6SLF

Nalpha-acylglutamine aminoacylase from Corynebacterium sp.releasing human axilla odorants co-crystallised with high affinity inhibitor

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.5	296	90microL of 30% PEG4K, 0.22M sodium acetate, 0.1M Tris pH 8.5 + 10microL of Index screen (Hampton Research) containing 0.2M ammonium sulphate, 0.1M Bis-Tris pH6.5, 25%PEG3350

Crystal Properties
Matthews coefficient	Solvent content
2.56	51.92

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 53.688	α = 90
b = 181.919	β = 104.14
c = 93.122	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	296	CCD	ADSC QUANTUM 1		2006-09-01	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID23-1	1.282	ESRF	ID23-1

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	1.5	29.58	100	0.0108	8.3	6.93		164787			33.5

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)
1	1.5	1.8	99.9		0.0418

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	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	1XMB, 1YSJ	1.75	29.58	164787	8738	99.97	0.1835	0.1821	0.2096	RANDOM	26.211

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	36.187
r_dihedral_angle_4_deg	13.454
r_dihedral_angle_3_deg	13.029
r_dihedral_angle_1_deg	5.482
r_angle_refined_deg	1.387
r_nbtor_refined	0.3
r_nbd_refined	0.201
r_symmetry_hbond_refined	0.187
r_symmetry_vdw_refined	0.149
r_xyhbond_nbd_refined	0.12

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.187
r_dihedral_angle_4_deg	13.454
r_dihedral_angle_3_deg	13.029
r_dihedral_angle_1_deg	5.482
r_angle_refined_deg	1.387
r_nbtor_refined	0.3
r_nbd_refined	0.201
r_symmetry_hbond_refined	0.187
r_symmetry_vdw_refined	0.149
r_xyhbond_nbd_refined	0.12
r_chiral_restr	0.096
r_metal_ion_refined	0.041
r_bond_refined_d	0.014
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	12137
Nucleic Acid Atoms
Solvent Atoms	1020
Heterogen Atoms	156

Software

Software
Software Name	Purpose
d*TREK	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
CrystalClear	data reduction

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.