BMRB Entry 50074

Name: 1H, 13C, and 15N backbone assignments of the pheromone binding protein 2 from the Ostrinia furnacalis (OfurPBP2)
Published: 2020-01-22

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PDB ID: 7uo6
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50074
MolProbity Validation Chart

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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 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:

Citation: Dahal, Salik; Lewellen, Jacob; Chaudhary, Bharat; Mohanty, Smita. "1H, 13C, and 15N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2)" Biomol. NMR Assign. 14, 115-118 (2020).
PubMed: 31975054

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	527
15N chemical shifts	137
1H chemical shifts	815

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

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

Entities:

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

1

SER

GLN

ALA

VAL

MET

LYS

ASP

MET

THR

LYS

2

ASN

PHE

ILE

LYS

ALA

TYR

GLU

VAL

CYS

ALA

3

LYS

GLU

TYR

ASN

LEU

PRO

GLU

ALA

GLY

4

ALA

GLU

VAL

MET

ASN

PHE

TRP

LYS

GLU

GLY

5

TYR

VAL

LEU

THR

SER

ARG

GLU

ALA

GLY

CYS

6

ALA

ILE

LEU

CYS

LEU

SER

LYS

LEU

ASN

7

LEU

ASP

PRO

GLU

GLY

THR

LEU

HIS

ARG

8

GLY

ASN

THR

VAL

GLU

PHE

ALA

LYS

GLN

HIS

9

GLY

SER

ASP

ALA

MET

ALA

HIS

GLN

LEU

10

VAL

ASP

ILE

VAL

HIS

ALA

CYS

GLU

LYS

SER

11

VAL

PRO

ASN

GLU

ASP

ASN

CYS

LEU

MET

12

ALA

LEU

GLY

ILE

SER

MET

CYS

PHE

LYS

THR

13

GLU

ILE

HIS

LYS

LEU

ASN

TRP

ALA

PRO

ASP

14

HIS

GLU

LEU

GLU

MET

ALA

15

GLU

MET

LYS

GLN

Samples:

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

sample_conditions_1: 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Delaglio, Zhengrong and Bax - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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