4LC4

Crystal structure of probable sugar kinase protein from Rhizobium Etli CFN 42 complexed with guanosine

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	4E3A	PDB ENTRY 4E3A

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	6.5	298	0.2M AMMONIUM ACETATE, 0.1M BIS:TRIS:HCL, PH 6.5,25% PEG3350, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.2	44.02

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 51.221	�� = 90
b = 80.879	�� = 98.4
c = 83.323	�� = 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		2013-04-26		SAD

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	NSLS BEAMLINE X29A	1.075	NSLS	X29A

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	1.6	50	97.7	0.083	7	3.6		86474

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	1.6	1.63	78.4		0.876		2.4	3458

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	PDB ENTRY 4E3A	1.7	42.94	73700	3747	99.74	0.1861	0.1833	0.2383	RANDOM	26.8984

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]
-8.47		-10.84	-6.48		14.95

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.748
r_sphericity_free	30.997
r_dihedral_angle_4_deg	12.719
r_dihedral_angle_3_deg	12.258
r_sphericity_bonded	11.383
r_dihedral_angle_1_deg	5.277
r_scbond_it	3.114
r_mcangle_it	2.432
r_rigid_bond_restr	2.239
r_mcbond_it	1.924

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.748
r_sphericity_free	30.997
r_dihedral_angle_4_deg	12.719
r_dihedral_angle_3_deg	12.258
r_sphericity_bonded	11.383
r_dihedral_angle_1_deg	5.277
r_scbond_it	3.114
r_mcangle_it	2.432
r_rigid_bond_restr	2.239
r_mcbond_it	1.924
r_angle_refined_deg	1.396
r_chiral_restr	0.15
r_bond_refined_d	0.008
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	5008
Nucleic Acid Atoms
Solvent Atoms	689
Heterogen Atoms	96

Software

Software
Software Name	Purpose
SCALEPACK	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
CBASS	data collection
HKL-2000	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 R01GM157729.