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- PDB-2mrw: Solution Structure of MciZ from Bacillus subtilis -

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Basic information

Entry
Database: PDB / ID: 2mrw
TitleSolution Structure of MciZ from Bacillus subtilis
ComponentsCell division factor
KeywordsCELL CYCLE / FtsZ
Function / homologyCell division inhibitor MciZ / Mother cell inhibitor of FtsZ / sporulation resulting in formation of a cellular spore / Cell division inhibitor MciZ
Function and homology information
Biological speciesBacillus subtilis (bacteria)
MethodSOLUTION NMR / DGSA-distance geometry simulated annealing, torsion angle dynamics
Model detailsminimized average structure, model1
Model type detailsminimized average
AuthorsCastellen, P. / Sforca, M.L. / Zeri, A.C.M. / Gueiros-Filho, F.J.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2015
Title: FtsZ filament capping by MciZ, a developmental regulator of bacterial division.
Authors: Bisson-Filho, A.W. / Discola, K.F. / Castellen, P. / Blasios, V. / Martins, A. / Sforca, M.L. / Garcia, W. / Zeri, A.C. / Erickson, H.P. / Dessen, A. / Gueiros-Filho, F.J.
History
DepositionJul 16, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Mar 25, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 22, 2015Group: Database references
Revision 1.2May 13, 2015Group: Database references

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cell division factor


Theoretical massNumber of molelcules
Total (without water)4,7861
Polymers4,7861
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1minimized average structure

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Components

#1: Protein/peptide Cell division factor / MciZ


Mass: 4785.785 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (synth.) Bacillus subtilis (bacteria) / References: UniProt: L8EBJ9

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H TOCSY
1212D 1H-1H NOESY
1322D 1H-1H NOESY
1422D 1H-1H TOCSY

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Sample preparation

Details
Solution-IDContentsSolvent system
10.2 mM MciZ, 50 mM sodium phosphate, 50 mM potassium chloride, 90% H2O/10% D2O90% H2O/10% D2O
20.2 mM MciZ, 50 mM sodium phosphate, 50 mM potassium chloride, 100% D2O100% D2O
Sample
Conc. (mg/ml)ComponentSolution-ID
0.2 mMMciZ-11
50 mMsodium phosphate-21
50 mMpotassium chloride-31
0.2 mMMciZ-42
50 mMsodium phosphate-52
50 mMpotassium chloride-62
Sample conditionsIonic strength: 0.05 / pH: 4.0 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometerType: Agilent INOVA / Manufacturer: Agilent / Model: INOVA / Field strength: 600 MHz

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Processing

NMR software
NameDeveloperClassification
NMRViewJohnson, One Moon Scientificchemical shift assignment
NMRViewJohnson, One Moon Scientificchemical shift calculation
NMRViewJohnson, One Moon Scientificpeak picking
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxdata analysis
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxchemical shift assignment
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CYANAGuntert, Mumenthaler and Wuthrichrefinement
NMRDrawDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
RefinementMethod: DGSA-distance geometry simulated annealing, torsion angle dynamics
Software ordinal: 1
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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