4DWM

Crystal structure of the complex of type I Ribosome inactivating protein with N-acetylglucosamine at 1.62 A resolution

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	3MRW

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.8	298	14% PEG 6000, 100mM citrate buffer, pH 5.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K

Crystal Properties
Matthews coefficient	Solvent content
2.44	49.57

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 130.198	α = 90
b = 130.198	β = 90
c = 40.51	γ = 120

Symmetry
Space Group	H 3

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	77	CCD	MARRESEARCH	mirror	2011-10-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	ESRF BEAMLINE BM14	0.97	ESRF	BM14

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	1.62	65.1	99.2	0.036	27.3		40774	40774

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	1.62	1.65	100		0.462	2.3

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	MOLECULAR REPLACEMENT	THROUGHOUT	3MRW	1.62	50	40774	30951	1604	100	0.15905	0.15808	0.15626	0.19283	RANDOM	24.226

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]
-0.79	-0.4		-0.79		1.19

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.204
r_dihedral_angle_4_deg	18.232
r_dihedral_angle_3_deg	14.096
r_scangle_it	6.286
r_dihedral_angle_1_deg	5.578
r_scbond_it	4.061
r_mcangle_it	2.532
r_angle_refined_deg	1.873
r_mcbond_it	1.521
r_chiral_restr	0.188

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	36.204
r_dihedral_angle_4_deg	18.232
r_dihedral_angle_3_deg	14.096
r_scangle_it	6.286
r_dihedral_angle_1_deg	5.578
r_scbond_it	4.061
r_mcangle_it	2.532
r_angle_refined_deg	1.873
r_mcbond_it	1.521
r_chiral_restr	0.188
r_bond_refined_d	0.022
r_gen_planes_refined	0.014

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1911
Nucleic Acid Atoms
Solvent Atoms	281
Heterogen Atoms	41

Software

Software
Software Name	Purpose
HKL-2000	data collection
AMoRE	phasing
REFMAC	refinement
DENZO	data reduction
SCALEPACK	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.