4FG7

Crystal structure of human calcium/calmodulin-dependent protein kinase I 1-293 in complex with ATP

X-RAY DIFFRACTION

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION, HANGING DROP	6	277	200mM NH4Ac, 100mM (CH3)2AsO2Na, 25% PEG 8000, pH 6.0, vapor diffusion, hanging drop, temperature 277K

Crystal Properties
Matthews coefficient	Solvent content
2.27	45.86

Crystal Data

Unit Cell
Length ( Å )	Angle ( ˚ )
a = 65.681	α = 90
b = 65.681	β = 90
c = 139.889	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	100	CCD	ADSC QUANTUM 4		2007-03-04	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	PHOTON FACTORY BEAMLINE BL-6A	1.0000	Photon Factory	BL-6A

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	59.46	99.4	0.052	33.6	7.5	8967				68.7

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	2.8	99.8		0.425	4.9	6.5

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 (Observed)	R-Work	R-Free	R-Free Selection Details	Mean Isotropic B
X-RAY DIFFRACTION	MOLECULAR REPLACEMENT	THROUGHOUT	PDB ENTRY 1A06	2.7	59.46	8967	8918	461	99.25	0.2214	0.2201	0.2458	RANDOM	51.0192

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]

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.569
r_dihedral_angle_4_deg	18.64
r_dihedral_angle_3_deg	15.95
r_dihedral_angle_1_deg	5.119
SIDE-CHAIN ANGLE REFINED ATOMS (A''2)	4.594
SIDE-CHAIN BOND REFINED ATOMS (A''2)	2.995
MAIN-CHAIN ANGLE REFINED ATOMS (A''2)	2.193
RIGID-BOND RESTRAINTS (A''2)	1.682
r_angle_refined_deg	1.435
MAIN-CHAIN BOND REFINED ATOMS (A''2)	1.23

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	38.569
r_dihedral_angle_4_deg	18.64
r_dihedral_angle_3_deg	15.95
r_dihedral_angle_1_deg	5.119
SIDE-CHAIN ANGLE REFINED ATOMS (A''2)	4.594
SIDE-CHAIN BOND REFINED ATOMS (A''2)	2.995
MAIN-CHAIN ANGLE REFINED ATOMS (A''2)	2.193
RIGID-BOND RESTRAINTS (A''2)	1.682
r_angle_refined_deg	1.435
MAIN-CHAIN BOND REFINED ATOMS (A''2)	1.23
CHIRAL-CENTER RESTRAINTS (A''3)	0.093
r_bond_refined_d	0.017
r_gen_planes_refined	0.006

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	2008
Nucleic Acid Atoms
Solvent Atoms	79
Heterogen Atoms	31

Software

Software
Software Name	Purpose
REFMAC	refinement
PDB_EXTRACT	data extraction
HKL-2000	data collection
HKL-2000	data reduction
HKL-2000	data scaling
CNS	phasing

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.