3UEC

Crystal structure of human Survivin bound to histone H3 phosphorylated on threonine-3.

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.5	289	12% peg 8000; O.1 M MOPS 7.5; 0.1 M Magnesium acetate tetrahydrate , VAPOR DIFFUSION, HANGING DROP, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
3.11	60.41

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 69.254	α = 90
b = 70.225	β = 90
c = 88.83	γ = 90

Symmetry
Space Group	I 2 2 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 315r	mirrors	2010-11-12	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 19-ID	0.9792	APS	19-ID

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	2.18	50	99.9	0.067	24.2	3.8	11616	11616		-3	44.3

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	2.18	2.22	100		0.776	2.3	7.2	586

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	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	SAD	THROUGHOUT	2.18	50	11061	11061	554	99.66	0.19919	0.19919	0.19838	0.21488	RANDOM	56.691

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]
0.31			0.06		-0.37

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.223
r_dihedral_angle_4_deg	18.769
r_dihedral_angle_3_deg	17.65
r_dihedral_angle_1_deg	5.314
r_angle_other_deg	1.998
r_angle_refined_deg	1.675
r_chiral_restr	0.098
r_bond_refined_d	0.019
r_bond_other_d	0.01
r_gen_planes_refined	0.007

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	37.223
r_dihedral_angle_4_deg	18.769
r_dihedral_angle_3_deg	17.65
r_dihedral_angle_1_deg	5.314
r_angle_other_deg	1.998
r_angle_refined_deg	1.675
r_chiral_restr	0.098
r_bond_refined_d	0.019
r_bond_other_d	0.01
r_gen_planes_refined	0.007
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1138
Nucleic Acid Atoms
Solvent Atoms	53
Heterogen Atoms	40

Software

Software
Software Name	Purpose
HKL-3000	data collection
HKL-3000	phasing
MLPHARE	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.