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- PDB-1bc9: CYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE -

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Basic information

Entry
Database: PDB / ID: 1bc9
TitleCYTOHESIN-1/B2-1 SEC7 DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsCYTOHESIN-1
KeywordsEXCHANGE FACTOR / INTEGRIN BINDING PROTEIN
Function / homology
Function and homology information


Intra-Golgi traffic / regulation of ARF protein signal transduction / establishment of epithelial cell polarity / ARF guanyl-nucleotide exchange factor activity / adherens junction / regulation of cell adhesion / bicellular tight junction / vesicle-mediated transport / extrinsic component of cytoplasmic side of plasma membrane / lipid binding ...Intra-Golgi traffic / regulation of ARF protein signal transduction / establishment of epithelial cell polarity / ARF guanyl-nucleotide exchange factor activity / adherens junction / regulation of cell adhesion / bicellular tight junction / vesicle-mediated transport / extrinsic component of cytoplasmic side of plasma membrane / lipid binding / Golgi membrane / plasma membrane / cytosol / cytoplasm
PH domain / SEC7 domain profile. / PH domain profile. / Sec7 domain superfamily / Sec7, C-terminal domain superfamily / PH-like domain superfamily / Pleckstrin homology domain / Sec7 domain / Sec7 domain
Cytohesin-1
Specimen sourceHomo sapiens (human)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEALING
AuthorsBetz, S.F. / Schnuchel, A. / Wang, H. / Olejniczak, E.T. / Meadows, R.P. / Fesik, S.W.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 1998
Title: Solution structure of the cytohesin-1 (B2-1) Sec7 domain and its interaction with the GTPase ADP ribosylation factor 1.
Authors: Betz, S.F. / Schnuchel, A. / Wang, H. / Olejniczak, E.T. / Meadows, R.P. / Lipsky, B.P. / Harris, E.A. / Staunton, D.E. / Fesik, S.W.
Validation Report
SummaryFull reportAbout validation report
DateDeposition: May 6, 1998 / Release: May 11, 1999
RevisionDateData content typeGroupProviderType
1.0May 11, 1999Structure modelrepositoryInitial release
1.1Mar 24, 2008Structure modelVersion format compliance
1.2Jul 13, 2011Structure modelVersion format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: CYTOHESIN-1


Theoretical massNumber of molelcules
Total (without water)23,3891
Polyers23,3891
Non-polymers00
Water0
NMR ensembles
Datacriteria
Number of conformers (submitted / calculated)1 / 287MINIMIZED AVERAGE
Representative

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Components

#1: Protein/peptide CYTOHESIN-1 / B2-1 / SEC7 HOMOLOG B2-1


Mass: 23388.758 Da / Num. of mol.: 1 / Fragment: SEC7 DOMAIN, / Source: (gene. exp.) Homo sapiens (human) / Cell line: BL21 / Gene: B2-1 / Organ: SPLEEN / Plasmid: PET-20B / Species (production host): Escherichia coli / Gene (production host): B2-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q15438

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment

Conditions-ID: 1 / Solution-ID: 1

Experiment-IDType
1HNCA
2HN(CO)CA
3HN(CA)CB
4HN (COCA)CB
5HNCO
6HN(CA)CO
7(H)CCH-TOCSY
813C-NOESY
915N-NOESY
10HNHA-J
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED CYTOHESIN-1 SEC7 DOMAIN.

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Sample preparation

DetailsContents: 20 MM NAPI, 150 MM (NH4)2SO4, 3MM DTT, 10% D2O
sample conditionsIonic strength: 0.47 M / pH: 6.8 / Pressure: 1 atm / Temperature: 305 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer

Manufacturer: Bruker

TypeModelField strength (MHz)Spectrometer-ID
Bruker DRX500DRX5005001
Bruker DRX600DRX6006002
Bruker AMX750AMX7507503
Bruker DRX800DRX8008004

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software

Name: X-PLOR / Version: 3.1

DeveloperClassification
BRUNGERrefinement
structure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEALING / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION.
NMR ensembleConformer selection criteria: MINIMIZED AVERAGE / Conformers calculated total number: 287 / Conformers submitted total number: 1

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