5TEN

Structure of 4-Hydroxy-tetrahydrodipicolinate Reductase from Vibrio vulnificus with 2,5 Furan Dicarboxylic and NADH with Intact Polyhistidine Tag

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP		298	100 mM HEPES pH 7, 1.26 M Ammonium Sulfate

Crystal Properties
Matthews coefficient	Solvent content
2.1	46.63

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 68.439	α = 90
b = 117.545	β = 92.19
c = 131.524	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	MARMOSAIC 300 mm CCD		2013-06-23	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 22-ID	1	APS	22-ID

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	2.45	50	96.9	0.131	0.131	6.1	3.1		74404

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	CC (Half)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.45	2.49	96.5		0.723	0.798	2.1	3

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	1ARZ	2.45	50	70349	3712	96.86	0.2243	0.2226	0.2553	RANDOM	49.427

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]
-2		-0.28	-2.83		4.85

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.604
r_dihedral_angle_4_deg	23.099
r_dihedral_angle_3_deg	13.761
r_dihedral_angle_1_deg	6.304
r_angle_other_deg	3.906
r_mcangle_it	2.394
r_angle_refined_deg	1.864
r_mcbond_it	1.408
r_mcbond_other	1.407
r_chiral_restr	0.097

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	35.604
r_dihedral_angle_4_deg	23.099
r_dihedral_angle_3_deg	13.761
r_dihedral_angle_1_deg	6.304
r_angle_other_deg	3.906
r_mcangle_it	2.394
r_angle_refined_deg	1.864
r_mcbond_it	1.408
r_mcbond_other	1.407
r_chiral_restr	0.097
r_bond_refined_d	0.018
r_gen_planes_other	0.013
r_gen_planes_refined	0.009
r_bond_other_d

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	15654
Nucleic Acid Atoms
Solvent Atoms	218
Heterogen Atoms	535

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-3000	data reduction
HKL-3000	data scaling
HKL-3000	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.