4TPT

Crystal Structure of the Human LIMK2 Kinase Domain In Complex With a Non-ATP Competitive Inhibitor


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1BATCH MODE293The purified protein was used in crystallisation trials employing both, a standard screen with approximately 1200 different conditions, as well as crystallisation conditions identified using literature data.
Crystal Properties
Matthews coefficientSolvent content
2.4650.08

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 51.569α = 90
b = 77.903β = 100.84
c = 86.387γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100PIXELDECTRIS PILATUS 6M2010-08-25MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONSLS BEAMLINE X06SA1.0000SLSX06SA

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
12.684.8297.60.0533.920794
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)
12.62.7787.80.7243.4

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 REPLACEMENTTHROUGHOUT2.684.821940991997.810.222940.220460.27413RANDOM49.389
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]
-0.9-2.53-2.082.03
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.888
r_dihedral_angle_4_deg16.812
r_dihedral_angle_3_deg13.244
r_dihedral_angle_1_deg5.075
r_scangle_it2.803
r_scbond_it1.895
r_mcangle_it1.338
r_mcbond_it1.048
r_angle_refined_deg0.932
r_angle_other_deg0.719
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg34.888
r_dihedral_angle_4_deg16.812
r_dihedral_angle_3_deg13.244
r_dihedral_angle_1_deg5.075
r_scangle_it2.803
r_scbond_it1.895
r_mcangle_it1.338
r_mcbond_it1.048
r_angle_refined_deg0.932
r_angle_other_deg0.719
r_nbd_refined0.2
r_nbtor_refined0.175
r_mcbond_other0.174
r_nbd_other0.159
r_symmetry_vdw_other0.124
r_xyhbond_nbd_refined0.118
r_symmetry_vdw_refined0.104
r_nbtor_other0.078
r_chiral_restr0.056
r_symmetry_hbond_refined0.035
r_bond_refined_d0.006
r_gen_planes_refined0.002
r_bond_other_d0.001
r_gen_planes_other0.001
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_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 Atoms4417
Nucleic Acid Atoms
Solvent Atoms30
Heterogen Atoms62

Software

Software
Software NamePurpose
REFMACrefinement