Magnesium in PDB 1hn1: E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Enzymatic activity of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
All present enzymatic activity of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic):
3.1.2.23;
Protein crystallography data
The structure of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic), PDB code: 1hn1
was solved by
D.H.Juers,
B.W.Matthews,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
15.00 /
3.00
|
Space group
|
P 21 21 21
|
Cell size a, b, c (Å), α, β, γ (°)
|
153.900,
171.400,
204.500,
90.00,
90.00,
90.00
|
R / Rfree (%)
|
n/a /
n/a
|
Other elements in 1hn1:
The structure of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) also contains other interesting chemical elements:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
(pdb code 1hn1). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 8 binding sites of Magnesium where determined in the
E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic), PDB code: 1hn1:
Jump to Magnesium binding site number:
1;
2;
3;
4;
5;
6;
7;
8;
Magnesium binding site 1 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 1 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 1 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg3001
b:29.5
occ:1.00
|
OE2
|
A:GLU416
|
2.4
|
28.2
|
1.0
|
OE1
|
A:GLU461
|
2.5
|
60.5
|
1.0
|
ND1
|
A:HIS418
|
2.9
|
33.9
|
1.0
|
OD1
|
A:ASN102
|
3.3
|
49.6
|
1.0
|
CD
|
A:GLU416
|
3.6
|
71.1
|
1.0
|
O
|
A:HOH4001
|
3.6
|
52.9
|
1.0
|
CB
|
A:ASP201
|
3.7
|
35.0
|
1.0
|
CE1
|
A:HIS418
|
3.7
|
30.9
|
1.0
|
CD
|
A:GLU461
|
3.7
|
72.4
|
1.0
|
O
|
A:ASN102
|
3.7
|
40.4
|
1.0
|
N
|
A:ASP201
|
3.8
|
28.4
|
1.0
|
CG
|
A:HIS418
|
4.0
|
31.7
|
1.0
|
OE1
|
A:GLU416
|
4.1
|
21.9
|
1.0
|
O
|
A:ASP199
|
4.2
|
32.4
|
1.0
|
CA
|
A:ASP201
|
4.2
|
25.8
|
1.0
|
CB
|
A:HIS418
|
4.3
|
34.0
|
1.0
|
OE2
|
A:GLU461
|
4.3
|
35.0
|
1.0
|
C
|
A:ASN102
|
4.5
|
35.0
|
1.0
|
CG2
|
A:VAL103
|
4.6
|
2.3
|
1.0
|
CG
|
A:ASN102
|
4.6
|
64.6
|
1.0
|
C
|
A:GLN200
|
4.6
|
38.4
|
1.0
|
CG
|
A:GLU416
|
4.8
|
5.4
|
1.0
|
CA
|
A:GLN200
|
4.9
|
29.9
|
