+
Open data
-
Basic information
Entry | Database: PDB / ID: 1000000000 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution Structure of the Major Cherry Allergen Pru av 1 | ||||||
![]() | PRU AV 1 | ||||||
![]() | ALLERGEN / MAJOR CHERRY ALLERGEN / PATHOGENESIS-RELATED PROTEIN / HETERONUCLEAR NMR | ||||||
Function / homology | ![]() 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 | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Neudecker, P. / Nerkamp, J. / Schweimer, K. / Sticht, H. / Boehm, M. / Scheurer, S. / Vieths, S. / Roesch, P. | ||||||
![]() | ![]() 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: ![]() 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 |
| ||||||
Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR PROVIDED. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 1 MB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 896.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 346.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 578 KB | Display | |
Data in XML | ![]() | 116.9 KB | Display | |
Data in CIF | ![]() | 148.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 17553.678 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
NMR details | Text: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C/15N-LABELED PRU AV 1 |
-
Sample preparation
Details | Contents: 90% H2O / 10% D2O |
---|---|
Sample conditions | Ionic strength: 10 mM / pH: 7 / Pressure: 1 atm / Temperature: 308 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
---|
-
Processing
NMR software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 60 / Conformers submitted total number: 22 |