Table 4 Data collection and refinement statistics of HvExoI E220A structures in apo (unliganded)-form, and in-complex with glucose (Glc) and the mechanism-based inhibitor 2F-DNPGlc

From: The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase

 

E220A Apo

E220A Glc bound

E220A 2F-DNPGlc bound

PDB accession

8HJ6

8HJ7

8HJ8

Data collection

Space group

P43212

P43212

P43212

Number of molecules/ASU

1

1

1

Cell dimensions

 a, b, c (Å)

100.23, 100.23, 183.17

100.63, 100.63, 182.32

100.50, 100.50, 182.69

 α, β, γ (°)

90, 90, 90

90, 90, 90

90, 90, 90

Resolution (Å)

87.93–1.79 (1.84–1.79)a

88.10–1.85 (1.90–1.85)

88.06–1.95 (2.00–1.95)

Rmerge (%)b

9.6 (83.5)

9.4 (82.3)

9.2 (80.0)

I /σI

48.6 (2.3)

50.8 (2.3)

38.7 (3.0)

Completeness (%)

95.3 (68.3)

98.0 (80.0)

100 (100)

Redundancy

24.8

26.0

28.2

CC1/2 (%)

99.8

99.8

99.7

Refinement

Resolution (Å)

87.93–1.79

88.10–1.85

88.06–1.95

No. reflections

79,237

74,941

64,685

Rwork/Rfree

0.155/0.187

0.175/0.205

0.154/0.184

No. of atoms

5313

5300

5270

 Protein

4618

4577

4618

 Ligand/ion

0

24

23

 Water

695

699

629

B-factors

27.86

38.03

32.58

 Protein

70.03

35.48

30.19

 Ligand

–

44.84

40.50

 Water

37.94

49.79

41.72

RMSD values

 Bond lengths (Å)

0.021

0.009

0.024

 Bond angles (°)

1.661

1.159

1.818

  1. aValues in parentheses are for the highest resolution shell.
  2. bRmerge = 100 [∑(Ii− <I > )2/∑Ii2], summed over all (highest shell) independent reflections.
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