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- PDB-3swv: Crystal Structure of a domain of Brefeldin A-inhibited guanine nu... -

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Basic information

Entry
Database: PDB / ID: 3swv
TitleCrystal Structure of a domain of Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (Brefeldin A-inhibited GEP 2) from Homo sapiens (Human), Northeast Structural Genomics Consortium target id HR5562A
ComponentsBrefeldin A-inhibited guanine nucleotide-exchange protein 2
KeywordsMETAL BINDING PROTEIN / Structural Genomics / PSI-Biology / Northeast Structural Genomics Consortium / NESG / Guanine-nucleotide releasing factor / Phosphoprotein / Nucleotide-binding protein / Metal-binding protein
Function / homology
Function and homology information


endomembrane system organization / symmetric synapse / receptor recycling / axonemal microtubule / endosome organization / GABA receptor binding / Golgi to plasma membrane transport / regulation of ARF protein signal transduction / microtubule organizing center / myosin binding ...endomembrane system organization / symmetric synapse / receptor recycling / axonemal microtubule / endosome organization / GABA receptor binding / Golgi to plasma membrane transport / regulation of ARF protein signal transduction / microtubule organizing center / myosin binding / exocytosis / protein kinase A regulatory subunit binding / Association of TriC/CCT with target proteins during biosynthesis / asymmetric synapse / GABA-ergic synapse / guanyl-nucleotide exchange factor activity / trans-Golgi network / recycling endosome / positive regulation of tumor necrosis factor production / protein transport / presynapse / cytoplasmic vesicle / dendritic spine / intracellular signal transduction / Golgi membrane / intracellular membrane-bounded organelle / centrosome / glutamatergic synapse / perinuclear region of cytoplasm / Golgi apparatus / membrane / cytosol
Similarity search - Function
Sec7/BIG1-like, C-terminal domain / BIG2 C-terminal domain / Mon2/Sec7/BIG1-like, HDS / Mon2/Sec7/BIG1-like, HDS / Mon2/Sec7/BIG1-like, dimerisation and cyclophilin-binding domain / Mon2/Sec7/BIG1-like, dimerisation and cyclophilin-binding domain / Mon2/Sec7/BIG1-like, HUS domain / Mon2/Sec7/BIG1-like, HUS domain / Arf Nucleotide-binding Site Opener; domain 2 / Arf Nucleotide-binding Site Opener,domain 2 ...Sec7/BIG1-like, C-terminal domain / BIG2 C-terminal domain / Mon2/Sec7/BIG1-like, HDS / Mon2/Sec7/BIG1-like, HDS / Mon2/Sec7/BIG1-like, dimerisation and cyclophilin-binding domain / Mon2/Sec7/BIG1-like, dimerisation and cyclophilin-binding domain / Mon2/Sec7/BIG1-like, HUS domain / Mon2/Sec7/BIG1-like, HUS domain / Arf Nucleotide-binding Site Opener; domain 2 / Arf Nucleotide-binding Site Opener,domain 2 / Annexin V; domain 1 - #20 / Sec7 domain / Sec7, C-terminal domain superfamily / Sec7 domain superfamily / Sec7 domain / SEC7 domain profile. / Sec7 domain / Annexin V; domain 1 / Armadillo-like helical / Armadillo-type fold / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Brefeldin A-inhibited guanine nucleotide-exchange protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3 Å
AuthorsSeetharaman, J. / Su, M. / Forouhar, F. / Wang, D. / Janjua, H. / Cunningham, K. / Owens, L. / Xiao, R. / Liu, J. / Baran, M.C. ...Seetharaman, J. / Su, M. / Forouhar, F. / Wang, D. / Janjua, H. / Cunningham, K. / Owens, L. / Xiao, R. / Liu, J. / Baran, M.C. / Acton, T.B. / Montelione, G.T. / Hunt, J.F. / Tong, L. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: To be Published
Title: Crystal Structure of a domain of Brefeldin A-inhibited guanine nucleotide-exchange protein 2 (BrefeldinA-inhibited GEP 2) from Homo sapiens (Human), Northeast Structural Genomics Consortium target id HR5562A
Authors: Seetharaman, J. / Su, M. / Forouhar, F. / Wang, D. / Janjua, H. / Cunningham, K. / Owens, L. / Xiao, R. / Liu, J. / Baran, M.C. / Acton, T.B. / Montelione, G.T. / Hunt, J.F. / Tong, L.
History
DepositionJul 14, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 24, 2011Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Brefeldin A-inhibited guanine nucleotide-exchange protein 2


Theoretical massNumber of molelcules
Total (without water)23,7891
Polymers23,7891
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)53.939, 53.939, 75.725
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32

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Components

#1: Protein Brefeldin A-inhibited guanine nucleotide-exchange protein 2 / Brefeldin A-inhibited GEP 2


Mass: 23788.945 Da / Num. of mol.: 1 / Fragment: SEC7 domain residues 635-836
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ARFGEF2, ARFGEP2, BIG2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y6D5

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.67 Å3/Da / Density % sol: 53.99 %
Crystal growTemperature: 291 K / pH: 5
Details: 15% PEG1000, 0.1M sodium citrate, pH 5.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength
SYNCHROTRONNSLS X4A10.979
SYNCHROTRONNSLS X6A20.979
Detector
TypeIDDetectorDate
ADSC QUANTUM 4r1CCDDec 1, 2009
ADSC QUANTUM 2102CCD
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHx-ray1
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
Reflection twinOperator: -h,-k,l / Fraction: 0.26
ReflectionResolution: 3→50 Å / Num. obs: 9252 / % possible obs: 94.8 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Rmerge(I) obs: 0.069 / Rsym value: 0.063 / Net I/σ(I): 8.9
Reflection shellResolution: 3→3.11 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.309 / % possible all: 99.8

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
SOLVEphasing
CNS1.1refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 3→20 Å / σ(F): 2 / Stereochemistry target values: ENGH & HUBER / Details: twinning fraction = 0.260 twin law = -h, -k, l
RfactorNum. reflectionSelection details
Rfree0.262 814 RANDOM
Rwork0.203 --
obs0.203 7363 -
all-8177 -
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.374 Å20 Å20 Å2
2--5.374 Å20 Å2
3----10.747 Å2
Refinement stepCycle: LAST / Resolution: 3→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1531 0 0 0 1531
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d1.18
X-RAY DIFFRACTIONc_bond_d_na
X-RAY DIFFRACTIONc_bond_d_prot
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_d_na
X-RAY DIFFRACTIONc_angle_d_prot
X-RAY DIFFRACTIONc_angle_deg2.08
X-RAY DIFFRACTIONc_angle_deg_na
X-RAY DIFFRACTIONc_angle_deg_prot
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_d_na
X-RAY DIFFRACTIONc_dihedral_angle_d_prot
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_d_na
X-RAY DIFFRACTIONc_improper_angle_d_prot
X-RAY DIFFRACTIONc_mcbond_it1.1421.5
X-RAY DIFFRACTIONc_mcangle_it2.0522
X-RAY DIFFRACTIONc_scbond_it1.2232
X-RAY DIFFRACTIONc_scangle_it2.1092.5
LS refinement shellResolution: 3→20 Å / Num. reflection Rfree: 814
Xplor fileSerial no: 1 / Param file: protein_rep.param

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