BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 34383

Title: Solution structure of birch pollen allergen Bet v 1a   PubMed: 31213622

Deposition date: 2019-03-20 Original release date: 2019-10-03

Authors: Schweimer, K.

Citation: Jacob, T.; von Loetzen, C.; Reuter, A.; Lacher, U.; Schiller, D.; Schobert, R.; Mahler, V.; Vieths, S.; Rosch, P.; Schweimer, K.; Wohrl, B.. "Identification of a natural ligand of the hazel allergen Cor a 1."  Sci. Rep. 9, 8714-8714 (2019).

Assembly members:
entity_1, polymer, 159 residues, 17461.594 Da.

Natural source:   Common Name: European white birch   Taxonomy ID: 3505   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Betula pendula

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: GVFNYETETTSVIPAARLFK AFILDGDNLFPKVAPQAISS VENIEGNGGPGTIKKISFPE GFPFKYVKDRVDEVDHTNFK YNYSVIEGGPIGDTLEKISN EIKIVATPDGGSILKISNKY HTKGDHEVKAEQVKASKEMG ETLLRAVESYLLAHSDAYN

Data sets:
Data typeCount
13C chemical shifts646
15N chemical shifts151
1H chemical shifts1013

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 159 residues - 17461.594 Da.

1   GLYVALPHEASNTYRGLUTHRGLUTHRTHR
2   SERVALILEPROALAALAARGLEUPHELYS
3   ALAPHEILELEUASPGLYASPASNLEUPHE
4   PROLYSVALALAPROGLNALAILESERSER
5   VALGLUASNILEGLUGLYASNGLYGLYPRO
6   GLYTHRILELYSLYSILESERPHEPROGLU
7   GLYPHEPROPHELYSTYRVALLYSASPARG
8   VALASPGLUVALASPHISTHRASNPHELYS
9   TYRASNTYRSERVALILEGLUGLYGLYPRO
10   ILEGLYASPTHRLEUGLULYSILESERASN
11   GLUILELYSILEVALALATHRPROASPGLY
12   GLYSERILELEULYSILESERASNLYSTYR
13   HISTHRLYSGLYASPHISGLUVALLYSALA
14   GLUGLNVALLYSALASERLYSGLUMETGLY
15   GLUTHRLEULEUARGALAVALGLUSERTYR
16   LEULEUALAHISSERASPALATYRASN

Samples:

sample_1: Betv1a, [U-13C; U-15N], 0.5 mM; sodium chloride 0.05 mM; sodium phosphate 0.05 mM

sample_conditions_1: ionic strength: 50 mM; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment

Xplor-NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

XwinNMR, Bruker Biospin - collection

NMR spectrometers:

  • Bruker AvanceII 800 MHz
  • Bruker Avance 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts