Experiment: 2P0C

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	5.5	298	The protein in 20mM Tris-HCl pH 8.0, 0.5M NaCl, 5% glycerol, 2mM BME, 2.5 mM AMP-PNP, 10 mM MgCl2, 5mM peptide (ADEPNYETWG) was mixed with crystallization buffer (15% PEG 8000, 0.2M ammonium sulfate, and 0.1 M Sodium cacodylate, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K

Crystal Properties
Matthews coefficient	Solvent content
2.23	44.72

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 52.47	α = 90
b = 90.057	β = 102.44
c = 69.253	γ = 90

Symmetry
Space Group	P 1 21 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	IMAGE PLATE	RIGAKU RAXIS IV++		2007-01-23	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU	1.54178

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	2.4	25	99.8	0.067	21.6	3.5	24544	24544		-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)
	2.4	2.49	99.7		0.293	5.2	3.4	2456

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	PDB entry 2G15	2.4	24.79	23326	1232	99.54	0.20761	0.20414	0.27392	RANDOM	39.11

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]
5.72		-0.91	-3.14		-2.97

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.742
r_dihedral_angle_4_deg	16.83
r_dihedral_angle_3_deg	15.862
r_dihedral_angle_1_deg	5.194
r_scangle_it	2.174
r_scbond_it	1.618
r_mcangle_it	1.316
r_angle_refined_deg	1.201
r_mcbond_it	0.766
r_nbtor_refined	0.299

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.742
r_dihedral_angle_4_deg	16.83
r_dihedral_angle_3_deg	15.862
r_dihedral_angle_1_deg	5.194
r_scangle_it	2.174
r_scbond_it	1.618
r_mcangle_it	1.316
r_angle_refined_deg	1.201
r_mcbond_it	0.766
r_nbtor_refined	0.299
r_nbd_refined	0.195
r_symmetry_vdw_refined	0.181
r_symmetry_hbond_refined	0.168
r_metal_ion_refined	0.16
r_xyhbond_nbd_refined	0.135
r_chiral_restr	0.073
r_bond_refined_d	0.009
r_gen_planes_refined	0.003

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	3934
Nucleic Acid Atoms
Solvent Atoms	164
Heterogen Atoms	69

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
PHASER	phasing

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.