4CDT

Structure of rat neuronal nitric oxide synthase heme domain in complex with 7-((3-Fluorophenethylamino)ethyl)quinolin-2-amine


X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
TypeSourceAccession CodeDetails
experimental modelPDB 1OM4PDB ENTRY 1OM4

Crystallization

Crystalization Experiments
IDMethodpHTemperatureDetails
15.820-24% PEG3350, 0.1 MES PH5.8, 140-200MM AMMONIUM ACETATE, 10% ETHYLENE GLYCOL, 5MM GSH, 30UM SD
Crystal Properties
Matthews coefficientSolvent content
2.2544.8

Crystal Data

Unit Cell
Length ( Å )Angle ( ˚ )
a = 52.37α = 90
b = 111.82β = 90
c = 165.45γ = 90
Symmetry
Space GroupP 21 21 21

Diffraction

Diffraction Experiment
ID #Crystal IDScattering TypeData Collection TemperatureDetectorDetector TypeDetailsCollection DateMonochromatorProtocol
11x-ray100CCDADSC QUANTUM 315rMIRRORS2013-11-01MSINGLE WAVELENGTH
Radiation Source
ID #SourceTypeWavelength ListSynchrotron SiteBeamline
1SYNCHROTRONALS BEAMLINE 8.2.2ALS8.2.2

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
125096.20.1115.33.662187-329
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)
122.0783.60.661.12.6

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 REPLACEMENTTHROUGHOUTPDB ENTRY 1OM4292.6558610306192.410.19850.19590.2469RANDOM49.64
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]
0.931.39-2.33
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.572
r_dihedral_angle_3_deg18.068
r_dihedral_angle_4_deg17.485
r_dihedral_angle_1_deg6.544
r_mcangle_it3.342
r_scbond_it3.16
r_mcbond_it2.293
r_angle_refined_deg1.879
r_chiral_restr0.135
r_bond_refined_d0.016
RMS Deviations
KeyRefinement Restraint Deviation
r_dihedral_angle_2_deg35.572
r_dihedral_angle_3_deg18.068
r_dihedral_angle_4_deg17.485
r_dihedral_angle_1_deg6.544
r_mcangle_it3.342
r_scbond_it3.16
r_mcbond_it2.293
r_angle_refined_deg1.879
r_chiral_restr0.135
r_bond_refined_d0.016
r_gen_planes_refined0.01
r_bond_other_d
r_angle_other_deg
r_gen_planes_other
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_mcbond_other
r_mcangle_other
r_scbond_other
r_scangle_it
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 Atoms6659
Nucleic Acid Atoms
Solvent Atoms183
Heterogen Atoms175

Software

Software
Software NamePurpose
REFMACrefinement
HKL-2000data reduction
SCALEPACKdata scaling
REFMACphasing