3MAA

Complex of GS-Alpha with the Catalytic Domains of Mammalian Adenylyl Cyclase: Complex with Adenosine 5-O-(l-Thiophosphate) and Low Ca Concentration

X-RAY DIFFRACTION

Starting Model(s)

Initial Refinement Model(s)
Type	Source	Accession Code	Details
experimental model	PDB	1AZS	PDB entry 1AZS

Crystallization

Crystalization Experiments
ID	Method	pH	Temperature	Details
1	VAPOR DIFFUSION	5.6	289	7.5-7.8% PEG8000, 0.5M NACL, 0.1M PHOSPHATE BUFFER, pH 5.6, VAPOR DIFFUSION, temperature 289K

Crystal Properties
Matthews coefficient	Solvent content
2.97	58.53

Crystal Data

Unit Cell
Length ( ? )	Angle ( ? )
a = 118.744	�� = 90
b = 133.722	�� = 90
c = 70.992	�� = 90

Symmetry
Space Group	P 21 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 315	VERTICAL FOCUSING MIRROR, SINGLE CRYSTAL Si(311) BENT MONOCHROMATOR	2008-07-17	M	SINGLE WAVELENGTH

Radiation Source
ID #	Source	Type	Wavelength List	Synchrotron Site	Beamline
1	SYNCHROTRON	SSRL BEAMLINE BL9-1	1.0231	SSRL	BL9-1

Data Collection

Overall
ID #	Resolution (High)	Resolution (Low)	Percent Possible (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	3	25	82.7	0.175	5.1	2.8		20034			31.84

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	3	3.077	2.95		0.0305	0.414	3.3	2.1	1606

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	PDB entry 1AZS	3	25	18290	964	82.74	0.24228	0.23876	0.30888	RANDOM	31.84

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]
-1.44			-3.75		5.19

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	42.305
r_dihedral_angle_3_deg	21.693
r_dihedral_angle_4_deg	13.714
r_dihedral_angle_1_deg	6.979
r_angle_refined_deg	1.453
r_metal_ion_refined	0.335
r_nbtor_refined	0.324
r_nbd_refined	0.265
r_symmetry_hbond_refined	0.223
r_symmetry_vdw_refined	0.221

RMS Deviations
Key	Refinement Restraint Deviation
r_dihedral_angle_2_deg	42.305
r_dihedral_angle_3_deg	21.693
r_dihedral_angle_4_deg	13.714
r_dihedral_angle_1_deg	6.979
r_angle_refined_deg	1.453
r_metal_ion_refined	0.335
r_nbtor_refined	0.324
r_nbd_refined	0.265
r_symmetry_hbond_refined	0.223
r_symmetry_vdw_refined	0.221
r_xyhbond_nbd_refined	0.189
r_chiral_restr	0.097
r_bond_refined_d	0.012
r_gen_planes_refined	0.004

Non-Hydrogen Atoms Used in Refinement
Non-Hydrogen Atoms	Number
Protein Atoms	5627
Nucleic Acid Atoms
Solvent Atoms	12
Heterogen Atoms	105

Software

Software
Software Name	Purpose
Web-Ice	data collection
PHASES	phasing
REFMAC	refinement
HKL-2000	data reduction
HKL-2000	data scaling

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.