1.0
|
CG
|
A:ASP201
|
4.9
|
72.2
|
1.0
|
NE2
|
A:HIS418
|
4.9
|
25.9
|
1.0
|
CG
|
A:GLU461
|
5.0
|
34.7
|
1.0
|
|
Magnesium binding site 2 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 2 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 2 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Mg3002
b:29.5
occ:1.00
|
O
|
A:VAL21
|
2.1
|
46.3
|
1.0
|
O
|
A:ASP15
|
2.3
|
44.5
|
1.0
|
OE1
|
A:GLN163
|
2.4
|
34.0
|
1.0
|
O
|
A:ASN18
|
2.8
|
23.0
|
1.0
|
OD1
|
A:ASP193
|
2.8
|
28.7
|
1.0
|
OD2
|
A:ASP193
|
2.8
|
42.9
|
1.0
|
NE2
|
A:GLN163
|
3.0
|
1.0
|
1.0
|
CD
|
A:GLN163
|
3.1
|
37.5
|
1.0
|
CG
|
A:ASP193
|
3.1
|
29.3
|
1.0
|
C
|
A:VAL21
|
3.2
|
40.7
|
1.0
|
C
|
A:ASN18
|
3.4
|
27.9
|
1.0
|
C
|
A:ASP15
|
3.5
|
31.5
|
1.0
|
N
|
A:ASN18
|
3.7
|
43.1
|
1.0
|
CA
|
A:VAL21
|
3.9
|
34.4
|
1.0
|
N
|
A:VAL21
|
3.9
|
35.0
|
1.0
|
CA
|
A:ASN18
|
3.9
|
40.5
|
1.0
|
CB
|
A:VAL21
|
4.0
|
38.4
|
1.0
|
CA
|
A:TRP16
|
4.2
|
26.5
|
1.0
|
N
|
A:THR22
|
4.2
|
27.7
|
1.0
|
CE2
|
A:TYR161
|
4.2
|
15.2
|
1.0
|
N
|
A:TRP16
|
4.3
|
24.1
|
1.0
|
OH
|
A:TYR161
|
4.3
|
23.0
|
1.0
|
N
|
A:PRO19
|
4.3
|
34.1
|
1.0
|
CG1
|
A:VAL21
|
4.3
|
39.8
|
1.0
|
CB
|
A:ASN18
|
4.4
|
54.6
|
1.0
|
N
|
A:GLU17
|
4.4
|
18.1
|
1.0
|
CA
|
A:ASP15
|
4.5
|
27.0
|
1.0
|
C
|
A:TRP16
|
4.5
|
26.9
|
1.0
|
CA
|
A:THR22
|
4.5
|
23.2
|
1.0
|
CB
|
A:ASP193
|
4.6
|
41.7
|
1.0
|
CG
|
A:GLN163
|
4.6
|
22.3
|
1.0
|
CA
|
A:PRO19
|
4.7
|
33.0
|
1.0
|
CZ
|
A:TYR161
|
4.8
|
26.5
|
1.0
|
C
|
A:PRO19
|
4.8
|
42.5
|
1.0
|
C
|
A:GLU17
|
4.9
|
38.3
|
1.0
|
CB
|
A:ASP15
|
4.9
|
35.7
|
1.0
|
|
Magnesium binding site 3 out
of 8 in 1hn1
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Magnesium Binding Sites List in 1hn1
Magnesium binding site 3 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 3 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg3001
b:13.2
occ:1.00
|
OE2
|
B:GLU416
|
2.1
|
28.7
|
1.0
|
OE1
|
B:GLU461
|
2.2
|
57.8
|
1.0
|
ND1
|
B:HIS418
|
2.3
|
39.9
|
1.0
|
CE1
|
B:HIS418
|
3.0
|
36.8
|
1.0
|
OD1
|
B:ASN102
|
3.2
|
57.2
|
1.0
|
CD
|
B:GLU461
|
3.4
|
23.1
|
1.0
|
CD
|
B:GLU416
|
3.4
|
30.6
|
