Zinc in PDB 4e3t: Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
Enzymatic activity of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
All present enzymatic activity of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog:
3.1.8.1;
Protein crystallography data
The structure of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog, PDB code: 4e3t
was solved by
N.Tokuriki,
C.J.Jackson,
D.S.Tawfik,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
|
Resolution Low / High (Å)
|
29.58 /
1.65
|
|
Space group
|
P 21 21 2
|
|
Cell size a, b, c (Å), α, β, γ (°)
|
85.771,
85.975,
88.727,
90.00,
90.00,
90.00
|
|
R / Rfree (%)
|
17.3 /
20.5
|
Zinc Binding Sites:
The binding sites of Zinc atom in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
(pdb code 4e3t). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the
Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog, PDB code: 4e3t:
Jump to Zinc binding site number:
1;
2;
3;
4;
5;
6;
Zinc binding site 1 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 1 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn401
b:14.4
occ:0.67
|
NE2
|
A:HIS57
|
2.0
|
11.6
|
1.0
|
|
O
|
A:HOH706
|
2.0
|
20.2
|
1.0
|
|
OD1
|
A:ASP301
|
2.0
|
8.5
|
0.5
|
|
O
|
A:HOH704
|
2.1
|
30.2
|
1.0
|
|
NE2
|
A:HIS55
|
2.3
|
24.9
|
1.0
|
|
OD1
|
A:ASP301
|
2.3
|
16.9
|
0.5
|
|
NE2
|
A:HIS57
|
2.5
|
11.5
|
0.0
|
|
ZN
|
A:ZN403
|
2.5
|
9.2
|
0.3
|
|
NE2
|
A:HIS55
|
2.8
|
22.1
|
0.0
|
|
CG
|
A:ASP301
|
2.8
|
12.3
|
0.5
|
|
CE1
|
A:HIS57
|
2.9
|
12.1
|
1.0
|
|
OD2
|
A:ASP301
|
2.9
|
14.9
|
0.5
|
|
CD2
|
A:HIS57
|
3.0
|
11.3
|
0.0
|
|
CD2
|
A:HIS57
|
3.1
|
10.2
|
1.0
|
|
CD2
|
A:HIS55
|
3.1
|
24.8
|
1.0
|
|
CD2
|
A:HIS55
|
3.1
|
20.4
|
0.0
|
|
CG
|
A:ASP301
|
3.2
|
12.7
|
0.5
|
|
CE1
|
A:HIS55
|
3.4
|
23.2
|
1.0
|
|
OD2
|
A:ASP301
|
3.4
|
12.7
|
0.5
|
|
CE1
|
A:HIS57
|
3.7
|
11.5
|
0.0
|
|
ZN
|
A:ZN402
|
3.8
|
17.1
|
0.5
|
|
NZ
|
A:LYS169
|
3.9
|
12.3
|
0.6
|
|
CG2
|
A:VAL101
|
4.0
|
12.7
|
1.0
|
|
ND1
|
A:HIS57
|
4.0
