Experiment: 2QFL

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	Other		Model constructed from the consensus sequences of human, MJ0109 and AF2372 enzymes

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.1	298	20% PEG 3350, 0.2M ammonium acetate, 0.05M TRIS, pH 7.1, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystal Properties
Matthews coefficient	Solvent content
2.05	39.92

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 89.767	�� = 90
b = 45.447	�� = 125.43
c = 71.758	�� = 90

Symmetry
Space Group	C 1 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	110	IMAGE PLATE	RIGAKU RAXIS HTC	Osmic blue confocal	2006-11-11	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU FR-E+ DW	1.5418

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	1.82	47	95	0.05	19.9	3.3	15955	15115			25

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)
	1.9	1.97	36		0.27	4.1	2.6	740

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	Hybrid of human and MJ IMPase	1.9	47	15113	15113	830	94.97	0.21331	0.20922	0.28555	RANDOM	40.195

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]
0.97		-1.58	0.35		-3.16

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.111
r_dihedral_angle_4_deg	17.369
r_dihedral_angle_3_deg	16.895
r_dihedral_angle_1_deg	7.449
r_scangle_it	4.234
r_scbond_it	2.784
r_mcangle_it	2.087
r_angle_refined_deg	1.851
r_mcbond_it	1.288
r_nbtor_refined	0.314

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.111
r_dihedral_angle_4_deg	17.369
r_dihedral_angle_3_deg	16.895
r_dihedral_angle_1_deg	7.449
r_scangle_it	4.234
r_scbond_it	2.784
r_mcangle_it	2.087
r_angle_refined_deg	1.851
r_mcbond_it	1.288
r_nbtor_refined	0.314
r_nbd_refined	0.237
r_symmetry_vdw_refined	0.237
r_symmetry_hbond_refined	0.231
r_xyhbond_nbd_refined	0.192
r_chiral_restr	0.138
r_bond_refined_d	0.021
r_gen_planes_refined	0.008

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2007
Nucleic Acid Atoms
Solvent Atoms	96
Heterogen Atoms	4

Software

Software
Software Name	Purpose
REFMAC	refinement
CrystalClear	data collection
HKL-2000	data reduction
SCALEPACK	data scaling
MOLREP	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.