Resolution: 2.2→2.28 Å / Redundancy: 2.2 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 2.1 / Num. unique all: 1775 / % possible all: 95.5
-
Processing
Software
Name
Version
Classification
StructureStudio
datacollection
MOLREP
phasing
CNS
1.1
refinement
HKL-2000
datareduction
SCALEPACK
datascaling
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: Homology built model from human, AF and MJ IMPases Resolution: 2.2→42 Å / Isotropic thermal model: Isotropic / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.279
1815
-
RANDOM
Rwork
0.207
-
-
-
obs
0.209
46203
93.5 %
-
all
-
49804
-
-
Displacement parameters
Biso mean: 45.3 Å2
Baniso -1
Baniso -2
Baniso -3
1-
-2.533 Å2
0 Å2
-0.993 Å2
2-
-
9.616 Å2
0 Å2
3-
-
-
-7.083 Å2
Refinement step
Cycle: LAST / Resolution: 2.2→42 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
8084
0
4
302
8390
Refine LS restraints
Refine-ID
Type
Dev ideal
X-RAY DIFFRACTION
c_bond_d
0.007
X-RAY DIFFRACTION
c_angle_deg
1.367
LS refinement shell
Resolution: 2.2→2.3 Å
Rfactor
Num. reflection
Rfree
0.379
241
Rwork
0.339
-
obs
-
4916
+
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