|
12.0
|
1.0
|
|
CE1
|
A:HIS55
|
4.1
|
21.3
|
0.0
|
|
CG
|
A:HIS57
|
4.1
|
11.8
|
1.0
|
|
O
|
A:HOH728
|
4.2
|
24.9
|
1.0
|
|
CG
|
A:HIS57
|
4.2
|
11.5
|
0.0
|
|
NE2
|
A:HIS230
|
4.3
|
23.3
|
1.0
|
|
CB
|
A:ASP301
|
4.3
|
12.4
|
0.5
|
|
CG
|
A:HIS55
|
4.3
|
14.0
|
1.0
|
|
ND1
|
A:HIS55
|
4.4
|
22.1
|
1.0
|
|
CG
|
A:HIS55
|
4.5
|
17.8
|
0.0
|
|
CB
|
A:ASP301
|
4.5
|
11.7
|
0.5
|
|
ND1
|
A:HIS57
|
4.5
|
11.4
|
0.0
|
|
CE1
|
A:HIS230
|
4.7
|
16.5
|
1.0
|
|
CA
|
A:ASP301
|
4.9
|
9.7
|
0.5
|
|
ND1
|
A:HIS55
|
4.9
|
18.7
|
0.0
|
|
CA
|
A:ASP301
|
4.9
|
10.2
|
0.5
|
|
Zinc binding site 2 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 2 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn402
b:17.1
occ:0.50
|
ND1
|
A:HIS201
|
1.8
|
18.1
|
0.5
|
|
CE1
|
A:HIS230
|
2.1
|
16.5
|
1.0
|
|
O
|
A:HOH728
|
2.2
|
24.9
|
1.0
|
|
CE1
|
A:HIS201
|
2.4
|
17.4
|
0.5
|
|
CE1
|
A:HIS201
|
2.6
|
22.3
|
0.5
|
|
O
|
A:HOH704
|
2.6
|
30.2
|
1.0
|
|
NE2
|
A:HIS201
|
2.7
|
16.6
|
0.5
|
|
ZN
|
A:ZN403
|
2.8
|
9.2
|
0.3
|
|
NE2
|
A:HIS230
|
2.8
|
23.3
|
1.0
|
|
O
|
A:HOH706
|
2.9
|
20.2
|
1.0
|
|
CG
|
A:HIS201
|
2.9
|
17.6
|
0.5
|
|
ND1
|
A:HIS201
|
3.0
|
16.6
|
0.5
|
|
ND1
|
A:HIS230
|
3.3
|
20.6
|
1.0
|
|
CD2
|
A:HIS201
|
3.5
|
20.3
|
0.5
|
|
CB
|
A:HIS201
|
3.5
|
16.6
|
0.5
|
|
CG
|
A:HIS201
|
3.6
|
16.3
|
0.5
|
|
NE2
|
A:HIS201
|
3.8
|
15.5
|
0.5
|
|
ZN
|
A:ZN401
|
3.8
|
14.4
|
0.7
|
|
NZ
|
A:LYS169
|
3.9
|
13.4
|
0.4
|
|
CD2
|
A:HIS201
|
3.9
|
19.3
|
0.5
|
|
NZ
|
A:LYS169
|
4.0
|
12.3
|
0.6
|
|
NE1
|
A:TRP131
|
4.1
|
20.9
|
1.0
|
|
CD2
|
A:HIS230
|
4.1
|
17.4
|
1.0
|
|
OD2
|
A:ASP301
|
4.2
|
14.9
|
0.5
|
|
CA
|
A:HIS201
|
4.2
|
15.1
|
0.5
|
|
CG
|
A:HIS230
|
4.3
|
17.7
|
1.0
|
|
CE1
|
A:HIS55
|
4.3
|
23.2
|
1.0
|
|
NE2
|
A:HIS55
|
4.3
|
24.9
|
1.0
|
|
NE2
|
A:HIS55
|
4.4
|
22.1
|
0.0
|
|
CE
|
A:LYS169
|
4.5
|
12.4
|
0.6
|
|
CE
|
A:LYS169
|
4.5
|
10.8
|
0.4
|
|
OD2
|
A:ASP301
|
4.6
|
12.7
|
0.5
|
|
CD1
|
A:TRP131
|
4.6
|
20.7
|
1.0
|
|
CE1
|
A:HIS55
|
4.7
|
21.3
|
0.0
