3UED

Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3 (C2 space group).

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	289	15% PEG 3350, 0.16 M sodium citrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
3.54	65.23

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 113.415	α = 90
b = 71.276	β = 129.91
c = 83.136	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	MARMOSAIC 300 mm CCD	beryllium lens	2011-03-20	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 21-ID-G	0.97856	APS	21-ID-G

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	2.7	50	99.8	0.055	32.3	4.2	14102	14102		-3	87.3

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	2.7	2.72	100		0.48	2.1	4.1	334

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	3UEC	2.7	41.28	13346	13346	709	99.7	0.19469	0.19469	0.19209	0.24086	RANDOM	77.55

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]
1.21		1.52	-0.31		1.06

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.534
r_dihedral_angle_4_deg	21.708
r_dihedral_angle_3_deg	16.799
r_dihedral_angle_1_deg	5.184
r_angle_other_deg	3.941
r_angle_refined_deg	1.636
r_chiral_restr	0.088
r_bond_refined_d	0.014
r_bond_other_d	0.012
r_gen_planes_refined	0.008

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	34.534
r_dihedral_angle_4_deg	21.708
r_dihedral_angle_3_deg	16.799
r_dihedral_angle_1_deg	5.184
r_angle_other_deg	3.941
r_angle_refined_deg	1.636
r_chiral_restr	0.088
r_bond_refined_d	0.014
r_bond_other_d	0.012
r_gen_planes_refined	0.008
r_gen_planes_other	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2254
Nucleic Acid Atoms
Solvent Atoms	17
Heterogen Atoms	2

Software

Software
Software Name	Purpose
BLU-MAX	data collection
HKL-3000	phasing
MOLREP	phasing
REFMAC	refinement
Coot	model building
HKL-3000	data reduction
HKL-3000	data scaling

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.