
11.2
|
0.4
|
|
HD22
|
A:ASN105
|
3.3
|
12.8
|
1.0
|
|
HZ
|
A:PHE48
|
3.4
|
13.3
|
1.0
|
|
HB2
|
A:ASN105
|
3.4
|
14.8
|
1.0
|
|
CD2
|
A:LEF108
|
3.5
|
9.3
|
0.4
|
|
CZ
|
A:PHE48
|
3.5
|
11.1
|
1.0
|
|
CB
|
A:ASN105
|
3.6
|
12.4
|
1.0
|
|
HD22
|
A:LEF108
|
3.6
|
13.4
|
0.6
|
|
OD1
|
A:ASN101
|
3.6
|
10.5
|
1.0
|
|
HB2
|
A:LEF108
|
3.6
|
12.2
|
0.4
|
|
ND2
|
A:ASN105
|
3.6
|
10.7
|
1.0
|
|
CB
|
A:LEF108
|
3.7
|
10.2
|
0.4
|
|
CE2
|
A:PHE99
|
3.7
|
9.6
|
1.0
|
|
CB
|
A:LEF108
|
3.7
|
9.9
|
0.6
|
|
HD21
|
A:LEF108
|
3.7
|
13.4
|
0.6
|
|
HG2
|
A:MET49
|
3.7
|
11.0
|
1.0
|
|
HE1
|
A:PHE107
|
3.7
|
13.7
|
1.0
|
|
CG
|
A:ASN105
|
3.8
|
9.7
|
1.0
|
|
HB3
|
A:LEF108
|
4.0
|
12.2
|
0.4
|
|
HB2
|
A:LEF108
|
4.0
|
11.8
|
0.6
|
|
HB3
|
A:LEF108
|
4.0
|
11.8
|
0.6
|
|
CD1
|
A:PHE48
|
4.0
|
10.3
|
1.0
|
|
HZ
|
A:PHE99
|
4.0
|
11.9
|
1.0
|
|
HD21
|
A:LEF108
|
4.1
|
11.2
|
0.4
|
|
HD1
|
A:PHE48
|
4.1
|
12.4
|
1.0
|
|
HD21
|
A:ASN105
|
4.2
|
12.8
|
1.0
|
|
CZ
|
A:PHE99
|
4.2
|
9.9
|
1.0
|
|
CE1
|
A:PHE107
|
4.2
|
11.4
|
1.0
|
|
HD22
|
A:LEF108
|
4.4
|
11.2
|
0.4
|
|
HB3
|
A:MET49
|
4.4
|
10.5
|
1.0
|
|
H
|
A:LEF108
|
4.4
|
11.8
|
0.4
|
|
HZ
|
A:PHE107
|
4.4
|
14.7
|
1.0
|
|
CD2
|
A:PHE99
|
4.5
|
8.9
|
1.0
|
|
CG
|
A:MET49
|
4.6
|
9.2
|
1.0
|
|
CZ
|
A:PHE107
|
4.6
|
12.3
|
1.0
|
|
HD2
|
A:PHE99
|
4.6
|
10.7
|
1.0
|
|
OD1
|
A:ASN105
|
4.7
|
10.8
|
1.0
|
|
CE2
|
A:PHE48
|
4.8
|
11.1
|
1.0
|
|
CG
|
A:ASN101
|
4.8
|
9.0
|
1.0
|
|
HG3
|
A:MET49
|
4.8
|
11.0
|
1.0
|
|
HB3
|
A:ASN78
|
4.8
|
12.0
|
1.0
|
|
O
|
A:ASN105
|
4.9
|
11.3
|
1.0
|
|
CA
|
A:LEF108
|
5.0
|
9.8
|
0.6
|
|
Fluorine binding site 6 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 6 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 6 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F108
b:11.0
occ:0.39
|
F1
|
A:LEF108
|
0.0
|
11.0
|
0.4
|
|
F1
|
A:LEF108
|
1.1
|
12.6
|
0.6
|
|
CD1
|
A:LEF108
|
1.4
|
9.7
|
0.4
|
|
HD23
|
A:LEF108
|
1.6
|
13.4
|
0.6
|
|
CD1
|
A:LEF108
|
1.9
|
9.6
|
0.6
|
|
HD13
