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- PDB-1jw2: SOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha... -

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Basic information

Entry
Database: PDB / ID: 1jw2
TitleSOLUTION STRUCTURE OF HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha FROM ESCHERICHIA COLI. Ontario Centre for Structural Proteomics target EC0308_1_72; Northeast Structural Genomics Target ET88
ComponentsHEMOLYSIN EXPRESSION MODULATING PROTEIN Hha
KeywordsGENE REGULATION / Hha / HEMOLYSIN EXPRESSION MODULATING PROTEIN / Structural Genomics / Protein Structure Initiative / OCSP / NESG / PSI / Northeast Structural Genomics Consortium
Function / homology
Function and homology information


H-NS-Hha complex / regulation of gene expression / transcription regulator complex / regulation of DNA-templated transcription / DNA binding / cytosol
Similarity search - Function
HHA / Haemolysin expression modulating, HHA / HHA superfamily / Haemolysin expression modulating protein / Monooxygenase / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Hemolysin expression-modulating protein Hha
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / distance geometry simulated annealing
AuthorsChang, X. / Yee, A. / Savchenko, A. / Edwards, A.M. / Arrowsmith, C.H. / Northeast Structural Genomics Consortium (NESG)
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2002
Title: An NMR approach to structural proteomics
Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / ...Authors: Yee, A. / Chang, X. / Pineda-Lucena, A. / Wu, B. / Semesi, A. / Le, B. / Ramelot, T. / Lee, G.M. / Bhattacharyya, S. / Gutierrez, P. / Denisov, A. / Lee, C.H. / Cort, J.R. / Kozlov, G. / Liao, J. / Finak, G. / Chen, L. / Wishart, D. / Lee, W. / McIntosh, L.P. / Gehring, K. / Kennedy, M.A. / Edwards, A.M. / Arrowsmith, C.H.
History
DepositionSep 2, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 27, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 2022Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
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: HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha


Theoretical massNumber of molelcules
Total (without water)8,6421
Polymers8,6421
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 / 30structures with the lowest energy
RepresentativeModel #7lowest energy

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Components

#1: Protein HEMOLYSIN EXPRESSION MODULATING PROTEIN Hha


Mass: 8642.016 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli) / Plasmid: PET15B / Production host: Escherichia coli (E. coli) / References: UniProt: P0ACE3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 13C-separated NOESY
1213D 15N-separated NOESY

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Sample preparation

DetailsContents: 2mM Hha U-15N, 13C;
Solvent system: 150 mM NACL, 25 mM PHOSPHATE, 10% D2O, PH 6.5
Sample conditionsIonic strength: 150 mM NACL / pH: 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
VarianVarianINOVA6001
VarianVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipe2000.02.14Delagioprocessing
Sparky3.95Goddarddata analysis
CNS1Brungerstructure solution
CNS1Brungerrefinement
RefinementMethod: distance geometry simulated annealing / Software ordinal: 1
Details: the structures are based on a total of 1116 restraints, 968 are NOE-derived distance constraints, 96 dihedral angle restraints,52 distance restraints from hydrogen bonds.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 30 / Conformers submitted total number: 10

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