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- PDB-1xee: Solution structure of the Chemotaxis Inhibitory Protein of Staphy... -

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Basic information

Entry
Database: PDB / ID: 1xee
TitleSolution structure of the Chemotaxis Inhibitory Protein of Staphylococcus aureus
Componentschemotaxis-inhibiting protein CHIPS
KeywordsIMMUNE SYSTEM / Chemotaxis Inhibitory Protein / Staphylococcus aureus / Superantigen / C5a
Function / homology
Function and homology information


extracellular region
Similarity search - Function
Chemotaxis-inhibiting protein CHIPS / Chemotaxis inhibitory protein / FPRL1/chemotaxis inhibitory protein / FPRL1/chemotaxis inhibitory protein superfamily / Chemotaxis-inhibiting protein CHIPS / Ubiquitin-like (UB roll) / Roll / Alpha Beta
Similarity search - Domain/homology
Chemotaxis inhibitory protein / Chemotaxis inhibitory protein
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsHaas, P.J. / de Haas, C.J. / Poppelier, M.J. / van Kessel, K.P. / van Strijp, J.A. / Dijkstra, K. / Scheek, R.M. / Fan, H. / Kruijtzer, J.A. / Liskamp, R.M. / Kemmink, J.
CitationJournal: J.Mol.Biol. / Year: 2005
Title: The structure of the C5a receptor-blocking domain of chemotaxis inhibitory protein of Staphylococcus aureus is related to a group of immune evasive molecules
Authors: Haas, P.J. / de Haas, C.J. / Poppelier, M.J. / van Kessel, K.P. / van Strijp, J.A. / Dijkstra, K. / Scheek, R.M. / Fan, H. / Kruijtzer, J.A. / Liskamp, R.M. / Kemmink, J.
History
DepositionSep 10, 2004Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Sep 27, 2005Provider: 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_spectrometer ...database_2 / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_spectrometer.model
Revision 1.4May 29, 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: chemotaxis-inhibiting protein CHIPS


Theoretical massNumber of molelcules
Total (without water)10,4761
Polymers10,4761
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 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein chemotaxis-inhibiting protein CHIPS


Mass: 10475.967 Da / Num. of mol.: 1 / Fragment: Residues 31-121
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Gene: CHP / Plasmid: pRSET / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21 (DE3) / References: UniProt: Q7WUJ0, UniProt: A6QIG7*PLUS

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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: 1-2mM 15N or 13C,15N labeled protein, 20mM sodium phosphate buffer
Solvent system: 93% H2O/7% D2O
Sample conditionspH: 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 INOVAVarianINOVA5001
Varian INOVAVarianINOVA6002
Bruker AVANCEBrukerAVANCE9003

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Processing

NMR software
NameVersionDeveloperClassification
CNS1.1Brunger et al.refinement
ARIA1.2Nilgesrefinement
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 20

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