1UNL

Structural mechanism for the inhibition of CD5-p25 from the roscovitine, aloisine and indirubin.


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
1713% PEG 3350, 0.1 M KI, 0.1 M BISTRISPROPANE PH 7.0, 10 MM DTT
Crystal Properties
Matthews coefficientSolvent content
2.856

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 117.988α = 90
b = 117.988β = 90
c = 156.167γ = 120
Symmetry
Space GroupP 32 2 1

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray287CCDADSC CCD2002-09-15MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONESRF BEAMLINE ID14-2ESRFID14-2

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
12.22594.60.0118.98.8648182.5
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)
12.22.397.70.372.83

Refinement

Statistics
Diffraction IDStructure Solution MethodCross Validation methodStarting modelResolution (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 REPLACEMENTTHROUGHOUT1H4L2.219.7657534305794.40.2160.2160.219RANDOM23.02
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]
0.350.170.35-0.52
RMS Deviations
KeyRefinement Restraint Deviation
r_chiral_restr6.273
r_dihedral_angle_3_deg3.71
r_scangle_it2.899
r_scbond_it1.885
r_angle_other_deg1.541
r_mcangle_it1.159
r_mcbond_it0.659
r_symmetry_vdw_other0.348
r_symmetry_vdw_refined0.292
r_nbd_other0.27
RMS Deviations
KeyRefinement Restraint Deviation
r_chiral_restr6.273
r_dihedral_angle_3_deg3.71
r_scangle_it2.899
r_scbond_it1.885
r_angle_other_deg1.541
r_mcangle_it1.159
r_mcbond_it0.659
r_symmetry_vdw_other0.348
r_symmetry_vdw_refined0.292
r_nbd_other0.27
r_xyhbond_nbd_refined0.238
r_symmetry_hbond_refined0.208
r_nbd_refined0.205
r_nbtor_other0.113
r_bond_refined_d0.016
r_gen_planes_other0.008
r_gen_planes_refined0.006
r_bond_other_d
r_angle_refined_deg
r_dihedral_angle_1_deg
r_dihedral_angle_2_deg
r_dihedral_angle_4_deg
r_nbtor_refined
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_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 Atoms7096
Nucleic Acid Atoms
Solvent Atoms302
Heterogen Atoms26

Software

Software
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
AMoREphasing