|
|
CB
|
A:HIS201
|
4.8
|
19.4
|
0.5
|
|
Zinc binding site 3 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 3 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Zn403
b:9.2
occ:0.31
|
NE2
|
A:HIS230
|
1.9
|
23.3
|
1.0
|
|
OD2
|
A:ASP301
|
1.9
|
14.9
|
0.5
|
|
NE2
|
A:HIS55
|
1.9
|
24.9
|
1.0
|
|
CE1
|
A:HIS55
|
2.2
|
23.2
|
1.0
|
|
NE2
|
A:HIS55
|
2.3
|
22.1
|
0.0
|
|
ZN
|
A:ZN401
|
2.5
|
14.4
|
0.7
|
|
O
|
A:HOH704
|
2.5
|
30.2
|
1.0
|
|
CE1
|
A:HIS230
|
2.7
|
16.5
|
1.0
|
|
CG
|
A:ASP301
|
2.8
|
12.3
|
0.5
|
|
ZN
|
A:ZN402
|
2.8
|
17.1
|
0.5
|
|
CE1
|
A:HIS55
|
2.9
|
21.3
|
0.0
|
|
O
|
A:HOH706
|
3.0
|
20.2
|
1.0
|
|
CD2
|
A:HIS55
|
3.0
|
20.4
|
0.0
|
|
CD2
|
A:HIS230
|
3.0
|
17.4
|
1.0
|
|
CD2
|
A:HIS55
|
3.0
|
24.8
|
1.0
|
|
OD2
|
A:ASP301
|
3.0
|
12.7
|
0.5
|
|
OD1
|
A:ASP301
|
3.1
|
8.5
|
0.5
|
|
CG
|
A:ASP301
|
3.3
|
12.7
|
0.5
|
|
OD1
|
A:ASP301
|
3.3
|
16.9
|
0.5
|
|
ND1
|
A:HIS55
|
3.3
|
22.1
|
1.0
|
|
CG
|
A:HIS55
|
3.7
|
14.0
|
1.0
|
|
ND1
|
A:HIS55
|
3.7
|
18.7
|
0.0
|
|
CG
|
A:HIS55
|
3.8
|
17.8
|
0.0
|
|
ND1
|
A:HIS230
|
3.9
|
20.6
|
1.0
|
|
CG
|
A:HIS230
|
4.0
|
17.7
|
1.0
|
|
CB
|
A:ASP301
|
4.1
|
12.4
|
0.5
|
|
O
|
A:HOH728
|
4.3
|
24.9
|
1.0
|
|
CB
|
A:ASP301
|
4.3
|
11.7
|
0.5
|
|
NZ
|
A:LYS169
|
4.3
|
13.4
|
0.4
|
|
NZ
|
A:LYS169
|
4.4
|
12.3
|
0.6
|
|
NE2
|
A:HIS57
|
4.4
|
11.6
|
1.0
|
|
ND1
|
A:HIS201
|
4.5
|
18.1
|
0.5
|
|
ND1
|
A:HIS201
|
4.6
|
16.6
|
0.5
|
|
CE1
|
A:HIS201
|
4.6
|
17.4
|
0.5
|
|
NH1
|
A:ARG254
|
4.7
|
41.6
|
1.0
|
|
CD
|
A:ARG254
|
4.7
|
19.7
|
1.0
|
|
NE2
|
A:HIS57
|
4.8
|
11.5
|
0.0
|
|
CG
|
A:ARG254
|
4.8
|
22.3
|
1.0
|
|
OD1
|
A:ASP253
|
4.9
|
24.2
|
1.0
|
|
CE
|
A:LYS169
|
5.0
|
12.4
|
0.6
|
|
Zinc binding site 4 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 4 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn401
b:19.4
occ:0.60
|
OAH
|
B:HLN404
|
1.8
|
11.8
|
0.7
|
|
O
|
B:HOH721
|
1.9
|
16.8
|
1.0
|
|
NE2
|
B:HIS55
|
2.1
|
23.4
|
0.5
|
|
NE2
|
B:HIS57
|
2.1
|
15.9
|
1.0
|
|
OD1
|
