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- PDB-4aka: IPSE alpha-1, an IgE-binding crystallin -

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Basic information

Entry
Database: PDB / ID: 4aka
TitleIPSE alpha-1, an IgE-binding crystallin
ComponentsIL-4-INDUCING PROTEIN
KeywordsIMMUNE SYSTEM / SCHISTOSOMA MANSONI / IMMUNOGLOBULIN BINDING
Function / homologyInterleukin-4 inducing immunoglobulin-binding domain / Interleukin-4 inducing immunoglobulin-binding domain / Crystallins / Gamma-B Crystallin; domain 1 / Gamma-crystallin-like / Sandwich / Mainly Beta / IL-4-inducing protein
Function and homology information
Biological speciesSCHISTOSOMA MANSONI (invertebrata)
MethodSOLUTION NMR / CYANA
AuthorsMeyer, N.H. / Mayerhofer, H. / Tripsianes, K. / Barths, D. / Blindow, S. / Bade, S. / Madl, T. / Frey, A. / Haas, H. / Mueller-Dieckmann, J. ...Meyer, N.H. / Mayerhofer, H. / Tripsianes, K. / Barths, D. / Blindow, S. / Bade, S. / Madl, T. / Frey, A. / Haas, H. / Mueller-Dieckmann, J. / Sattler, M. / Scharmm, G.
Citation
Journal: J.Biol.Chem. / Year: 2015
Title: A Crystallin Fold in the Interleukin-4-Inducing Principle of Schistosoma Mansoni Eggs (Ipse/Alpha-1) Mediates Ige Binding for Antigen-Independent Basophil Activation
Authors: Meyer, N.H. / Mayerhofer, H. / Tripsianes, K. / Barths, D. / Blindow, S. / Bade, S. / Madl, T. / Frey, A. / Haas, H. / Mueller-Dieckmann, J. / Sattler, M. / Scharmm, G.
#1: Journal: Biomol.NMR Assign. / Year: 2011
Title: 1H, 13C and 15N Chemical Shift Assignments of Ipsedeltanls
Authors: Meyer, N.H. / Schramm, G. / Sattler, M.
History
DepositionFeb 22, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 13, 2013Provider: repository / Type: Initial release
Revision 1.1Jul 29, 2015Group: Database references
Revision 1.2Sep 23, 2015Group: Database references
Revision 1.3Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 1.4Nov 13, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: IL-4-INDUCING PROTEIN


Theoretical massNumber of molelcules
Total (without water)11,9811
Polymers11,9811
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein IL-4-INDUCING PROTEIN / INTERLEUKIN-4-INDUCING PROTEIN / IPSE ALPHA-1


Mass: 11981.478 Da / Num. of mol.: 1 / Fragment: RESIDUES 21-124
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) SCHISTOSOMA MANSONI (invertebrata) / Plasmid: PPROEXHTB IPSEDNLS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: Q869D4
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111NOESY
121NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED IPSEDELTANLS

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Sample preparation

DetailsContents: 10% D2O/ 90% H2O
Sample conditionsIonic strength: 200 mM / pH: 7.2 / Pressure: 1.0 atm / Temperature: 298.0 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE9001
Bruker AVANCEBrukerAVANCE7502

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Processing

NMR software
NameVersionDeveloperClassification
CNS, ARIAARIAJP.LINGE,MA.WILLIAMS,CA.SPRONK,AM.BONVIN,M.refinement
NMRPipestructure solution
Sparkystructure solution
CYANAstructure solution
ARIAstructure solution
RefinementMethod: CYANA / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 100 / Conformers submitted total number: 20

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