3DXV

The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.7	293	25% PEG4000, 0.17M magnesium chloride, 0.08M Tris/HCl (pH8.7), 5% Sucrose, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
1.86	33.85

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 56.547	α = 90
b = 61.063	β = 103.22
c = 105.227	γ = 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	ADSC QUANTUM 315		2008-03-14	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSRRC BEAMLINE BL13B1	1.0	NSRRC	BL13B1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	R Sym 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	2.21	50	99.6	0.108	0.074		5.9		35281

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.21	2.29	98.2		0.494	0.429		5.2

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	PDB ENTRY 1SFT	2.21	19.96	35281	33451	1765	99.63	0.19976	0.19734	0.24522	RANDOM	30.541

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]

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.533
r_dihedral_angle_4_deg	19.198
r_dihedral_angle_3_deg	17.617
r_dihedral_angle_1_deg	5.463
r_scangle_it	2.197
r_scbond_it	1.324
r_angle_refined_deg	1.274
r_mcangle_it	0.907
r_mcbond_it	0.528
r_nbtor_refined	0.302

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.533
r_dihedral_angle_4_deg	19.198
r_dihedral_angle_3_deg	17.617
r_dihedral_angle_1_deg	5.463
r_scangle_it	2.197
r_scbond_it	1.324
r_angle_refined_deg	1.274
r_mcangle_it	0.907
r_mcbond_it	0.528
r_nbtor_refined	0.302
r_symmetry_vdw_refined	0.205
r_nbd_refined	0.2
r_xyhbond_nbd_refined	0.149
r_symmetry_hbond_refined	0.115
r_chiral_restr	0.08
r_bond_refined_d	0.009
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	6325
Nucleic Acid Atoms
Solvent Atoms	120
Heterogen Atoms	30

Software

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

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 R01GM133198.