BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 5030

Title: 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2   PubMed: 11727984

Authors: Lescop, Ewen; Briand, Loic; Pernollet, Jean-Claude; van Heijenoort, Carine; Guittet, Eric

Citation: Lescop, Ewen; Briand, Loic; Pernollet, Jean-Claude; van Heijenoort, Carine; Guittet, Eric. "Letter to the Editor: 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2"  J. Biomol. NMR 21, 181-182 (2001).

Assembly members:
ASP2, polymer, 123 residues, 13695 Da.

Natural source:   Common Name: Honeybee   Taxonomy ID: 7460   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Apis mellifera

Experimental source:   Production method: recombinant technology   Host organism: Pichia pastoris

Entity Sequences (FASTA):
ASP2: IDQDTVVAKYMEYLMPDIMP CADELHISEDIATNIQAAKN GADMSQLGCLKACVMKRIEM LKGTELYVEPVYKMIEVVHA GNADDIQLVKGIANECIENA KGETDECNIGNKYTDCYIEK LFS

Data sets:
Data typeCount
1H chemical shifts466
13C chemical shifts361
15N chemical shifts119

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ASP21

Entities:

Entity 1, ASP2 123 residues - 13695 Da.

1   ILEASPGLNASPTHRVALVALALALYSTYR
2   METGLUTYRLEUMETPROASPILEMETPRO
3   CYSALAASPGLULEUHISILESERGLUASP
4   ILEALATHRASNILEGLNALAALALYSASN
5   GLYALAASPMETSERGLNLEUGLYCYSLEU
6   LYSALACYSVALMETLYSARGILEGLUMET
7   LEULYSGLYTHRGLULEUTYRVALGLUPRO
8   VALTYRLYSMETILEGLUVALVALHISALA
9   GLYASNALAASPASPILEGLNLEUVALLYS
10   GLYILEALAASNGLUCYSILEGLUASNALA
11   LYSGLYGLUTHRASPGLUCYSASNILEGLY
12   ASNLYSTYRTHRASPCYSTYRILEGLULYS
13   LEUPHESER

Samples:

15N13C_H2O: ASP2, [U-98% 13C; U-98% 15N], 0.7 – 1.5 mM; TSP 0.1 mM; phosphate buffer 100 mM; NaN3 0.1 mM; H2O 90%; D2O 10%

15N13C_D2O: ASP2, [U-98% 13C; U-98% 15N], 1.3 mM; TSP 0.1 mM; phosphate buffer 100 mM; NaN3 0.1 mM; D2O 100%

15N_H2O: ASP2, [U-98% 15N], 1 mM; TSP 0.1 mM; phosphate buffer 100 mM; NaN3 0.1 mM; H2O 90%; D2O 10%

Cond_D2O: pH: 7.7; temperature: 308 K; ionic strength: 0.11 M

Cond_H2O: pH: 5.7; temperature: 308 K; ionic strength: 0.11 M

Experiments:

NameSampleSample stateSample conditions
The 1H-15N NOESY and 1H-15N TOCSY experiments were collected on the 15N proteinnot availablenot availablenot available
in H2O (sample 15N_H20).not availablenot availablenot available
The HNCA,HN(CO)CA, HNCO, HN(CA)CO, HNCACB and CBCA(CO)NH experiments werenot availablenot availablenot available
collected on the 13C-15N protein in 100%H20 (sample 15N13C_H2O).not availablenot availablenot available
The HCCH-TOCSY and 13C and NOESY-HSQC experiments were collected on the 13C-15Nnot availablenot availablenot available
protein in 100% D2O (sample 13C15N_D2O).not availablenot availablenot available

Software:

XWINNMR v2.6 - acquisition, processing

AURELIA v2.8.4 - Analysis

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
GB AAD51945 AAL60418 ABD97844
REF NP_001011591