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- PDB-1e09: Solution Structure of the Major Cherry Allergen Pru av 1 -

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Basic information

Entry
Database: PDB / ID: 1000000000
TitleSolution Structure of the Major Cherry Allergen Pru av 1
ComponentsPRU AV 1
KeywordsALLERGEN / MAJOR CHERRY ALLERGEN / PATHOGENESIS-RELATED PROTEIN / HETERONUCLEAR NMR
Function / homology
Function and homology information


abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / defense response / signaling receptor activity / nucleus / cytoplasm
Similarity search - Function
Pathogenesis-related proteins Bet v I family signature. / Bet v I type allergen / Bet v I/Major latex protein / Pathogenesis-related protein Bet v 1 family / : / START domain / Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4 / START-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Major allergen Pru av 1
Similarity search - Component
Biological speciesPRUNUS AVIUM (sweet cherry)
MethodSOLUTION NMR / simulated annealing
AuthorsNeudecker, P. / Nerkamp, J. / Schweimer, K. / Sticht, H. / Boehm, M. / Scheurer, S. / Vieths, S. / Roesch, P.
Citation
Journal: J.Biol.Chem. / Year: 2001
Title: Allergic Cross-Reactivity Made Visible: The Solution Structure of the Major Cherry Allergen Pru Av 1
Authors: Neudecker, P. / Schweimer, K. / Nerkamp, J. / Scheurer, S. / Vieths, S. / Sticht, H. / Roesch, P.
#1: Journal: Appl.Magn.Reson. / Year: 1999
Title: NMR Spectroscopy Reveals Common Structural Features of the Birch Pollen Allergen Bet V 1 and the Cherry Allergen Pru a 1
Authors: Schweimer, K. / Sticht, H. / Nerkamp, J. / Boehm, M. / Breitenbach, M. / Vieths, S. / Roesch, P.
#2: Journal: J.Biomol.NMR / Year: 2000
Title: Sequence-Specific 1H, 13C and 15N Resonance Assignments of the Major Cherry Allergen Pru a 1
Authors: Neudecker, P. / Schweimer, K. / Nerkamp, J. / Boehm, M. / Scheurer, S. / Vieths, S. / Sticht, H. / Roesch, P.
History
DepositionMar 15, 2000Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 15, 2001Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3May 15, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Remark 650 HELIX DETERMINATION METHOD: AUTHOR PROVIDED.
Remark 700 SHEET DETERMINATION METHOD: AUTHOR PROVIDED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PRU AV 1


Theoretical massNumber of molelcules
Total (without water)17,5541
Polymers17,5541
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)22 / 60LOWEST ENERGY
RepresentativeModel #1

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Components

#1: Protein PRU AV 1


Mass: 17553.678 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) PRUNUS AVIUM (sweet cherry) / Plasmid: PET16B / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O24248

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D-TOCSY
1212D-NOESY
1311H
14115N-HSQC
151HNHA
1613D-1H
17115N-TOCSY-HSQC
1813D-1H
19115N-NOESY-HSQC
11013D-1H
111115N/ 1H
112115N-HMQC-NOESY-HSQC
11311H
114113C-CTHSQC
1151HNCO
1161HNCA
1171HN(CA)CB
1181CBCA(CO)NH
1191H(C)CH-COSY
1201(H)CCH-COSY
1211HC(C)H-TOCSY
12213D-1H
123113C-NOESY-HSQC
12413D-1H
125113C/ 1H
126115N-HMQC-NOESY-HSQC
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C/15N-LABELED PRU AV 1

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Sample preparation

DetailsContents: 90% H2O / 10% D2O
Sample conditionsIonic strength: 10 mM / pH: 7 / Pressure: 1 atm / Temperature: 308 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
NDEEstructure solution
NMRView4.1.0structure solution
X-PLOR3.851structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 60 / Conformers submitted total number: 22

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