DNA polymerase processivity factor activity / leading strand elongation / regulation of DNA replication / mismatch repair / translesion synthesis / DNA binding Similarity search - Function
The biological assembly is a trimer generated from the monomer in the asymmetric unit by applying the transformation matrix: [0 1 0] [0 0 1] [1 0 0] and [0 0 1] [1 0 0] [0 1 0]
Resolution: 1.8→1.86 Å / Redundancy: 93.9 % / Rmerge(I) obs: 0.263 / Mean I/σ(I) obs: 5.8 / Num. unique all: 5493 / Rsym value: 0.263 / % possible all: 96.6
-
Processing
Software
Name
Version
Classification
DENZO
datareduction
SCALEPACK
datascaling
AMoRE
phasing
CNS
1
refinement
Refinement
Method to determine structure: MOLECULAR REPLACEMENT Starting model: Model built from 2.1 angstrom resolution data phased by a single anomalous derivative (ethyl mercury phosphate) Resolution: 1.8→30 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
Rfactor
Num. reflection
Selection details
Rfree
0.238
5563
random
Rwork
0.219
-
-
all
0.221
55307
-
obs
0.221
55307
-
Refinement step
Cycle: LAST / Resolution: 1.8→30 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
1906
0
0
316
2222
Refine LS restraints
Refine-ID
Type
Dev ideal
X-RAY DIFFRACTION
x_bond_d
0.005
X-RAY DIFFRACTION
x_angle_d
1.3
X-RAY DIFFRACTION
x_torsion_deg
25.1
X-RAY DIFFRACTION
x_torsion_impr_deg
0.66
Refine LS restraints
*PLUS
Refine-ID
Type
Dev ideal
X-RAY DIFFRACTION
x_angle_d
X-RAY DIFFRACTION
x_angle_deg
1.3
+
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