3ZU5 | pdb_00003zu5

Structure of the enoyl-ACP reductase FabV from Yersinia pestis with the cofactor NADH and the 2-pyridone inhibitor PT173


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
137% PEG 4000, 150 MM AMMONIUM SULFATE, 100 MM MES PH 5.5.
Crystal Properties
Matthews coefficientSolvent content
2.8156

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 101.77α = 90
b = 101.77β = 90
c = 84.55γ = 120
Symmetry
Space GroupP 31 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100IMAGE PLATERIGAKU RAXIS HTCMSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1ROTATING ANODERIGAKU MICROMAX-007 HF

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
1242.21000.0813.15.9345592.5

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-Work (Depositor)R-Work (DCC)R-Free (Depositor)R-Free (DCC)R-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUT238.1232761173999.90.189410.187310.20.228390.24RANDOM43.933
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]
1.410.711.41-2.12
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg38.272
r_dihedral_angle_4_deg20.638
r_dihedral_angle_3_deg14.355
r_dihedral_angle_1_deg5.982
r_scangle_it3.89
r_scbond_it2.439
r_mcangle_it1.511
r_angle_refined_deg1.51
r_mcbond_it0.822
r_chiral_restr0.098
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms3091
Nucleic Acid Atoms
Solvent Atoms214
Heterogen Atoms67

Software

Software
Software NamePurpose
REFMACrefinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing