1NUH

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1IAT	PDN ENTRY 1IAT

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	8.5	294	2.1 M ammonium sulphate, 100 mM Tris pH 8.5, 5 mM 5-phosphoarabinonate, VAPOR DIFFUSION, HANGING DROP, temperature 294K

Crystal Properties
Matthews coefficient	Solvent content
2.41	49.06

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 94.4	α = 90
b = 94.4	β = 90
c = 137.1	γ = 90

Symmetry
Space Group	P 43 21 2

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	RIGAKU RAXIS IV	Osmic mirrors	2000-12-15	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RU300	1.5418

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	2.51	94.4	98.4	0.128	0.128	5.7	6.9	21797	21797			25.4

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.51	2.59	99.8		0.254	0.254	3.1	6.8	2171

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	REFINEMENT	THROUGHOUT	PDN ENTRY 1IAT	2.51	50	21468	21468	1101	98.4	0.217	0.217	0.214	0.268	RANDOM	25.156

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]
-0.51			-0.51		1.03

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	17.246
r_dihedral_angle_1_deg	3.624
r_scangle_it	3.022
r_scbond_it	1.834
r_angle_refined_deg	1.473
r_mcangle_it	1.008
r_mcbond_it	0.516
r_symmetry_hbond_refined	0.348
r_nbd_refined	0.241
r_symmetry_vdw_refined	0.202

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_3_deg	17.246
r_dihedral_angle_1_deg	3.624
r_scangle_it	3.022
r_scbond_it	1.834
r_angle_refined_deg	1.473
r_mcangle_it	1.008
r_mcbond_it	0.516
r_symmetry_hbond_refined	0.348
r_nbd_refined	0.241
r_symmetry_vdw_refined	0.202
r_xyhbond_nbd_refined	0.174
r_chiral_restr	0.104
r_bond_refined_d	0.011
r_gen_planes_refined	0.005

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4424
Nucleic Acid Atoms
Solvent Atoms	109
Heterogen Atoms	45

Software

Software
Software Name	Purpose
REFMAC	refinement
CrystalClear	data reduction
CrystalClear	data scaling

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.