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 18993

Title: Backbone resonance assignment of Alt a 1, the major allergen of Alternaria alternata   PubMed: 23715812

Deposition date: 2013-01-31 Original release date: 2013-02-21

Authors: Wagner, Gabriel; Zangger, Klaus

Citation: Wagner, Gabriel; Gutfreund, Sandra; Fauland, Kerstin; Keller, Walter; Valenta, Rudolf; Zangger, Klaus. "Backbone resonance assignment of Alt a 1, a unique -barrel protein and the major allergen of Alternaria alternata."  Biomol. NMR Assignments ., .-. (2013).

Assembly members:
Alt_a_1, polymer, 133 residues, Formula weight is not available

Natural source:   Common Name: Ascomycetes   Taxonomy ID: 5599   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Alternaria alternata

Experimental source:   Production method: obtained from a collaborator   Host organism: Escherichia coli   Vector: pET27b

Entity Sequences (FASTA):
Alt_a_1: MDTASCPVTTEGDYVWKISE FYGRKPEGTYYNSLGFNIKA TNGGTLDFTCSAQADKLEDH KWYSCGENSFMDFSFDSDRS GLLLKQKVSDDITYVATATL PNYCRAGGNGPKDFVCQGVA DAYITLVTLPKSS

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts126
1H chemical shifts126

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Alt_a_11

Entities:

Entity 1, Alt_a_1 133 residues - Formula weight is not available

1   METASPTHRALASERCYSPROVALTHRTHR
2   GLUGLYASPTYRVALTRPLYSILESERGLU
3   PHETYRGLYARGLYSPROGLUGLYTHRTYR
4   TYRASNSERLEUGLYPHEASNILELYSALA
5   THRASNGLYGLYTHRLEUASPPHETHRCYS
6   SERALAGLNALAASPLYSLEUGLUASPHIS
7   LYSTRPTYRSERCYSGLYGLUASNSERPHE
8   METASPPHESERPHEASPSERASPARGSER
9   GLYLEULEULEULYSGLNLYSVALSERASP
10   ASPILETHRTYRVALALATHRALATHRLEU
11   PROASNTYRCYSARGALAGLYGLYASNGLY
12   PROLYSASPPHEVALCYSGLNGLYVALALA
13   ASPALATYRILETHRLEUVALTHRLEUPRO
14   LYSSERSER

Samples:

sample_1: Alt_a_1, [U-98% 13C; U-98% 15N], 200 – 400 uM; sodium phosphate 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - data analysis

Analysis, CCPN - chemical shift assignment, chemical shift calculation, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

BMRB 3V0R
UNP P79085
PDB
EMBL CBK55527 CBK55528 CBK55529 CBK55535 CBK55538
GB AAB40400 AAB47552 AAM90320 AAS75297 AAT66592
SP P79085
AlphaFold P79085 P79085

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