1.0
|
CG
|
B:HIS418
|
3.5
|
35.6
|
1.0
|
CB
|
B:ASP201
|
3.8
|
34.3
|
1.0
|
N
|
B:ASP201
|
3.9
|
31.6
|
1.0
|
OE1
|
B:GLU416
|
3.9
|
62.0
|
1.0
|
CB
|
B:HIS418
|
4.0
|
31.2
|
1.0
|
OE2
|
B:GLU461
|
4.0
|
34.5
|
1.0
|
O
|
B:ASP199
|
4.2
|
36.8
|
1.0
|
O
|
B:ASN102
|
4.2
|
34.3
|
1.0
|
NE2
|
B:HIS418
|
4.2
|
32.4
|
1.0
|
CA
|
B:ASP201
|
4.3
|
34.5
|
1.0
|
CG
|
B:ASN102
|
4.4
|
48.1
|
1.0
|
ND2
|
B:ASN460
|
4.4
|
53.7
|
1.0
|
CD2
|
B:HIS418
|
4.5
|
29.2
|
1.0
|
CG
|
B:GLU416
|
4.5
|
35.2
|
1.0
|
CG
|
B:GLU461
|
4.6
|
3.6
|
1.0
|
O
|
B:HOH4568
|
4.6
|
59.9
|
1.0
|
O
|
B:HOH4298
|
4.7
|
23.0
|
1.0
|
CB
|
B:GLU461
|
4.7
|
8.3
|
1.0
|
C
|
B:ASN102
|
4.8
|
39.3
|
1.0
|
C
|
B:GLN200
|
4.9
|
36.5
|
1.0
|
CG2
|
B:VAL103
|
4.9
|
24.7
|
1.0
|
CG
|
B:ASP201
|
5.0
|
45.7
|
1.0
|
|
Magnesium binding site 4 out
of 8 in 1hn1
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Magnesium Binding Sites List in 1hn1
Magnesium binding site 4 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 4 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Mg3002
b:30.0
occ:1.00
|
O
|
B:ASP15
|
2.0
|
25.9
|
1.0
|
O
|
B:ASN18
|
2.1
|
29.2
|
1.0
|
O
|
B:VAL21
|
2.2
|
37.9
|
1.0
|
OE1
|
B:GLN163
|
2.4
|
69.9
|
1.0
|
OD2
|
B:ASP193
|
2.4
|
5.2
|
1.0
|
C
|
B:ASN18
|
2.9
|
31.4
|
1.0
|
N
|
B:ASN18
|
3.0
|
31.6
|
1.0
|
CD
|
B:GLN163
|
3.2
|
42.2
|
1.0
|
C
|
B:ASP15
|
3.2
|
33.0
|
1.0
|
C
|
B:VAL21
|
3.3
|
42.3
|
1.0
|
CA
|
B:ASN18
|
3.3
|
29.6
|
1.0
|
NE2
|
B:GLN163
|
3.4
|
14.9
|
1.0
|
CG
|
B:ASP193
|
3.4
|
43.9
|
1.0
|
OD1
|
B:ASP193
|
3.8
|
48.8
|
1.0
|
N
|
B:PRO19
|
4.0
|
29.5
|
1.0
|
CB
|
B:ASN18
|
4.0
|
28.6
|
1.0
|
CA
|
B:VAL21
|
4.0
|
36.2
|
1.0
|
N
|
B:VAL21
|
4.0
|
34.6
|
1.0
|
CA
|
B:TRP16
|
4.1
|
28.1
|
1.0
|
N
|
B:TRP16
|
4.1
|
26.0
|
1.0
|
OH
|
B:TYR161
|
4.1
|
38.4
|
1.0
|
N
|
B:GLU17
|
4.1
|
37.6
|
1.0
|
C
|
B:TRP16
|
4.2
|
37.4
|
1.0
|
CB
|
B:VAL21
|
4.2
|
35.6
|
1.0
|
C
|
B:GLU17
|
4.3
|
42.7
|
1.0
|
CA
|
B:ASP15
|
4.3
|
30.2
|
1.0
|
CE2
|
B:TYR161
|
4.3
|
65.1
|
1.0
|
N
|
B:THR22
|
4.4
|
31.3
|
1.0
|
CA
|
B:THR22
|
4.5
|
28.0
|
1.0
|
CA
|
B:PRO19
|
4.5
|
25.4
|
1.0
|
CZ
|
