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- PDB-1xn6: Solution Structure of Northeast Structural Genomics Target Protei... -

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Basic information

Entry
Database: PDB / ID: 1xn6
TitleSolution Structure of Northeast Structural Genomics Target Protein BcR68 encoded in gene Q816V6 of B. cereus
Componentshypothetical protein BC4709
KeywordsSTRUCTURAL GENOMICS / UNKNOWN FUNCTION / Protein Structure Initiative / PSI / NESG Target Protein BcR68 / alpha + beta / GFT NMR / Northeast Structural Genomics Consortium / NESG
Function / homologyActivator of Hsp90 ATPase homologue 1-like / Activator of Hsp90 ATPase homolog 1-like protein / START domain / Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4 / START-like domain superfamily / 2-Layer Sandwich / Alpha Beta / Activator of Hsp90 ATPase homologue 1/2-like C-terminal domain-containing protein
Function and homology information
Biological speciesBacillus cereus (bacteria)
MethodSOLUTION NMR / Torsion angle space dynamics
AuthorsLiu, G. / Acton, T. / Parish, D. / Ma, L. / Xu, D. / Xiao, R. / Montelione, G.T. / Szyperski, T. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2005
Title: NMR data collection and analysis protocol for high-throughput protein structure determination.
Authors: Liu, G. / Shen, Y. / Atreya, H.S. / Parish, D. / Shao, Y. / Sukumaran, D.K. / Xiao, R. / Yee, A. / Lemak, A. / Bhattacharya, A. / Acton, T.A. / Arrowsmith, C.H. / Montelione, G.T. / Szyperski, T.
History
DepositionOct 4, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 14, 2004Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 2, 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: hypothetical protein BC4709


Theoretical massNumber of molelcules
Total (without water)16,0971
Polymers16,0971
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)20 / 100target function
RepresentativeModel #1fewest violations

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Components

#1: Protein hypothetical protein BC4709


Mass: 16097.150 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus cereus (bacteria) / Plasmid: pET21 / Production host: Escherichia coli (E. coli) / References: UniProt: Q816V6

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111GFT (4,3)D HNNCABCA
121GFT (4,3)D CabCa(CO)NHN
131GFT (4,3)D (H)CCH
141GFT (4,3)D HabCab(CO)NHN
151simultaneous heteronuclear resolved [1H,1H]-NOESY
NMR detailsText: by GFT NMR

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Sample preparation

DetailsContents: 5% D2O, 0.02% NaN3, 10mM DTT, 5mM CaCl2, 100mM NaCl, 20mM MES, pH 6.5
Solvent system: D2O
Sample conditionspH: 6.5 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA7502

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipe2.3Delaglio, F.processing
XEASY1.3.1.3Bartels, C.data analysis
DYANA1.5Guentert, P.structure solution
AutoAssign1.13.2Zimmerman D.E.data analysis
AutoStructure2.0.0Huang, Y.J.data analysis
CYANA1.0.5Guentert, P.data analysis
DYANA1.5Guentert, P.refinement
RefinementMethod: Torsion angle space dynamics / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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