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- PDB-1b6f: BIRCH POLLEN ALLERGEN BET V 1 -

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Basic information

Entry
Database: PDB / ID: 1b6f
TitleBIRCH POLLEN ALLERGEN BET V 1
ComponentsPROTEIN (MAJOR POLLEN ALLERGEN BET V 1-A)
KeywordsPLANT PROTEIN / MAJOR BIRCH POLLEN ALLERGEN / PATHOGENESIS-RELATED PROTEIN
Function / homology
Function and homology information


response to biotic stimulus / abscisic acid binding / abscisic acid-activated signaling pathway / protein phosphatase inhibitor activity / defense response / signaling receptor activity / nucleus / cytoplasm
Similarity search - Function
Pathogenesis-related protein Bet v I family / 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 pollen allergen Bet v 1-A
Similarity search - Component
Biological speciesBetula pendula (European white birch)
MethodSOLUTION NMR / simulated annealing
AuthorsSchweimer, K. / Sticht, H. / Boehm, M. / Roesch, P.
Citation
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. / Boehm, M. / Roesch, P.
#1: Journal: Biol.Chem. / Year: 1997
Title: Expression in Escherichia Coli, Purification, and Spectroscopic Characterization of Two Mutant Bet V 1 Proteins
Authors: Boehm, M. / Roesch, P.
#2: Journal: J.Biol.Chem. / Year: 1996
Title: Secondary Structure and Tertiary Fold of the Birch Pollen Allergen Bet V 1 in Solution
Authors: Faber, C. / Lindemann, A. / Sticht, H. / Ejchart, A. / Kungl, A. / Susani, M. / Frank, R.W. / Kraft, D. / Breitenbach, M. / Roesch, P.
History
DepositionJan 13, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Jan 17, 2000Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations
Category: database_2 / pdbx_struct_assembly ...database_2 / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.4Dec 27, 2023Group: 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: PROTEIN (MAJOR POLLEN ALLERGEN BET V 1-A)


Theoretical massNumber of molelcules
Total (without water)17,4441
Polymers17,4441
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)23 / 60LOWEST ENERGY AND LEAST RESTRAINT VIOLATION
RepresentativeModel #1

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Components

#1: Protein PROTEIN (MAJOR POLLEN ALLERGEN BET V 1-A)


Mass: 17443.557 Da / Num. of mol.: 1 / Mutation: M139L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Betula pendula (European white birch) / Description: SYNTHETIC GENE / Cell: POLLEN / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21/DE3 / References: UniProt: P15494

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D HNCO
1213D HNCA
1313D CBCA(CO)NH
1413D HN(CA)CB
1513D (H)CCH-COSY
1613D (H)CCH-TOCSY
1713D-13C-NOESYHSQC
1813D-15N-NOESYHSQC
1913D-15N-TOCSYHSQC
11013D HNHA
11112D-NOESY(D2O)
11212D-TOCSY(D2O)
NMR detailsText: THE STRUCTURE WAS DETERMINED USING MULTIDIMENSIONAL HETERONUCLEAR NMR SPECTROSCOPY ON 13C, 15N-LABELED BET V 1.

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Sample preparation

Sample conditionsIonic strength: 10 mM / pH: 7.0 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DRX600 / Manufacturer: Bruker / Model: DRX600 / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
NDEEstructure solution
X-PLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: LOWEST ENERGY AND LEAST RESTRAINT VIOLATION
Conformers calculated total number: 60 / Conformers submitted total number: 23

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