|Entry||Database: EMDB / ID: 1510|
|Title||Structure of full-length Epac2 in complex with cyclic-AMP and Rap.|
|Keywords||GEF / GTPases / Epac / Rap / cAMP|
|Source||Homo sapiens / human|
Mus musculus / mammal / House Mouse / ハツカネズミ, はつかねずみ /
|Map data||This is a map of the Epac2-cAMP-Rap1B complex.|
|Method||single particle reconstruction, at 23 Å resolution|
|Authors||Arias-Palomo E / Rehmann H / Hadders M / Schwede F / Bos JL / Llorca O|
|Citation||Nature, 2008, 455, 124-127|
|Date||Deposition: Apr 25, 2008 / Header (metadata) release: Apr 28, 2008 / Map release: Mar 31, 2009 / Last update: Apr 16, 2014|
Downloads & links
|File||emd_1510.map.gz (map file in CCP4 format, 433 KB)|
|Projections & slices|
Images are generated by Spider package.
|Voxel size||X=Y=Z: 4.2 Å|
CCP4 map header:
-Entire Epac2-cAMP-Rap1B complex
|Entire||Name: Epac2-cAMP-Rap1B complex / Number of components: 3|
Oligomeric State: One monomer of Epac2 binds one monomer of Rap1B in presence of cAMP
|Mass||Theoretical: 135 kDa|
-Component #1: protein, Rap1B
|Protein||Name: Rap1B / a.k.a: Rap1B / Oligomeric Details: Monomer / Number of Copies: 1 / Recombinant expression: Yes|
|Mass||Theoretical: 18 kDa|
|Source||Species: Homo sapiens / human|
|External references||Gene Ontology: GO: 0005622 / InterPro: InterPro: 003577|
-Component #2: protein, Epac2
|Protein||Name: Epac2 / a.k.a: Epac2 / Oligomeric Details: Monomer / Recombinant expression: Yes / Number of Copies: 1|
|Mass||Theoretical: 115 kDa|
|Source||Species: Mus musculus / mammal / House Mouse / ハツカネズミ, はつかねずみ /|
|Source (engineered)||Expression System: Escherichia coli / bacteria / エシェリキア・コリ, 大腸菌 / |
|External references||InterPro: InterPro: 001895 / Gene Ontology: GO: 0019933|
-Component #3: ligand, Adenosine cyclic monophosphate
|Ligand||Name: Adenosine cyclic monophosphate / a.k.a: cAMP / Details: cAMP is the Epac2 activator. / Recombinant expression: No|
|Mass||Theoretical: 0.32921 kDa|
|Source||Species: Synthetic construct|
|Sample solution||Buffer solution: 50mM Tris-HCL, 100mM NaCl, 10mM CaCl2, 500 uM cAMP, 5% glycerol.|
|Support film||400 mesh Copper/Palladium grid|
|Staining||Grids with adsorbed protein floated on 2% w/v uranyl formate for 60 seconds|
|Vitrification||Instrument: NONE / Cryogen name: NONE|
-Electron microscopy imaging
|Imaging||Microscope: JEOL 1230 / Date: Jul 19, 2007 / Details: Microscope JEOL 1230|
|Electron gun||Electron source: TUNGSTEN HAIRPIN / Accelerating voltage: 100 kV / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 50000 X (nominal) / Cs: 2.9 mm / Imaging mode: BRIGHT FIELD|
|Specimen Holder||Holder: Eucentric / Model: OTHER|
|Camera||Detector: KODAK SO-163 FILM|
|Image acquisition||Scanner: OTHER / Sampling size: 10.5 microns / Bit depth: 8|
|Processing||Method: single particle reconstruction / Number of class averages: 233 / Number of projections: 3442 / Applied symmetry: C1 (asymmetric)|
|3D reconstruction||Algorithm: Maximum-likelihood multirefine / Software: EMAN,Xmipp / CTF correction: Phase correction at the micrograph level / Resolution: 23 Å / Resolution method: FSC 0.5|
-Atomic model buiding
|Modeling #1||Refinement space: REAL|
Input PDB model: 3CF6
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