4GPH

Structure of HmuO, heme oxygenase from Corynebacterium diphtheriae, in complex with the putative reaction intermediates between Fe3+-biliverdin and biliverdin (data set IV)

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	6.1	303	ammonium sulfate, MES, pH 6.1, VAPOR DIFFUSION, temperature 303K

Crystal Properties
Matthews coefficient	Solvent content
2.48	50.49

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 54.065	�� = 90
b = 62.966	�� = 100.78
c = 107.728	�� = 90

Symmetry
Space Group	P 1 21 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	CCD	RIGAKU JUPITER 210		2005-04-20	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SPRING-8 BEAMLINE BL38B1	1.0	SPring-8	BL38B1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	Net I Over Average Sigma (I)	Redundancy	Number Reflections (All)	Number Reflections (Observed)	Observed Criterion Sigma (F)	Observed Criterion Sigma (I)	B (Isotropic) From Wilson Plot
1	1.7	50	98.7			78377	77319

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.7	1.76	95.3

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Number Reflections (All)	Number Reflections (Observed)	Number Reflections (R-Free)	Percent Reflections (Observed)	R-Factor (All)	R-Factor (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	1.7	30	70408	69486	7805	98.69	0.16934	0.16934	0.16521	0.20547	RANDOM	29.928

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]
-0.38		0.37	0.73		-0.22

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.476
r_dihedral_angle_4_deg	18.332
r_dihedral_angle_3_deg	14.25
r_scangle_it	5.553
r_dihedral_angle_1_deg	5.352
r_scbond_it	3.591
r_angle_refined_deg	2.336
r_mcangle_it	2.258
r_mcbond_it	1.388
r_chiral_restr	0.171

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	33.476
r_dihedral_angle_4_deg	18.332
r_dihedral_angle_3_deg	14.25
r_scangle_it	5.553
r_dihedral_angle_1_deg	5.352
r_scbond_it	3.591
r_angle_refined_deg	2.336
r_mcangle_it	2.258
r_mcbond_it	1.388
r_chiral_restr	0.171
r_bond_refined_d	0.028
r_gen_planes_refined	0.027

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4961
Nucleic Acid Atoms
Solvent Atoms	473
Heterogen Atoms	183

Software

Software
Software Name	Purpose
HKL-2000	data collection
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.