|
A:LEF108
|
2.0
|
11.7
|
0.4
|
|
HD12
|
A:LEF108
|
2.0
|
11.7
|
0.4
|
|
HD12
|
A:LEF108
|
2.2
|
11.5
|
0.6
|
|
CD2
|
A:LEF108
|
2.3
|
11.2
|
0.6
|
|
CG
|
A:LEF108
|
2.4
|
8.5
|
0.4
|
|
HE1
|
A:PHE48
|
2.4
|
13.1
|
1.0
|
|
HD23
|
A:LEF108
|
2.4
|
11.2
|
0.4
|
|
CG
|
A:LEF108
|
2.5
|
11.2
|
0.6
|
|
HZ
|
A:PHE48
|
2.7
|
13.3
|
1.0
|
|
HG
|
A:LEF108
|
2.7
|
10.2
|
0.4
|
|
HD13
|
A:LEF108
|
2.8
|
11.5
|
0.6
|
|
HG
|
A:LEF108
|
2.8
|
13.4
|
0.6
|
|
CD2
|
A:LEF108
|
2.9
|
9.3
|
0.4
|
|
CE1
|
A:PHE48
|
3.0
|
10.9
|
1.0
|
|
HD22
|
A:LEF108
|
3.0
|
13.4
|
0.6
|
|
CZ
|
A:PHE48
|
3.1
|
11.1
|
1.0
|
|
HD21
|
A:LEF108
|
3.1
|
13.4
|
0.6
|
|
HD21
|
A:LEF108
|
3.3
|
11.2
|
0.4
|
|
HE1
|
A:PHE107
|
3.4
|
13.7
|
1.0
|
|
CB
|
A:LEF108
|
3.7
|
10.2
|
0.4
|
|
HE2
|
A:PHE99
|
3.8
|
11.6
|
1.0
|
|
HD22
|
A:LEF108
|
3.8
|
11.2
|
0.4
|
|
HB3
|
A:ASN105
|
3.8
|
14.8
|
1.0
|
|
CB
|
A:LEF108
|
3.9
|
9.9
|
0.6
|
|
HG2
|
A:MET49
|
3.9
|
11.0
|
1.0
|
|
HB3
|
A:LEF108
|
3.9
|
12.2
|
0.4
|
|
HB2
|
A:LEF108
|
4.0
|
12.2
|
0.4
|
|
HB3
|
A:LEF108
|
4.0
|
11.8
|
0.6
|
|
CE1
|
A:PHE107
|
4.0
|
11.4
|
1.0
|
|
CE2
|
A:PHE99
|
4.1
|
9.6
|
1.0
|
|
HZ
|
A:PHE99
|
4.1
|
11.9
|
1.0
|
|
CD1
|
A:PHE48
|
4.2
|
10.3
|
1.0
|
|
CZ
|
A:PHE99
|
4.2
|
9.9
|
1.0
|
|
HB2
|
A:LEF108
|
4.4
|
11.8
|
0.6
|
|
CE2
|
A:PHE48
|
4.4
|
11.1
|
1.0
|
|
HD22
|
A:ASN105
|
4.4
|
12.8
|
1.0
|
|
HB2
|
A:ASN105
|
4.4
|
14.8
|
1.0
|
|
CB
|
A:ASN105
|
4.5
|
12.4
|
1.0
|
|
H
|
A:LEF108
|
4.5
|
11.8
|
0.4
|
|
HD1
|
A:PHE48
|
4.5
|
12.4
|
1.0
|
|
HZ
|
A:PHE107
|
4.6
|
14.7
|
1.0
|
|
ND2
|
A:ASN105
|
4.6
|
10.7
|
1.0
|
|
OD1
|
A:ASN101
|
4.7
|
10.5
|
1.0
|
|
CZ
|
A:PHE107
|
4.7
|
12.3
|
1.0
|
|
HD1
|
A:PHE107
|
4.7
|
13.7
|
1.0
|
|
CG
|
A:ASN105
|
4.7
|
9.7
|
1.0
|
|
CD1
|
A:PHE107
|
4.8
|
11.4
|
1.0
|
|
CG
|
A:MET49
|
4.8
|
9.2
|
1.0
|
|
HE2
|
A:PHE48
|
4.8
|
13.3
|
1.0
|
|
HA
|
A:LEF108
|
4.8
|
11.8
|
0.6
|
|
CD2
|
A:PHE99
|
4.9
|
8.9
|
1.0
|
|
CA
|
A:LEF108
|
4.9
|
9.8
|
0.6
|
|
CA
|
A:LEF108
|
4.9
|
9.8
|
0.4
|
|
HG3
|
