2B7A

The structural basis of Janus Kinase 2 inhibition by a potent and specific pan-Janus kinase inhibitor

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1M14	PDB ENTRY 1M14

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6	293	28% PEG 8000, 0.2M ammonium acetate, 0.1M citrate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Crystal Properties
Matthews coefficient	Solvent content
3.16	61.03

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 111.273	�� = 90
b = 111.273	�� = 90
c = 70.577	�� = 90

Symmetry
Space Group	P 41

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		2004-02-02	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	ROTATING ANODE	RIGAKU RU300	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	100	96.8	0.065	15.95	2.7	146053	53644

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	2.07	97.1		0.55	2.12	2.4

Refinement

Statistics
Diffraction ID	Structure Solution Method	Cross Validation method	Starting model	Resolution (High)	Resolution (Low)	Cut-off Sigma (I)	Number Reflections (All)	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 1M14	2	100	2	146053	53644	2861	96.86	0.2108	0.20881	0.24927	RANDOM	39.233

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]
0.98			0.98		-1.96

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.844
r_dihedral_angle_4_deg	15.598
r_dihedral_angle_3_deg	13.24
r_dihedral_angle_1_deg	4.73
r_scangle_it	3.144
r_scbond_it	1.989
r_mcangle_it	1.434
r_angle_refined_deg	1.02
r_mcbond_it	0.85
r_nbtor_refined	0.297

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.844
r_dihedral_angle_4_deg	15.598
r_dihedral_angle_3_deg	13.24
r_dihedral_angle_1_deg	4.73
r_scangle_it	3.144
r_scbond_it	1.989
r_mcangle_it	1.434
r_angle_refined_deg	1.02
r_mcbond_it	0.85
r_nbtor_refined	0.297
r_nbd_refined	0.161
r_symmetry_vdw_refined	0.118
r_symmetry_hbond_refined	0.118
r_xyhbond_nbd_refined	0.089
r_chiral_restr	0.06
r_bond_refined_d	0.006
r_gen_planes_refined	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	4762
Nucleic Acid Atoms
Solvent Atoms	395
Heterogen Atoms	46

Software

Software
Software Name	Purpose
REFMAC	refinement
SCALEPACK	data scaling
AMoRE	phasing

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 R01GM157729.