B:TYR161
|
4.6
|
57.5
|
1.0
|
CB
|
B:ASP193
|
4.7
|
33.9
|
1.0
|
CG
|
B:GLN163
|
4.7
|
11.2
|
1.0
|
CG
|
B:ASN18
|
4.7
|
76.1
|
1.0
|
CA
|
B:GLU17
|
4.8
|
38.8
|
1.0
|
CB
|
B:ASP15
|
4.8
|
28.6
|
1.0
|
C
|
B:PRO19
|
4.8
|
34.7
|
1.0
|
O
|
B:TRP16
|
4.8
|
38.1
|
1.0
|
CG2
|
B:THR22
|
4.8
|
2.2
|
1.0
|
N
|
B:GLY20
|
4.9
|
26.1
|
1.0
|
ND2
|
B:ASN18
|
5.0
|
81.8
|
1.0
|
|
Magnesium binding site 5 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 5 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 5 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg3001
b:25.6
occ:1.00
|
OE2
|
C:GLU416
|
2.1
|
31.2
|
1.0
|
OE1
|
C:GLU461
|
2.2
|
62.2
|
1.0
|
ND1
|
C:HIS418
|
2.4
|
38.8
|
1.0
|
CD
|
C:GLU416
|
3.0
|
83.3
|
1.0
|
OE1
|
C:GLU416
|
3.2
|
7.4
|
1.0
|
CE1
|
C:HIS418
|
3.3
|
36.5
|
1.0
|
CD
|
C:GLU461
|
3.4
|
32.0
|
1.0
|
CG
|
C:HIS418
|
3.5
|
30.4
|
1.0
|
OD1
|
C:ASN102
|
3.7
|
68.5
|
1.0
|
N
|
C:ASP201
|
3.9
|
24.3
|
1.0
|
CB
|
C:ASP201
|
3.9
|
31.1
|
1.0
|
CB
|
C:HIS418
|
3.9
|
22.3
|
1.0
|
O
|
C:ASP199
|
3.9
|
41.6
|
1.0
|
OE2
|
C:GLU461
|
4.2
|
18.9
|
1.0
|
CG
|
C:GLU416
|
4.4
|
35.4
|
1.0
|
ND2
|
C:ASN460
|
4.4
|
43.9
|
1.0
|
CB
|
C:GLU461
|
4.4
|
23.2
|
1.0
|
CA
|
C:ASP201
|
4.5
|
27.8
|
1.0
|
CG
|
C:GLU461
|
4.5
|
25.1
|
1.0
|
NE2
|
C:HIS418
|
4.5
|
29.7
|
1.0
|
CA
|
C:GLN200
|
4.6
|
37.0
|
1.0
|
O
|
C:ASN102
|
4.6
|
52.6
|
1.0
|
C
|
C:GLN200
|
4.6
|
38.4
|
1.0
|
CD2
|
C:HIS418
|
4.6
|
30.4
|
1.0
|
CG
|
C:ASN102
|
4.9
|
53.8
|
1.0
|
C
|
C:ASP199
|
5.0
|
34.9
|
1.0
|
|
Magnesium binding site 6 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 6 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 6 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Mg3002
b:25.7
occ:1.00
|
O
|
C:ASN18
|
2.1
|
30.4
|
1.0
|
OD2
|
C:ASP193
|
2.1
|
1.0
|
1.0
|
O
|
C:ASP15
|
2.2
|
20.7
|
1.0
|
O
|
C:VAL21
|
2.3
|
27.3
|
1.0
|
OE1
|
C:GLN163
|
2.4
|
49.2
|
1.0
|
NE2
|
C:GLN163
|
2.8
|
4.9
|
1.0
|
C
|
C:ASN18
|
2.9
|
35.7
|
1.0
|
CD
|
C:GLN163
|
3.0
|
34.6
|
1.0
|
CG
|
C:ASP193
|
3.1
|
42.8
|
1.0
|
N
|
C:ASN18
|
3.2
|
29.0
|
1.0
|
C
|
C:ASP15
|
3.3
|
27.5
|
1.0
|
CA
