3QRJ

The crystal structure of human abl1 kinase domain T315I mutant in complex with DCC-2036


X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
TypeSourceAccession CodeDetails
otherAbl kinase

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1VAPOR DIFFUSION, SITTING DROP7.129029% PEG 3350, 100MM BISTRIS PH 7.1, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K
Crystal Properties
Matthews coefficientSolvent content
1.8433.06

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 55.261α = 90
b = 59.435β = 109.55
c = 76.285γ = 90
Symmetry
Space GroupP 1 21 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC QUANTUM 315r2006-10-03MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONALS BEAMLINE 5.0.21.0000ALS5.0.2

Data Collection

Overall
ID #Resolution (High)Resolution (Low)Percent Possible (Observed)R Sym 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
11.822096.50.08716.1433554183820
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)
11.821.8980.40.4082.2

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (High)Resolution (Low)Number Reflections (All)Number Reflections (Observed)Number Reflections (R-Free)Percent Reflections (Observed)R-Factor (All)R-Factor (Observed)R-WorkR-FreeR-Free Selection DetailsMean Isotropic B
X-RAY DIFFRACTIONMOLECULAR REPLACEMENTTHROUGHOUTAbl kinase1.8219.59433554036020350.2320.2320.2290.286RANDOM16.58
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]
-0.060.020.11-0.04
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg39.157
r_dihedral_angle_4_deg17.169
r_dihedral_angle_3_deg15.626
r_dihedral_angle_1_deg7.022
r_scangle_it3.351
r_scbond_it2.248
r_angle_refined_deg1.724
r_mcangle_it1.463
r_angle_other_deg0.978
r_mcbond_it0.864
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg39.157
r_dihedral_angle_4_deg17.169
r_dihedral_angle_3_deg15.626
r_dihedral_angle_1_deg7.022
r_scangle_it3.351
r_scbond_it2.248
r_angle_refined_deg1.724
r_mcangle_it1.463
r_angle_other_deg0.978
r_mcbond_it0.864
r_mcbond_other0.233
r_chiral_restr0.092
r_bond_refined_d0.016
r_gen_planes_refined0.007
r_gen_planes_other0.002
r_bond_other_d0.001
r_nbd_refined
r_nbd_other
r_nbtor_refined
r_nbtor_other
r_xyhbond_nbd_refined
r_xyhbond_nbd_other
r_metal_ion_refined
r_metal_ion_other
r_symmetry_vdw_refined
r_symmetry_vdw_other
r_symmetry_hbond_refined
r_symmetry_hbond_other
r_symmetry_metal_ion_refined
r_symmetry_metal_ion_other
r_rigid_bond_restr
r_sphericity_free
r_sphericity_bonded
Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen AtomsNumber
Protein Atoms4128
Nucleic Acid Atoms
Solvent Atoms243
Heterogen Atoms82

Software

Software
Software NamePurpose
BOSdata collection
MOLREPphasing
REFMACrefinement
HKL-2000data reduction
HKL-2000data scaling