7LHY

Caenorhabditis elegans SWSN-4 (SMARCA4-BRG1) ATPase Bromodomain in complex with a modified histone H3, N6-epsilon-acetyl-L-lysine 14 (H3K14ac) polypeptide

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	7.3	277	35% total PEG concentration, divided equally among PEG 400, PEG 550 MME, PEG 600 and PEG 1,000. There was no buffer in this condition, but the protein was purified in 10 mM HEPES, pH 7.3

Crystal Properties
Matthews coefficient	Solvent content
2.07	40.49

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 69.064	α = 90
b = 69.064	β = 90
c = 55.32	γ = 90

Symmetry
Space Group	P 41 21 2

Diffraction

Diffraction Experiment
ID #	Crystal ID	Scattering Type	Data Collection Temperature	Detector	Detector Type	Details	Collection Date	Monochromator	Protocol
1	1	x-ray	170	PIXEL	DECTRIS EIGER X 16M		2016-10-22	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	APS BEAMLINE 22-ID	1.0	APS	22-ID

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	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	1.29	50	99.65	0.075	0.078	0.023	13.9	13.8		34008			17.25

Highest Resolution Shell
ID #	Resolution (High)	Resolution (Low)	Percent Possible (All)	Percent Possible (Observed)	R Merge I (Observed)	Rrim I (All)	Rpim I (All)	Mean I Over Sigma (Observed)	Redundancy	Number Unique Reflections (All)
1	1.29	1.34	100		0.93	0.97	0.3		12

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	2grc	1.3	48.84	31468	1998	99.34	0.1822	0.1813	0.1978	RANDOM	21.9287

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]
-0.53			-0.53		1.06

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	31.728
r_dihedral_angle_3_deg	10.966
r_dihedral_angle_4_deg	9.23
r_dihedral_angle_1_deg	4.869
r_angle_refined_deg	2.341
r_angle_other_deg	1.091
r_chiral_restr	0.134
r_bond_refined_d	0.027
r_gen_planes_refined	0.013
r_bond_other_d	0.003

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	31.728
r_dihedral_angle_3_deg	10.966
r_dihedral_angle_4_deg	9.23
r_dihedral_angle_1_deg	4.869
r_angle_refined_deg	2.341
r_angle_other_deg	1.091
r_chiral_restr	0.134
r_bond_refined_d	0.027
r_gen_planes_refined	0.013
r_bond_other_d	0.003
r_gen_planes_other	0.002

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	907
Nucleic Acid Atoms
Solvent Atoms	115
Heterogen Atoms

Software

Software
Software Name	Purpose
REFMAC	refinement
HKL-2000	data reduction
SCALEPACK	data scaling
PHASER	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 R01GM133198.