3GFW

Crystal Structure of Human Dual Specificity Protein Kinase (TTK) in complex with a pyrolo-pyridin ligand

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, SITTING DROP	5.6	277	40% PEG300, 0.25M NaCl, 0.1M Na/K phosphate pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
3.13	60.73

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 70.969	α = 90
b = 114.686	β = 90
c = 111.174	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	MARMOSAIC 225 mm CCD		2008-05-08	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SLS BEAMLINE X10SA	0.97642	SLS	X10SA

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (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	2.74	60.302	99.1	0.073	0.073	10.3	3.7	12195	12085

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	R-Sym I (Observed)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	2.74	2.89	99.9		0.647	0.647	2	3.7	1742

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	3CEK	2.74	41.4	12273	12083	598	98.45	0.206	0.206	0.204	0.239	RANDOM	46.505

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]
-5.41			6.89		-1.48

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	43.594
r_dihedral_angle_4_deg	26.734
r_dihedral_angle_3_deg	18.049
r_dihedral_angle_1_deg	6.74
r_scangle_it	2.446
r_angle_refined_deg	1.58
r_scbond_it	1.472
r_angle_other_deg	0.92
r_mcangle_it	0.897
r_mcbond_it	0.467

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	43.594
r_dihedral_angle_4_deg	26.734
r_dihedral_angle_3_deg	18.049
r_dihedral_angle_1_deg	6.74
r_scangle_it	2.446
r_angle_refined_deg	1.58
r_scbond_it	1.472
r_angle_other_deg	0.92
r_mcangle_it	0.897
r_mcbond_it	0.467
r_chiral_restr	0.084
r_mcbond_other	0.084
r_bond_refined_d	0.014
r_gen_planes_refined	0.005
r_bond_other_d	0.001
r_gen_planes_other	0.001

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	1987
Nucleic Acid Atoms
Solvent Atoms	5
Heterogen Atoms	67

Software

Software
Software Name	Purpose
SCALA	data scaling
PHASER	phasing
REFMAC	refinement
PDB_EXTRACT	data extraction
CrystalClear	data collection
MOSFLM	data reduction

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.