BMRB Entry 51937

Name: 1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein 3 of Ostrinia nubilalis (OnubPBP3), an agricultural pest.
Published: 2023-08-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51937

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H, 13C, and 15N resonance assignment and secondary structure of the pheromone binding protein 3 of Ostrinia nubilalis (OnubPBP3), an agricultural pest.

Deposition date:

2023-04-24

Original release date:

2023-08-30

Authors:

Al-Danoon, Omar; Mohanty, Smita

Citation:

Citation: Al-Danoon, Omar; Mohanty, Smita. "Backbone and side chain NMR assignments and secondary structure calculation of the pheromone binding protein3 of Ostrinia nubilalis, an agricultural pest" Biomol. NMR Assignments 17, 223-227 (2023).
PubMed: 37498448

Assembly members:

Assembly members:
entity_1, polymer, 144 residues, 16299.60 Da.

Natural source:

Natural source: Common Name: European corn borer Taxonomy ID: 29057 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Ostrinia nubilalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SQTVMREMTRNFIKAYEVCA KEYNLPEATGSELINFWKEG HELTTREAGCAILCMSTKLN LLDVQGSVHRGNTVEFAKHH GSDDAMAHQVVDILHACEKA TPNEDKCMLALSIAMCFKAE IHKLDWAPNHELMFEELVSD MWNS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	552
15N chemical shifts	139
1H chemical shifts	852

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	OnubPBP3	1

Entities:

Entity 1, OnubPBP3 144 residues - 16299.60 Da.

1

SER

GLN

THR

VAL

MET

ARG

GLU

MET

THR

ARG

2

ASN

PHE

ILE

LYS

ALA

TYR

GLU

VAL

CYS

ALA

3

LYS

GLU

TYR

ASN

LEU

PRO

GLU

ALA

THR

GLY

4

SER

GLU

LEU

ILE

ASN

PHE

TRP

LYS

GLU

GLY

5

HIS

GLU

LEU

THR

ARG

GLU

ALA

GLY

CYS

6

ALA

ILE

LEU

CYS

MET

SER

THR

LYS

LEU

ASN

7

LEU

ASP

VAL

GLN

GLY

SER

VAL

HIS

ARG

8

GLY

ASN

THR

VAL

GLU

PHE

ALA

LYS

HIS

9

GLY

SER

ASP

ALA

MET

ALA

HIS

GLN

VAL

10

VAL

ASP

ILE

LEU

HIS

ALA

CYS

GLU

LYS

ALA

11

THR

PRO

ASN

GLU

ASP

LYS

CYS

MET

LEU

ALA

12

LEU

SER

ILE

ALA

MET

CYS

PHE

LYS

ALA

GLU

13

ILE

HIS

LYS

LEU

ASP

TRP

ALA

PRO

ASN

HIS

14

GLU

LEU

MET

PHE

GLU

LEU

VAL

SER

ASP

15

MET

TRP

ASN

SER

Samples:

sample_1: Ostrinia nubilalis Pheromone Binding Protein 3, [U-100% 13C; U-100% 15N], 460 uM; EDTA 1 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1
3D 15N-TOCSY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.98 - chemical shift assignment

NMRPipe v11.0 - processing

SPARKY v3.115 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz
Bruker AVANCE III 800 MHz