|
C:ASN18
|
3.4
|
28.4
|
1.0
|
OD1
|
C:ASP193
|
3.4
|
43.1
|
1.0
|
C
|
C:VAL21
|
3.6
|
26.8
|
1.0
|
CA
|
C:TRP16
|
3.9
|
24.1
|
1.0
|
N
|
C:PRO19
|
3.9
|
29.7
|
1.0
|
C
|
C:TRP16
|
3.9
|
31.8
|
1.0
|
CB
|
C:ASN18
|
3.9
|
23.3
|
1.0
|
OH
|
C:TYR161
|
4.0
|
42.0
|
1.0
|
N
|
C:TRP16
|
4.0
|
17.2
|
1.0
|
O
|
C:TRP16
|
4.1
|
27.0
|
1.0
|
N
|
C:GLU17
|
4.3
|
32.5
|
1.0
|
CB
|
C:ASP193
|
4.4
|
43.3
|
1.0
|
CA
|
C:PRO19
|
4.4
|
22.7
|
1.0
|
C
|
C:GLU17
|
4.4
|
36.6
|
1.0
|
CA
|
C:VAL21
|
4.4
|
25.5
|
1.0
|
N
|
C:VAL21
|
4.4
|
23.4
|
1.0
|
CA
|
C:ASP15
|
4.4
|
39.0
|
1.0
|
CG
|
C:GLN163
|
4.5
|
35.7
|
1.0
|
N
|
C:THR22
|
4.5
|
16.7
|
1.0
|
CE2
|
C:TYR161
|
4.6
|
32.0
|
1.0
|
CA
|
C:THR22
|
4.6
|
19.1
|
1.0
|
CZ
|
C:TYR161
|
4.7
|
41.6
|
1.0
|
CB
|
C:VAL21
|
4.7
|
32.2
|
1.0
|
N
|
C:ASP193
|
4.8
|
32.8
|
1.0
|
CG
|
C:ASN18
|
4.8
|
71.9
|
1.0
|
CB
|
C:ASP15
|
4.8
|
43.3
|
1.0
|
C
|
C:PRO19
|
4.9
|
23.1
|
1.0
|
CA
|
C:GLU17
|
4.9
|
31.8
|
1.0
|
CG2
|
C:THR22
|
5.0
|
14.8
|
1.0
|
N
|
C:GLY20
|
5.0
|
15.0
|
1.0
|
|
Magnesium binding site 7 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 7 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 7 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg3001
b:26.2
occ:1.00
|
OE2
|
D:GLU416
|
2.1
|
32.4
|
1.0
|
OE1
|
D:GLU461
|
2.2
|
42.8
|
1.0
|
ND1
|
D:HIS418
|
2.3
|
35.4
|
1.0
|
CE1
|
D:HIS418
|
3.1
|
26.5
|
1.0
|
O
|
D:HOH4412
|
3.3
|
55.1
|
1.0
|
OD1
|
D:ASN102
|
3.3
|
75.7
|
1.0
|
CD
|
D:GLU461
|
3.4
|
25.3
|
1.0
|
CD
|
D:GLU416
|
3.4
|
59.9
|
1.0
|
CG
|
D:HIS418
|
3.5
|
34.9
|
1.0
|
N
|
D:ASP201
|
3.8
|
45.1
|
1.0
|
CB
|
D:ASP201
|
3.8
|
45.7
|
1.0
|
OE2
|
D:GLU461
|
4.0
|
35.8
|
1.0
|
CB
|
D:HIS418
|
4.0
|
34.8
|
1.0
|
OE1
|
D:GLU416
|
4.1
|
49.4
|
1.0
|
O
|
D:ASP199
|
4.2
|
35.3
|
1.0
|
CA
|
D:ASP201
|
4.3
|
43.2
|
1.0
|
O
|
D:ASN102
|
4.4
|
36.7
|
1.0
|
NE2
|
D:HIS418
|
4.4
|
18.1
|
1.0
|
CG
|
D:GLU416
|
4.5
|
6.2
|
1.0
|
ND2
|
D:ASN460
|
4.6
|
96.2
|
1.0
|
CG
|
D:ASN102
|
4.6
|
61.4
|
1.0
|
CD2
|
D:HIS418
|
4.6
|
17.4
|
1.0
|
CG
|
D:GLU461
|
4.6
|
4.1
|
1.0
|
C
|
D:GLN200
|
4.7
|
40.4
|
1.0
|
CA
|
D:GLN200
|