B:ASP301
|
2.1
|
21.9
|
0.7
|
|
ZN
|
B:ZN403
|
2.1
|
18.1
|
0.5
|
|
OD1
|
B:ASP301
|
2.5
|
20.2
|
0.3
|
|
CG
|
B:ASP301
|
2.8
|
19.8
|
0.7
|
|
OD2
|
B:ASP301
|
2.9
|
22.4
|
0.7
|
|
CE1
|
B:HIS57
|
3.0
|
17.2
|
1.0
|
|
NE2
|
B:HIS55
|
3.1
|
25.6
|
0.5
|
|
CD2
|
B:HIS55
|
3.1
|
20.2
|
0.5
|
|
CE1
|
B:HIS55
|
3.1
|
25.9
|
0.5
|
|
PAG
|
B:HLN404
|
3.1
|
37.8
|
0.7
|
|
CD2
|
B:HIS57
|
3.2
|
21.6
|
1.0
|
|
CG
|
B:ASP301
|
3.2
|
20.8
|
0.3
|
|
OD2
|
B:ASP301
|
3.5
|
16.2
|
0.3
|
|
CD2
|
B:HIS55
|
3.5
|
19.1
|
0.5
|
|
NZ
|
B:LYS169
|
3.7
|
13.3
|
0.4
|
|
OAJ
|
B:HLN404
|
3.8
|
45.0
|
0.7
|
|
ZN
|
B:ZN402
|
3.9
|
20.7
|
0.5
|
|
CAF
|
B:HLN404
|
3.9
|
23.5
|
0.7
|
|
CG2
|
B:VAL101
|
3.9
|
19.9
|
1.0
|
|
CE1
|
B:HIS55
|
4.0
|
22.0
|
0.5
|
|
CE1
|
B:HIS230
|
4.1
|
15.9
|
0.5
|
|
NE2
|
B:HIS230
|
4.1
|
15.4
|
0.5
|
|
ND1
|
B:HIS57
|
4.2
|
18.5
|
1.0
|
|
NE2
|
B:HIS230
|
4.2
|
15.2
|
0.5
|
|
ND1
|
B:HIS55
|
4.2
|
21.0
|
0.5
|
|
CG
|
B:HIS55
|
4.2
|
19.1
|
0.5
|
|
CG
|
B:HIS57
|
4.3
|
19.0
|
1.0
|
|
CB
|
B:ASP301
|
4.3
|
17.0
|
0.7
|
|
OAI
|
B:HLN404
|
4.3
|
31.8
|
0.7
|
|
CB
|
B:ASP301
|
4.4
|
19.3
|
0.3
|
|
CAE
|
B:HLN404
|
4.5
|
25.5
|
0.7
|
|
CG
|
B:HIS55
|
4.6
|
20.1
|
0.5
|
|
O
|
B:HOH676
|
4.6
|
37.0
|
1.0
|
|
CE1
|
B:HIS230
|
4.8
|
19.5
|
0.5
|
|
CA
|
B:ASP301
|
4.8
|
18.9
|
0.7
|
|
ND1
|
B:HIS55
|
4.8
|
21.2
|
0.5
|
|
CA
|
B:ASP301
|
4.8
|
20.2
|
0.3
|
|
CE
|
B:LYS169
|
4.9
|
19.7
|
0.4
|
|
Zinc binding site 5 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 5 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 5 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn402
b:20.7
occ:0.47
|
CE1
|
B:HIS201
|
1.8
|
27.7
|
0.7
|
|
CE1
|
B:HIS230
|
2.0
|
19.5
|
0.5
|
|
NE2
|
B:HIS230
|
2.1
|
15.2
|
0.5
|
|
OAI
|
B:HLN404
|
2.3
|
31.8
|
0.7
|
|
ND1
|
B:HIS201
|
2.3
|
34.3
|
0.7
|
|
OAH
|
B:HLN404
|
2.3
|
11.8
|
0.7
|
|
NE2
|
B:HIS201
|
2.4
|
24.9
|
0.7
|
|
NE2
|
B:HIS230
|
2.4
|
15.4
|
0.5
|
|
O
|
B:HOH721
|
2.8
|
16.8
|
1.0
|
|
CD2
|
B:HIS230
|
2.8
|
21.6
