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- PDB-1l1k: NMR Identification and Characterization of the Flexible Regions i... -

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Entry
Database: PDB / ID: 1l1k
TitleNMR Identification and Characterization of the Flexible Regions in the 160 KD Molten Globule-like Aggregate of Barstar at Low pH
ComponentsBarstar
KeywordsPROTEIN BINDING / Barstar / low pH / 160 kD / aggregate
Function / homologyBarstar (barnase inhibitor) / Barstar (barnase inhibitor) / Barstar-like superfamily / cytoplasm / Barstar
Function and homology information
Biological speciesBacillus amyloliquefaciens (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsJuneja, J. / Bhavesh, N.S. / Udgaokar, J.B. / Hosur, R.V.
CitationJournal: Biochemistry / Year: 2002
Title: NMR identification and characterization of the flexible regions in the 160 kDa molten globule-like aggregate of barstar at low pH.
Authors: Juneja, J. / Bhavesh, N.S. / Udgaonkar, J.B. / Hosur, R.V.
History
DepositionFeb 18, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 4, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Barstar


Theoretical massNumber of molelcules
Total (without water)2,2551
Polymers2,2551
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 10target function
Representative

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Components

#1: Protein/peptide Barstar / RIBONUCLEASE INHIBITOR


Mass: 2254.586 Da / Num. of mol.: 1 / Fragment: Flexible region (residues 1-20)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Gene: barstar / Plasmid: pMT316 / Production host: Escherichia coli (E. coli) / Strain (production host): MM294 / References: UniProt: P11540

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 15N-separated NOESY
131HNN, HN(C)N, 15N HSQC, HNCA, HN(CO)CA, CBCANH, CBCA(CO)NH, HNCO,
1412D TOCSY, 2D HSQC-TOCSY
161TOCSY
NMR detailsText: This structure was determined using standard 2D and 3D hetronuclear techniques.

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Sample preparation

DetailsContents: 1.2 mM Barstar U-15N, 13C; / Solvent system: 90 % H2O, 10& D2O; pH 2.7
Sample conditionspH: 2.7 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
VNMR1Bvariancollection
Felix97MSIprocessing
DYANA1ETHstructure solution
DYANA1ETHrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 10 / Conformers submitted total number: 10

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