4.8
|
28.8
|
1.0
|
CB
|
D:GLU461
|
4.8
|
13.3
|
1.0
|
C
|
D:ASN102
|
4.9
|
40.8
|
1.0
|
CG2
|
D:VAL103
|
5.0
|
25.2
|
1.0
|
|
Magnesium binding site 8 out
of 8 in 1hn1
Go back to
Magnesium Binding Sites List in 1hn1
Magnesium binding site 8 out
of 8 in the E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic)
Mono view
Stereo pair view
|
A full contact list of Magnesium with other atoms in the Mg binding
site number 8 of E. Coli (Lac Z) Beta-Galactosidase (Orthorhombic) within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Mg3002
b:30.8
occ:1.00
|
O
|
D:ASP15
|
2.0
|
36.4
|
1.0
|
O
|
D:VAL21
|
2.2
|
26.0
|
1.0
|
O
|
D:ASN18
|
2.2
|
41.1
|
1.0
|
OE1
|
D:GLN163
|
2.6
|
44.7
|
1.0
|
OD2
|
D:ASP193
|
2.6
|
36.4
|
1.0
|
OD1
|
D:ASP193
|
2.7
|
32.1
|
1.0
|
CG
|
D:ASP193
|
3.0
|
30.4
|
1.0
|
NE2
|
D:GLN163
|
3.0
|
1.0
|
1.0
|
C
|
D:ASN18
|
3.1
|
35.5
|
1.0
|
CD
|
D:GLN163
|
3.2
|
42.2
|
1.0
|
C
|
D:ASP15
|
3.2
|
35.8
|
1.0
|
C
|
D:VAL21
|
3.4
|
30.7
|
1.0
|
N
|
D:ASN18
|
3.6
|
46.2
|
1.0
|
CA
|
D:ASN18
|
3.8
|
40.1
|
1.0
|
N
|
D:PRO19
|
3.9
|
24.9
|
1.0
|
CA
|
D:TRP16
|
4.0
|
13.8
|
1.0
|
N
|
D:TRP16
|
4.0
|
20.4
|
1.0
|
N
|
D:VAL21
|
4.1
|
35.3
|
1.0
|
CA
|
D:PRO19
|
4.1
|
25.0
|
1.0
|
OH
|
D:TYR161
|
4.2
|
26.5
|
1.0
|
CB
|
D:ASN18
|
4.2
|
24.0
|
1.0
|
CA
|
D:VAL21
|
4.2
|
29.2
|
1.0
|
C
|
D:TRP16
|
4.2
|
30.4
|
1.0
|
CA
|
D:ASP15
|
4.3
|
38.5
|
1.0
|
N
|
D:GLU17
|
4.3
|
33.4
|
1.0
|
N
|
D:THR22
|
4.4
|
29.1
|
1.0
|
CB
|
D:ASP193
|
4.4
|
37.4
|
1.0
|
C
|
D:PRO19
|
4.5
|
47.9
|
1.0
|
CB
|
D:VAL21
|
4.5
|
27.5
|
1.0
|
CA
|
D:THR22
|
4.6
|
27.0
|
1.0
|
CE2
|
D:TYR161
|
4.6
|
29.9
|
1.0
|
CB
|
D:ASP15
|
4.7
|
40.4
|
1.0
|
CG
|
D:GLN163
|
4.7
|
42.1
|
1.0
|
N
|
D:GLY20
|
4.8
|
37.5
|
1.0
|
C
|
D:GLU17
|
4.8
|
46.3
|
1.0
|
O
|
D:TRP16
|
4.9
|
36.1
|
1.0
|
CZ
|
D:TYR161
|
4.9
|
56.8
|
1.0
|
|
Reference:
D.H.Juers,
B.W.Matthews.
Reversible Lattice Repacking Illustrates the Temperature Dependence of Macromolecular Interactions. J.Mol.Biol. V. 311 851 2001.
ISSN: ISSN 0022-2836
PubMed: 11518535
DOI: 10.1006/JMBI.2001.4891
Page generated: Tue Aug 13 03:59:25 2024
|