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Yorodumi- PDB-1h2o: SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 MUTANT E45W -
+Open data
-Basic information
Entry | Database: PDB / ID: 1h2o | ||||||
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Title | SOLUTION STRUCTURE OF THE MAJOR CHERRY ALLERGEN PRU AV 1 MUTANT E45W | ||||||
Components | MAJOR ALLERGEN PRU AV 1 | ||||||
Keywords | ALLERGEN / MAJOR CHERRY ALLERGEN / PATHOGENESIS-RELATED PROTEIN / HETERONUCLEAR NMR / PLANT DEFENSE | ||||||
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 | ||||||
Biological species | PRUNUS AVIUM (sweet cherry) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Neudecker, P. / Lehmann, K. / Nerkamp, J. / Schweimer, K. / Sticht, H. / Boehm, M. / Scheurer, S. / Vieths, S. / Roesch, P. | ||||||
Citation | Journal: Biochem.J. / Year: 2003 Title: Mutational Epitope Analysis of Pru Av 1 and Api G 1, the Major Allergens of Cherry (Prunus Avium) and Celery (Apium Graveolens): Correlating Ige Reactivity with Three-Dimensional Structure Authors: Neudecker, P. / Lehmann, K. / Nerkamp, J. / Haase, T. / Wangorsch, A. / Fotisch, K. / Hoffmann, S. / Roesch, P. / Vieths, S. / Scheurer, S. #1: Journal: J.Biol.Chem. / Year: 2001 Title: Allergic Cross-Reactivity Made Visible: 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. #2: Journal: J.Biomol.NMR / Year: 2001 Title: Improving the Efficiency of the Gaussian Conformational Database Potential for the Refinement of Protein and Nucleic Acid Structures Authors: Neudecker, P. / Sticht, H. / Roesch, P. #3: 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. #4: 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. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1h2o.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1h2o.ent.gz | 980.9 KB | Display | PDB format |
PDBx/mmJSON format | 1h2o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1h2o_validation.pdf.gz | 347.2 KB | Display | wwPDB validaton report |
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Full document | 1h2o_full_validation.pdf.gz | 604.2 KB | Display | |
Data in XML | 1h2o_validation.xml.gz | 126.7 KB | Display | |
Data in CIF | 1h2o_validation.cif.gz | 159.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h2/1h2o ftp://data.pdbj.org/pub/pdb/validation_reports/h2/1h2o | HTTPS FTP |
-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 17610.775 Da / Num. of mol.: 1 / Mutation: YES Source method: isolated from a genetically manipulated source Details: ENGINEERED MUTATION GLU 45 TRP / Source: (gene. exp.) PRUNUS AVIUM (sweet cherry) / Plasmid: PET11A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: O24248 |
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Compound details | PLANT DEFENSE PROTEIN, MEMBER OF THE BETV1 FAMILY OF PATHOGENESIS-RELATED PROTEINS. ENGINEERED ...PLANT DEFENSE PROTEIN, MEMBER OF THE BETV1 FAMILY OF PATHOGENES |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE CHANGES IN STRUCTURE COMPARED TO PRU AV 1 WT WERE DETERMINED USING DOUBLE-RESONANCE NMR SPECTROSCOPY ON 15N-LABELED PRU AV 1 E45W |
-Sample preparation
Details | Contents: 90% H2O / 10% D2O |
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Sample conditions | Ionic strength: 50 mM / pH: 7 / Pressure: 1 atm / Temperature: 298 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 60 / Conformers submitted total number: 24 |