2IAH

Crystal structure of the ferripyoverdine receptor of the outer membrane of Pseudomonas aeruginosa bound to ferripyoverdine.

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1XKH

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	4.6	298	Na Acetate 0.1 M, pH 4.6; 12 mM MgSO4, 12 % PEG 3350. Protein concentration in 0.5 % C8E4: 15 mg/ml, VAPOR DIFFUSION, SITTING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.79	55.86

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 82.123	α = 90
b = 82.123	β = 90
c = 286.225	γ = 90

Symmetry
Space Group	P 41 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	CCD	ADSC QUANTUM 210		2005-09-05	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE ID29	0.97857	ESRF	ID29

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	2.73	46.96	94.4	0.045	7.3	2.9		24636		-3

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.73	2.88	78.3		0.274	1.3	2.2	2982

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	1XKH	2.73	46.96	23442	1193	100	0.24611	0.24412	0.28522	RANDOM	51.148

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]
1.61			1.61		-3.21

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.541
r_dihedral_angle_3_deg	16.675
r_dihedral_angle_4_deg	12.359
r_dihedral_angle_1_deg	5.192
r_angle_refined_deg	1.096
r_scangle_it	0.677
r_scbond_it	0.49
r_nbtor_refined	0.297
r_mcangle_it	0.296
r_mcbond_it	0.208

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.541
r_dihedral_angle_3_deg	16.675
r_dihedral_angle_4_deg	12.359
r_dihedral_angle_1_deg	5.192
r_angle_refined_deg	1.096
r_scangle_it	0.677
r_scbond_it	0.49
r_nbtor_refined	0.297
r_mcangle_it	0.296
r_mcbond_it	0.208
r_nbd_refined	0.186
r_symmetry_vdw_refined	0.152
r_xyhbond_nbd_refined	0.114
r_chiral_restr	0.066
r_bond_refined_d	0.008
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	5973
Nucleic Acid Atoms
Solvent Atoms
Heterogen Atoms	32

Software

Software
Software Name	Purpose
REFMAC	refinement
XDS	data reduction
SCALA	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.