3OA1

Crystal structure of phosphoprotein/Protein P/Protein M1 residues 69-297 from Rabies virus reveals degradation to C-terminal domain only

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.5	289	6.48 mg/mL LyraA.17086.a.D14 PD00142 in 25 mM Tris pH 8, 0.2 M NaCl, 1 mM TCEP, 1% glycerol against Emerald Biosystems Wizard Full screen condition A8 2 M ammonium sulphate, 0.1 M Citrate pH 5.5, 16 C, 0.4 uL protein and 0.4 uL precipitant, crystal tracking ID 216420a8, VAPOR DIFFUSION, SITTING DROP, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
2.46	50

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 91.98	α = 90
b = 44.08	β = 127.8
c = 74.58	γ = 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	100	CCD	RIGAKU SATURN 944+	VariMax	2010-07-29	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU FR-E+ SUPERBRIGHT	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	2.2	50	97.8	0.071	19.01	7	12248	11974		-3	29.937

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)
	2.2	2.26	81.3		0.179	9.1	5.6	868

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	2.2	37.64	11947	569	98.13	0.1749	0.1723	0.225	RANDOM	22.7096

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]
0.37		0.18	-1.08		0.92

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.644
r_dihedral_angle_4_deg	15.413
r_dihedral_angle_3_deg	13.973
r_dihedral_angle_1_deg	5.01
r_scangle_it	3.966
r_scbond_it	2.499
r_mcangle_it	1.438
r_angle_refined_deg	1.382
r_mcbond_it	0.755
r_chiral_restr	0.09

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.644
r_dihedral_angle_4_deg	15.413
r_dihedral_angle_3_deg	13.973
r_dihedral_angle_1_deg	5.01
r_scangle_it	3.966
r_scbond_it	2.499
r_mcangle_it	1.438
r_angle_refined_deg	1.382
r_mcbond_it	0.755
r_chiral_restr	0.09
r_bond_refined_d	0.015
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1623
Nucleic Acid Atoms
Solvent Atoms	130
Heterogen Atoms	25

Software

Software
Software Name	Purpose
XSCALE	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
StructureStudio	data collection
XDS	data reduction

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.