1NX9

Acetobacter turbidans alpha-amino acid ester hydrolase S205A mutant complexed with ampicillin

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.6	293	PEG 4000, sodium citrate buffer, sodium ampicillin, pH 5.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 341.828	�� = 90
b = 341.828	�� = 90
c = 341.828	�� = 90

Symmetry
Space Group	I 2 3

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	100	IMAGE PLATE	MARRESEARCH	premirror, triangular monochromator, bent mirror	2002-11-18	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	EMBL/DESY, HAMBURG BEAMLINE BW7B	0.8463	EMBL/DESY, HAMBURG	BW7B

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.2	99	97.2	0.081	14.3	4.5	322911	322911	1	1

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.2	2.28	98.9		0.322

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Resolution (High)	Resolution (Low)	Cut-off Sigma (F)	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	2.2	15	1	322911	304675	16078	96.9	0.16698	0.16618	0.16608	0.18386	RANDOM	22.609

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_scangle_it	5.286
r_scbond_it	3.642
r_mcangle_it	2.212
r_dihedral_angle_1_deg	2.21
r_mcbond_it	1.309
r_angle_refined_deg	1.064
r_nbd_refined	0.172
r_symmetry_hbond_refined	0.148
r_symmetry_vdw_refined	0.121
r_xyhbond_nbd_refined	0.101

RMS Deviations
Key	Refinement Restraint Deviation
r_scangle_it	5.286
r_scbond_it	3.642
r_mcangle_it	2.212
r_dihedral_angle_1_deg	2.21
r_mcbond_it	1.309
r_angle_refined_deg	1.064
r_nbd_refined	0.172
r_symmetry_hbond_refined	0.148
r_symmetry_vdw_refined	0.121
r_xyhbond_nbd_refined	0.101
r_chiral_restr	0.075
r_bond_refined_d	0.007
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	19528
Nucleic Acid Atoms
Solvent Atoms	2229
Heterogen Atoms	120

Software

Software
Software Name	Purpose
REFMAC	refinement
DENZO	data reduction
SCALEPACK	data scaling
AMoRE	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 R01GM157729.