|
0.5
|
|
CD2
|
B:HIS201
|
2.8
|
30.7
|
0.3
|
|
PAG
|
B:HLN404
|
2.8
|
37.8
|
0.7
|
|
ZN
|
B:ZN403
|
2.8
|
18.1
|
0.5
|
|
NE2
|
B:HIS201
|
2.9
|
25.6
|
0.3
|
|
CG
|
B:HIS201
|
3.0
|
32.8
|
0.7
|
|
CD2
|
B:HIS201
|
3.1
|
27.4
|
0.7
|
|
ND1
|
B:HIS230
|
3.2
|
19.0
|
0.5
|
|
CG
|
B:HIS201
|
3.2
|
31.2
|
0.3
|
|
CE1
|
B:HIS230
|
3.2
|
15.9
|
0.5
|
|
CE1
|
B:HIS201
|
3.2
|
26.9
|
0.3
|
|
ND1
|
B:HIS201
|
3.4
|
26.8
|
0.3
|
|
CD2
|
B:HIS230
|
3.6
|
17.7
|
0.5
|
|
CAQ
|
B:HLN404
|
3.7
|
41.5
|
0.7
|
|
OAJ
|
B:HLN404
|
3.8
|
45.0
|
0.7
|
|
NZ
|
B:LYS169
|
3.8
|
20.3
|
0.6
|
|
NZ
|
B:LYS169
|
3.9
|
13.3
|
0.4
|
|
ZN
|
B:ZN401
|
3.9
|
19.4
|
0.6
|
|
CG
|
B:HIS230
|
4.0
|
19.1
|
0.5
|
|
CG
|
B:HIS230
|
4.0
|
19.7
|
0.5
|
|
CB
|
B:HIS201
|
4.0
|
35.0
|
0.3
|
|
NE1
|
B:TRP131
|
4.1
|
31.9
|
1.0
|
|
CAR
|
B:HLN404
|
4.1
|
42.3
|
0.7
|
|
CE1
|
B:HIS55
|
4.1
|
25.9
|
0.5
|
|
ND1
|
B:HIS230
|
4.2
|
20.0
|
0.5
|
|
CB
|
B:HIS201
|
4.2
|
37.2
|
0.7
|
|
CE
|
B:LYS169
|
4.2
|
19.7
|
0.4
|
|
NE2
|
B:HIS55
|
4.3
|
25.6
|
0.5
|
|
OD2
|
B:ASP301
|
4.3
|
22.4
|
0.7
|
|
CE
|
B:LYS169
|
4.4
|
20.9
|
0.6
|
|
CAF
|
B:HLN404
|
4.4
|
23.5
|
0.7
|
|
NE2
|
B:HIS55
|
4.4
|
23.4
|
0.5
|
|
CD1
|
B:TRP131
|
4.7
|
28.6
|
1.0
|
|
CAK
|
B:HLN404
|
4.7
|
39.9
|
0.7
|
|
CE1
|
B:HIS55
|
4.8
|
22.0
|
0.5
|
|
OD2
|
B:ASP301
|
4.9
|
16.2
|
0.3
|
|
CAP
|
B:HLN404
|
5.0
|
38.3
|
0.7
|
|
Zinc binding site 6 out
of 6 in 4e3t
Go back to
Zinc Binding Sites List in 4e3t
Zinc binding site 6 out
of 6 in the Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog
 Mono view
 Stereo pair view
|
|
A full contact list of Zinc with other atoms in the Zn binding
site number 6 of Round 18 Arylesterase Variant of Phosphotriesterase with Bound Transition State Analog within 5.0Å range:
|
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Zn403
b:18.1
occ:0.46
|
CE1
|
B:HIS230
|
2.0
|
15.9
|
0.5
|
|
NE2
|
B:HIS55
|
2.0
|
23.4
|
0.5
|
|
OD2
|
B:ASP301
|
2.1
|
22.4
|
0.7
|
|
NE2
|
B:HIS230
|
2.1
|
15.4
|
0.5
|
|
NE2
