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 50074

Title: 1H, 13C, and 15N backbone assignments of the pheromone binding protein 2 from the Ostrinia furnacalis (OfurPBP2)

Deposition date: 2019-10-11 Original release date: 2020-01-22

Authors: Dahal, Salik

Citation: Dahal, Salik. "1H, 13C, and 15N backbone assignments of the pheromone binding protein from the Ostrinia furnacalis (OfurPBP2)"  J. Biomol. NMR ., .-..

Assembly members:
OfurPBP2, polymer, 144 residues, Formula weight is not available

Natural source:   Common Name: Asian corn borer   Taxonomy ID: 93504   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Ostrinia furnacalis

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

Entity Sequences (FASTA):
OfurPBP2: SQAVMKDMTKNFIKAYEVCA KEYNLPEAAGAEVMNFWKEG YVLTSREAGCAILCLSSKLN LLDPEGTLHRGNTVEFAKQH GSDDAMAHQLVDIVHACEKS VPPNEDNCLMALGISMCFKT EIHKLNWAPDHELLLEEMMA EMKQ

Data sets:
Data typeCount
13C chemical shifts527
15N chemical shifts137
1H chemical shifts815

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1pheromone binding protein 2 [Ostrinia furnacalis]1

Entities:

Entity 1, pheromone binding protein 2 [Ostrinia furnacalis] 144 residues - Formula weight is not available

1   SERGLNALAVALMETLYSASPMETTHRLYS
2   ASNPHEILELYSALATYRGLUVALCYSALA
3   LYSGLUTYRASNLEUPROGLUALAALAGLY
4   ALAGLUVALMETASNPHETRPLYSGLUGLY
5   TYRVALLEUTHRSERARGGLUALAGLYCYS
6   ALAILELEUCYSLEUSERSERLYSLEUASN
7   LEULEUASPPROGLUGLYTHRLEUHISARG
8   GLYASNTHRVALGLUPHEALALYSGLNHIS
9   GLYSERASPASPALAMETALAHISGLNLEU
10   VALASPILEVALHISALACYSGLULYSSER
11   VALPROPROASNGLUASPASNCYSLEUMET
12   ALALEUGLYILESERMETCYSPHELYSTHR
13   GLUILEHISLYSLEUASNTRPALAPROASP
14   HISGLULEULEULEUGLUGLUMETMETALA
15   GLUMETLYSGLN

Samples:

sample_1: Protein, [U-13C; U-15N], 400 ± 0 uM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

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

Software:

SPARKY, Delaglio, Zhengrong and Bax - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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