A:MET49
|
5.0
|
11.0
|
1.0
|
|
Fluorine binding site 7 out
of 7 in 8vrg
Go back to
Fluorine Binding Sites List in 8vrg
Fluorine binding site 7 out
of 7 in the E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines
 Mono view
 Stereo pair view
|
|
A full contact list of Fluorine with other atoms in the F binding
site number 7 of E. Coli Peptidyl-Prolyl Cis-Trans Isomerase Containing DELTA1- Monofluoro-Leucines within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:F115
b:20.6
occ:1.00
|
F1
|
A:LEF115
|
0.0
|
20.6
|
1.0
|
|
CD1
|
A:LEF115
|
1.4
|
30.5
|
1.0
|
|
HD12
|
A:LEF115
|
2.0
|
36.6
|
1.0
|
|
HD13
|
A:LEF115
|
2.0
|
36.6
|
1.0
|
|
CG
|
A:LEF115
|
2.3
|
24.9
|
1.0
|
|
HB3
|
A:LEF115
|
2.5
|
26.4
|
1.0
|
|
HG
|
A:LEF115
|
2.6
|
29.8
|
1.0
|
|
HD3
|
A:PRO91
|
2.7
|
15.9
|
1.0
|
|
CB
|
A:LEF115
|
2.8
|
22.0
|
1.0
|
|
HA
|
A:LEF115
|
2.9
|
23.9
|
1.0
|
|
HD2
|
A:PRO91
|
3.0
|
15.9
|
1.0
|
|
CD
|
A:PRO91
|
3.3
|
13.2
|
1.0
|
|
CA
|
A:LEF115
|
3.4
|
19.9
|
1.0
|
|
HA
|
A:ALA90
|
3.7
|
16.1
|
1.0
|
|
CD2
|
A:LEF115
|
3.7
|
35.5
|
1.0
|
|
HG2
|
A:PRO91
|
3.7
|
20.5
|
1.0
|
|
HB2
|
A:LEF115
|
3.8
|
26.4
|
1.0
|
|
CG
|
A:PRO91
|
4.0
|
17.1
|
1.0
|
|
HD22
|
A:LEF115
|
4.0
|
42.6
|
1.0
|
|
HD23
|
A:LEF115
|
4.0
|
42.6
|
1.0
|
|
HG3
|
A:PRO91
|
4.2
|
20.5
|
1.0
|
|
N
|
A:LEF115
|
4.3
|
20.4
|
1.0
|
|
O
|
A:GLN89
|
4.3
|
23.4
|
1.0
|
|
HD21
|
A:LEF115
|
4.5
|
42.6
|
1.0
|
|
C
|
A:LEF115
|
4.6
|
19.0
|
1.0
|
|
N
|
A:PRO91
|
4.6
|
12.2
|
1.0
|
|
CA
|
A:ALA90
|
4.6
|
13.4
|
1.0
|
|
HE22
|
A:GLN89
|
4.7
|
31.6
|
1.0
|
|
O
|
A:LEF115
|
4.8
|
20.2
|
1.0
|
|
H
|
A:LEF115
|
4.9
|
24.5
|
1.0
|
|
Reference:
R.L.Frkic,
Y.J.Tan,
E.H.Abdelkader,
A.Maleckis,
E.Tarcoveanu,
C.Nitsche,
G.Otting,
C.J.Jackson.
Conformational Preferences of the Non-Canonical Amino Acids (2S,4S)-5-Fluoroleucine, (2S,4R)-5-Fluoroleucine, and 5,5'-Difluoroleucine in A Protein Biochemistry 2024.
ISSN: ISSN 0006-2960
DOI: 10.1021/ACS.BIOCHEM.4C00081
Page generated: Sat Aug 3 01:33:01 2024
|