|
B:HIS55
|
2.1
|
25.6
|
0.5
|
|
ZN
|
B:ZN401
|
2.1
|
19.4
|
0.6
|
|
OAH
|
B:HLN404
|
2.1
|
11.8
|
0.7
|
|
CE1
|
B:HIS55
|
2.2
|
25.9
|
0.5
|
|
NE2
|
B:HIS230
|
2.3
|
15.2
|
0.5
|
|
O
|
B:HOH721
|
2.6
|
16.8
|
1.0
|
|
CG
|
B:ASP301
|
2.7
|
19.8
|
0.7
|
|
ZN
|
B:ZN402
|
2.8
|
20.7
|
0.5
|
|
OD1
|
B:ASP301
|
2.9
|
21.9
|
0.7
|
|
CD2
|
B:HIS55
|
2.9
|
19.1
|
0.5
|
|
OD2
|
B:ASP301
|
3.0
|
16.2
|
0.3
|
|
CE1
|
B:HIS230
|
3.0
|
19.5
|
0.5
|
|
CD2
|
B:HIS230
|
3.1
|
17.7
|
0.5
|
|
CG
|
B:ASP301
|
3.2
|
20.8
|
0.3
|
|
CD2
|
B:HIS55
|
3.2
|
20.2
|
0.5
|
|
CE1
|
B:HIS55
|
3.2
|
22.0
|
0.5
|
|
ND1
|
B:HIS230
|
3.3
|
20.0
|
0.5
|
|
OD1
|
B:ASP301
|
3.3
|
20.2
|
0.3
|
|
ND1
|
B:HIS55
|
3.3
|
21.0
|
0.5
|
|
PAG
|
B:HLN404
|
3.5
|
37.8
|
0.7
|
|
CD2
|
B:HIS230
|
3.6
|
21.6
|
0.5
|
|
CG
|
B:HIS55
|
3.8
|
19.1
|
0.5
|
|
OAJ
|
B:HLN404
|
3.9
|
45.0
|
0.7
|
|
CB
|
B:ASP301
|
4.1
|
17.0
|
0.7
|
|
CG
|
B:HIS230
|
4.1
|
19.7
|
0.5
|
|
CG
|
B:HIS55
|
4.1
|
20.1
|
0.5
|
|
CB
|
B:ASP301
|
4.1
|
19.3
|
0.3
|
|
OAI
|
B:HLN404
|
4.1
|
31.8
|
0.7
|
|
ND1
|
B:HIS230
|
4.2
|
19.0
|
0.5
|
|
NZ
|
B:LYS169
|
4.2
|
13.3
|
0.4
|
|
CG
|
B:HIS230
|
4.2
|
19.1
|
0.5
|
|
NE2
|
B:HIS57
|
4.2
|
15.9
|
1.0
|
|
ND1
|
B:HIS55
|
4.2
|
21.2
|
0.5
|
|
ND1
|
B:HIS201
|
4.3
|
34.3
|
0.7
|
|
CE1
|
B:HIS201
|
4.4
|
27.7
|
0.7
|
|
CAQ
|
B:HLN404
|
4.4
|
41.5
|
0.7
|
|
CAR
|
B:HLN404
|
4.7
|
42.3
|
0.7
|
|
NZ
|
B:LYS169
|
4.7
|
20.3
|
0.6
|
|
NE
|
B:ARG254
|
4.7
|
29.8
|
1.0
|
|
CD
|
B:ARG254
|
4.9
|
19.7
|
1.0
|
|
OD1
|
B:ASP253
|
4.9
|
30.6
|
1.0
|
|
CG
|
B:ARG254
|
4.9
|
23.5
|
1.0
|
|
CE
|
B:LYS169
|
5.0
|
19.7
|
0.4
|
|
CG2
|
B:VAL101
|
5.0
|
19.9
|
1.0
|
|
CAF
|
B:HLN404
|
5.0
|
23.5
|
0.7
|
|
Reference:
N.Tokuriki,
C.J.Jackson,
L.Afriat-Jurnou,
K.T.Wyganowski,
R.Tang,
D.S.Tawfik.
Diminishing Returns and Tradeoffs Constrain the Laboratory Optimization of An Enzyme Nat Commun V. 3 1257 2012.
ISSN: ESSN 2041-1723
PubMed: 23212386
DOI: 10.1038/NCOMMS2246
Page generated: Sat Oct 26 21:52:37 2024
|
