BMRB Entry 16175

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16175

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Title:
Backbone assignments for odorant binding protein 1
Deposition date:
2009-02-13
Original release date:
2009-07-10
Authors:
Ames, James
Citation:

Citation: Xu, Xianzhong; Xu, Wei; Ishida, Yuko; Li, Yun; Leal, Walter; Ames, James. "(1)H, (15)N, and (13)C chemical shift assignments of the mosquito odorant binding protein-1 (CquiOBP1) bound to the mosquito oviposition pheromone."  Biomol NMR Assign 3, 195-197 (2009).
PubMed: 19888689

Assembly members:

Assembly members:
CquiOBP1, polymer, 125 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: southern house mosquito   Taxonomy ID: 7176   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Culex Culex pipiens quinquefasciatus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CquiOBP1: DVTPRRDAEYPPPELLEALK PLHDICAKKTGVTDEAIIEF SDGKIHEDEKLKCYMNCLFH EAKVVDDNGDVHLEKLRDSL PNSMHDIAMHMGKRCLYPEG ENLCEKAFWLHKCWKQADPK HYFLV

Data sets:
Data typeCount
13C chemical shifts496
15N chemical shifts120
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 125 residues - Formula weight is not available

1   ASPVALTHRPROARGARGASPALAGLUTYR
2   PROPROPROGLULEULEUGLUALALEULYS
3   PROLEUHISASPILECYSALALYSLYSTHR
4   GLYVALTHRASPGLUALAILEILEGLUPHE
5   SERASPGLYLYSILEHISGLUASPGLULYS
6   LEULYSCYSTYRMETASNCYSLEUPHEHIS
7   GLUALALYSVALVALASPASPASNGLYASP
8   VALHISLEUGLULYSLEUARGASPSERLEU
9   PROASNSERMETHISASPILEALAMETHIS
10   METGLYLYSARGCYSLEUTYRPROGLUGLY
11   GLUASNLEUCYSGLULYSALAPHETRPLEU
12   HISLYSCYSTRPLYSGLNALAASPPROLYS
13   HISTYRPHELEUVAL

Samples:

sample_1: CquiOBP1, [U-98% 13C; U-98% 15N], 0.5 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
GB AAL86413 AAO73465 ACI00062 ACI00063 EDS29369
REF XP_001848926

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