2WA8

Structural basis of N-end rule substrate recognition in Escherichia coli by the ClpAP adaptor protein ClpS - The Phe peptide structure


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
18.5pH 8.5
Crystal Properties
Matthews coefficientSolvent content
2.145

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 32.223α = 90
b = 58.405β = 101.89
c = 56.413γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray90CCDMARRESEARCHMSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONSLS BEAMLINE X10SASLSX10SA

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Merge I (Observed)Net I Over Average Sigma (I)RedundancyNumber Reflections (All)Number Reflections (Observed)Observed Criterion Sigma (F)Observed Criterion Sigma (I)B (Isotropic) From Wilson Plot
12.1530940.016.62.8107282.3
Highest Resolution Shell
ID #Resolution (High)Resolution (Low)Percent Possible (All)Percent Possible (Observed)R Merge I (Observed)Mean I Over Sigma (Observed)RedundancyNumber Unique Reflections (All)
12.152.2790.50.452.32.7

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodResolution (High)Resolution (Low)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT2.152099097471000.2280.2250.268RANDOM33.16
Temperature Factor Modeling
Anisotropic B[1][1]Anisotropic B[1][2]Anisotropic B[1][3]Anisotropic B[2][2]Anisotropic B[2][3]Anisotropic B[3][3]
-1.130.162.02-0.82
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg39.623
r_dihedral_angle_4_deg21.084
r_dihedral_angle_3_deg19.12
r_scangle_it10.417
r_scbond_it7.258
r_dihedral_angle_1_deg6.932
r_mcangle_it6.323
r_mcbond_it4.92
r_angle_refined_deg1.542
r_nbtor_refined0.334
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg39.623
r_dihedral_angle_4_deg21.084
r_dihedral_angle_3_deg19.12
r_scangle_it10.417
r_scbond_it7.258
r_dihedral_angle_1_deg6.932
r_mcangle_it6.323
r_mcbond_it4.92
r_angle_refined_deg1.542
r_nbtor_refined0.334
r_symmetry_vdw_refined0.316
r_nbd_refined0.288
r_symmetry_hbond_refined0.181
r_xyhbond_nbd_refined0.152
r_chiral_restr0.119
r_bond_refined_d0.01
r_gen_planes_refined0.007
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
r_nbd_other
r_nbtor_other
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_mcbond_other
r_mcangle_other
r_scbond_other
r_scangle_other
r_long_range_B_refined
r_long_range_B_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms1660
Nucleic Acid Atoms
Solvent Atoms91
Heterogen Atoms

Software

Software
Software NamePurpose
REFMACrefinement
XDSdata reduction
XDSdata scaling
MOLREPphasing