1H2M

Factor Inhibiting HIF-1 alpha in complex with HIF-1 alpha fragment peptide


X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
17.51.2M AMMONIUM SULPHATE, 4% PEG400, 0.1M HEPES PH7.5, 11MG/ML PROTEIN WITH 1MM ZN(II), 2.5MM NOG AND 2.5MM PEPTIDE, pH 7.50
Crystal Properties
Matthews coefficientSolvent content
3.463

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 86.249α = 90
b = 86.249β = 90
c = 148.26γ = 90
Symmetry
Space GroupP 41 21 2

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC CCD2002-05-15MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONSRS BEAMLINE PX9.6SRSPX9.6

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
12.587.7199.70.0510.76.520058
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)
12.52.6497.90.2892.64.4

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 REPLACEMENTTHROUGHOUT2.51818404151699.70.1940.1920.225RANDOM35.78
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]
-0.68-0.681.35
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_3_deg18.015
r_dihedral_angle_1_deg4.024
r_scangle_it3.678
r_scbond_it2.22
r_angle_refined_deg1.612
r_mcangle_it1.421
r_angle_other_deg0.832
r_mcbond_it0.761
r_symmetry_vdw_other0.255
r_symmetry_hbond_refined0.244
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_3_deg18.015
r_dihedral_angle_1_deg4.024
r_scangle_it3.678
r_scbond_it2.22
r_angle_refined_deg1.612
r_mcangle_it1.421
r_angle_other_deg0.832
r_mcbond_it0.761
r_symmetry_vdw_other0.255
r_symmetry_hbond_refined0.244
r_nbd_refined0.232
r_nbd_other0.214
r_symmetry_vdw_refined0.194
r_xyhbond_nbd_refined0.173
r_xyhbond_nbd_other0.126
r_chiral_restr0.097
r_metal_ion_refined0.054
r_symmetry_hbond_other0.053
r_bond_refined_d0.017
r_gen_planes_refined0.006
r_gen_planes_other0.002
r_bond_other_d0.001
r_dihedral_angle_2_deg
r_dihedral_angle_4_deg
r_nbtor_refined
r_nbtor_other
r_metal_ion_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 Atoms2859
Nucleic Acid Atoms
Solvent Atoms99
Heterogen Atoms21

Software

Software
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling