1TUG

Aspartate Transcarbamoylase Catalytic Chain Mutant E50A Complex with Phosphonoacetamide, Malonate, and Cytidine-5-Prime-Triphosphate (CTP)

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
other		UNPUBLISHED

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1		6	295	100 mM sodium citrate, 1 mM 2-mercaptoethanol, 0.2 mM EDTA and 1.0 mM CTP pH 6.0 then soaked for 24 hours in 100 mM malonate, 2 mM CTP, 3 mM sodium azide, 2 mM 2-mercaptoethanol, and 15% PEG 8000 pH 7.0. Before mounting, 50 mM PAM was added and the crystal allowed to soak until data collected., MICRODIALYSIS, temperature 295K, pH 6.00

Crystal Properties
Matthews coefficient	Solvent content
2.23	44.9

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 122.29	α = 90
b = 122.29	β = 90
c = 142.41	γ = 120

Symmetry
Space Group	P 3 2 1

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	298	AREA DETECTOR	UCSD MARK III		1997-12-31	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RU200

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	2.1	30	88.4	0.1	6.41	3.5		67173

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)
	2.1	2.2	68.1		0.43	1.09	1.09

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X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	FREE R	UNPUBLISHED	2.1	30	66971	66971	3356	88.1	0.2298	0.2196		0.2719	RANDOM

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]

Coordinate Error
Structure Solution Method	Refinement High Resolution	Refinement Low Resolution
		7994.05

RMS Deviations
Key	Refinement Restraint Deviation
s_similar_adp_cmpnt	0.12
s_non_zero_chiral_vol	0.034
s_from_restr_planes	0.025
s_zero_chiral_vol	0.025
s_angle_d	0.024
s_anti_bump_dis_restr	0.016
s_bond_d	0.006
s_similar_dist
s_rigid_bond_adp_cmpnt
s_approx_iso_adps

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	7224
Nucleic Acid Atoms
Solvent Atoms	698
Heterogen Atoms	90

Software

Software
Software Name	Purpose
SHELX	model building
SHELXL-97	refinement
SDMS	data reduction
SDMS	data scaling
X-PLOR	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.