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- PDB-1ka5: Refined Solution Structure of Histidine Containing Phosphocarrier... -

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Basic information

Entry
Database: PDB / ID: 1ka5
TitleRefined Solution Structure of Histidine Containing Phosphocarrier Protein from Staphyloccocus aureus
ComponentsPHOSPHOCARRIER PROTEIN HPR
KeywordsLIGAND TRANSPORT / Open Faced beta-Sandwich / Structural Proteomics in Europe / SPINE / Structural Genomics
Function / homology
Function and homology information


phosphoenolpyruvate-dependent sugar phosphotransferase system / cytoplasm
Similarity search - Function
Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / PTS HPR domain serine phosphorylation site signature. / HPr-like / Histidine-containing Protein; Chain: A; / Phosphocarrier protein HPr-like / HPr-like superfamily / PTS HPr component phosphorylation site / PTS HPR domain profile. ...Phosphotransferase system, HPr histidine phosphorylation site / PTS HPR domain histidine phosphorylation site signature. / Phosphotransferase system, HPr serine phosphorylation site / PTS HPR domain serine phosphorylation site signature. / HPr-like / Histidine-containing Protein; Chain: A; / Phosphocarrier protein HPr-like / HPr-like superfamily / PTS HPr component phosphorylation site / PTS HPR domain profile. / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Phosphocarrier protein HPr
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsMaurer, T. / Meier, S. / Hengstenberg, W. / Kalbitzer, H.R. / Structural Proteomics in Europe (SPINE)
Citation
Journal: J.Bacteriol. / Year: 2004
Title: High-resolution structure of the histidine-containing phosphocarrier protein (HPr) from Staphylococcus aureus and characterization of its interaction with the bifunctional HPr kinase/phosphorylase
Authors: Maurer, T. / Meier, S. / Kachel, N. / Munte, C.E. / Hasenbein, S. / Koch, B. / Hengstenberg, W. / Kalbitzer, H.R.
#1: Journal: Eur.J.Biochem. / Year: 1993
Title: The Solution Structure of the Histidine Containing Phosphocarrier Protein (HPr) from Staphylococcus aureus as Determined by Two-Dimensional 1H-NMR Spectroscopy
Authors: Kalbitzer, H.R. / Hengstenberg, W.
History
DepositionOct 31, 2001Deposition site: RCSB / Processing site: RCSB
SupersessionJun 3, 2003ID: 1ZER
Revision 1.0Jun 3, 2003Provider: 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PHOSPHOCARRIER PROTEIN HPR


Theoretical massNumber of molelcules
Total (without water)9,5051
Polymers9,5051
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)16 / 440target function
RepresentativeModel #1lowest energy

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Components

#1: Protein PHOSPHOCARRIER PROTEIN HPR / HISTIDINE-CONTAINING PROTEIN


Mass: 9504.689 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Staphylococcus aureus (bacteria) / References: UniProt: P0A0E3

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 13C-separated NOESY
1313D 15N-separated NOESY
141HNHA
151DQF-COSY

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Sample preparation

DetailsContents: 2mM HPr / Solvent system: 95% H2O, 5% 2H2O
Sample conditionsIonic strength: 0 / pH: 7.4 / Pressure: ambinet / 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 spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX6001
Bruker DRXBrukerDRX8002

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Processing

NMR software
NameVersionDeveloperClassification
DYANA1.6Guentert, P., Mumenthaler, C. and Wuethrich, K.structure solution
DYANA1.6Guentert, P., Mumenthaler, C. and Wuethrich, K.refinement
RefinementMethod: simulated annealing / Software ordinal: 1
Details: 1883 distance and angle restraints and hydrogen bonding patterns
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 440 / Conformers submitted total number: 16

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