|
Parameters
|
Wild type
|
D61G
|
E139D
|
Y279C
|
N308D
|
Q506P
|
|---|
|
Data collection:
|
|
Resolution, (Å)
|
2.75
|
2.20
|
2.45
|
2.10
|
2.10
|
2.70
|
|
Outermost resolution shell, (Å)
|
(2.85-2.75)
|
(2.30-2.20)
|
(2.55-2.45)
|
(2.20-2.10)
|
(2.20-2.10)
|
(2.80-2.70)
|
|
Space group
|
P21
|
P21212
|
P212121
|
P21
|
P212121
|
P21212
|
|
Unit cell parameters
|
|
a, (Å)
|
55.7
|
55.0
|
56.3
|
55.7
|
55.9
|
54.8
|
|
b, (Å)
|
211.7
|
220.3
|
212.4
|
212.0
|
211.2
|
202.4
|
|
c, (Å)
|
91.2
|
41.7
|
92.2
|
46.0
|
91.6
|
44.5
|
|
β, (°)
|
89.97
| | |
96.6
| | |
|
Molecules per asymmetric unit
|
4
|
1
|
2
|
2
|
2
|
1
|
|
Unique reflections
|
53,849
|
26,689
|
41,625
|
61,515
|
64,401
|
14,342
|
|
Multiplicity
|
3.1 (3.4)
|
6.3 (6.1)
|
6.5 (6.3)
|
3.5 (3.5)
|
7.0 (7.2)
|
6.5 (6.3)
|
|
Average I/σ (I)
|
5.5 (2.2)
|
11.1 (2.7)
|
9.2 (2.3)
|
6.9 (1.9)
|
11.0 (3.2)
|
12.0 (2.8)
|
|
R
merge
, (%)
|
18.9 (46.0)
|
10.6 (52.0)
|
11.4 (57.1)
|
10.4 (49.7)
|
9.4 (43.0)
|
13.9 (56.0)
|
|
Completeness, (%)
|
95.9 (98.5)
|
99.3 (96.2)
|
99.7 (98.1)
|
99.9 (99.6)
|
99.9 (100)
|
99.9 (100)
|
|
Refinement and structure statistics
|
|
R
work
, (%)
|
25.6
|
21.1
|
21.3
|
21.1
|
24.2
|
22.7
|
|
R
free
, (%)
|
28.5
|
23.3
|
25.4
|
24.3
|
28.7
|
24.2
|
|
RMSD from ideal geometry
|
|
Bond lengths, (Å)
|
0.007
|
0.007
|
0.010
|
0.008
|
0.009
|
0.007
|
|
Bond angles, (°)
|
0.91
|
0.99
|
1.24
|
1.00
|
1.10
|
0.91
|
|
Numbers of atoms
|
|
Protein (non-hydrogen)
|
15,560
|
4,021
|
8,214
|
8,013
|
8,100
|
3,951
|
|
Water oxygen atoms
|
784
|
134
|
365
|
261
|
679
|
54
|
|
Ligand’s atoms
| |
20
| |
90
| |
36
|
|
PDB ID
|
4NXD
|
4H10
|
4NWG
|
4GWF
|
4NWF
|
4H34
|
- R
merge
= ∑
hkl
|I − 〈I〉|/∑
hkl
I, where I is the intensity of the individual reflections.
- R
work
= ∑ |F
obs
− F
cal
|/∑|F
obs
, where Fobs and Fcalc are the observed and the calculated structure factors, respectively.
- R
free
was calculated using 5% of total reflections randomly chosen and excluded from the crystallographic refinement.
