1SMI

A single mutation of P450 BM3 induces the conformational rearrangement seen upon substrate-binding in wild-type enzyme

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1JPZ

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.3	277	PEG 2000, MME, 10mM Manganese sulphate, pH 6.3, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.47	49.8

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 61.206	α = 90
b = 118.929	β = 90
c = 146.338	γ = 90

Symmetry
Space Group	P 21 21 21

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	ADSC QUANTUM 4		2003-08-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID14-1	0.900	ESRF	ID14-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (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	2	15	94	0.051	28.2		68550	68550

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
	2	2.07	97.1		0.441	2.41

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	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	1JPZ	2	14.92	65010	65010	3440	100	0.22699	0.22699	0.22376	0.28831	RANDOM	45.945

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]
			0.01		-0.01

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.33
r_dihedral_angle_3_deg	17.131
r_dihedral_angle_4_deg	16.963
r_dihedral_angle_1_deg	6.906
r_scangle_it	3.719
r_scbond_it	2.568
r_angle_refined_deg	1.719
r_mcangle_it	1.683
r_mcbond_it	1.125
r_nbd_refined	0.239

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.33
r_dihedral_angle_3_deg	17.131
r_dihedral_angle_4_deg	16.963
r_dihedral_angle_1_deg	6.906
r_scangle_it	3.719
r_scbond_it	2.568
r_angle_refined_deg	1.719
r_mcangle_it	1.683
r_mcbond_it	1.125
r_nbd_refined	0.239
r_xyhbond_nbd_refined	0.187
r_symmetry_vdw_refined	0.172
r_symmetry_hbond_refined	0.151
r_chiral_restr	0.114
r_bond_refined_d	0.018
r_metal_ion_refined	0.013
r_gen_planes_refined	0.007

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	7124
Nucleic Acid Atoms
Solvent Atoms	492
Heterogen Atoms	86

Software

Software
Software Name	Purpose
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	phasing
REFMAC	refinement

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.