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- PDB-2kq1: Solution Structure Of Protein BH0266 From Bacillus halodurans. No... -

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Basic information

Entry
Database: PDB / ID: 2kq1
TitleSolution Structure Of Protein BH0266 From Bacillus halodurans. Northeast Structural Genomics Consortium Target BhR97a
ComponentsBH0266 protein
KeywordsStructural Genomics / Unknown function / NESG / PSI-2 / Protein Structure Initiative / Northeast Structural Genomics Consortium
Function / homologyRNA Polymerase Alpha Subunit; Chain A, domain 2 - #30 / YbbR-like / : / YbbR-like protein / RNA Polymerase Alpha Subunit; Chain A, domain 2 / Beta Complex / Mainly Beta / membrane / BH0266 protein
Function and homology information
Biological speciesBacillus halodurans (bacteria)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsWu, Y. / Eletsky, A. / Lee, D. / Sathyamoorthy, B. / Buchwald, W. / Hua, J. / Ciccosanti, C. / He, Y. / Hamilton, K. / Acton, T. ...Wu, Y. / Eletsky, A. / Lee, D. / Sathyamoorthy, B. / Buchwald, W. / Hua, J. / Ciccosanti, C. / He, Y. / Hamilton, K. / Acton, T. / Xiao, R. / Everett, J. / Lee, H. / Prestegard, J. / Montelione, G.T. / Szyperski, T. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: To be Published
Title: Solution Structure Of Protein BH0266 From Bacillus halodurans
Authors: Wu, Y. / Eletsky, A. / Lee, D. / Sathyamoorthy, B. / Buchwald, W. / Hua, J. / Ciccosanti, C. / He, Y. / Hamilton, K. / Acton, T. / Xiao, R. / Everett, J. / Lee, H. / Prestegard, J. / ...Authors: Wu, Y. / Eletsky, A. / Lee, D. / Sathyamoorthy, B. / Buchwald, W. / Hua, J. / Ciccosanti, C. / He, Y. / Hamilton, K. / Acton, T. / Xiao, R. / Everett, J. / Lee, H. / Prestegard, J. / Montelione, G.T. / Szyperski, T.
History
DepositionOct 23, 2009Deposition site: BMRB / Processing site: RCSB
Revision 1.0Dec 22, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Feb 26, 2020Group: Database references / Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_assembly ...pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _struct_ref_seq_dif.details
Revision 1.3Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.4May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: BH0266 protein


Theoretical massNumber of molelcules
Total (without water)13,5891
Polymers13,5891
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #1lowest energy

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Components

#1: Protein BH0266 protein


Mass: 13589.061 Da / Num. of mol.: 1 / Fragment: sequence database residues 39-148
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus halodurans (bacteria) / Gene: BH0266 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9KG47

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1222D 1H-13C HSQC
1313D CBCA(CO)NH
1413D HN(CA)CB
1513D (H)CCH-TOCSY
1613D (H)CCH-COSY
171simNOESY

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Sample preparation

Details
Solution-IDContentsSolvent system
11.0 mM [U-100% 13C; U-100% 15N] protein, 90% H2O/10% D2O90% H2O/10% D2O
21.0 mM [U-5% 13C; U-99% 15N] protein, 90% H2O/10% D2O90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1.0 mMprotein-1[U-100% 13C; U-100% 15N]1
1.0 mMprotein-2[U-5% 13C; U-99% 15N]2
Sample conditionsIonic strength: 0.2 / pH: 6.5 / Pressure: ambient / Temperature: 288 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Bruker DMXBrukerDMX8002

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Processing

NMR software
NameDeveloperClassification
AutoAssignZimmerman, Moseley, Kulikowski and Montelionechemical shift assignment
AutoStructureHuang, Tejero, Powers and Montelionestructure solution
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
CNSBrunger, Adams, Clore, Gros, Nilges and Readrefinement
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
XEASYBartels et al.data analysis
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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