BMRB Entry 27951

Name: 1H, 13C, and 15N Chemical shift assignments of gypsy moth Lymantria dispar pheromone-binding protein 1 (LdisPBP1)
Published: 2020-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27951

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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: 1H, 13C, and 15N Chemical shift assignments of gypsy moth Lymantria dispar pheromone-binding protein 1 (LdisPBP1) PubMed: 32877603

Deposition date: 2019-06-19 Original release date: 2020-09-18

Authors: Terrado, Mailyn; Okon, Mark; McIntosh, Lawrence; Plettner, Erika

Citation: Terrado, Mailyn; Okon, Mark; McIntosh, Lawrence; Plettner, Erika. "Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1)" Biochemistry 57, 3411-3426 (2020).

Assembly members:
PBP1, polymer, 148 residues, Formula weight is not available

Natural source: Common Name: gypsy moth Taxonomy ID: 13123 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Lymantria dispar

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET30Xa/LIC

Entity Sequences (FASTA):
PBP1: GSGGGSKEVMKQMTINFAKP MEACKQELNVPDAVMQDFFN FWKEGYQITNREAGCVILCL AKKLELLDQDMNLHHGKAME FAMKHGADEAMAKQLLDIKH SCEKVITIVADDPCQTMLNL AMCFKAEIHKLDWAPTLDVA VGELLADT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	610
15N chemical shifts	156
1H chemical shifts	981

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PBP1	1

Entities:

Entity 1, PBP1 148 residues - Formula weight is not available

1

GLY

SER

GLY

SER

LYS

GLU

VAL

MET

2

LYS

GLN

MET

THR

ILE

ASN

PHE

ALA

LYS

PRO

3

MET

GLU

ALA

CYS

LYS

GLN

GLU

LEU

ASN

VAL

4

PRO

ASP

ALA

VAL

MET

GLN

ASP

PHE

ASN

5

PHE

TRP

LYS

GLU

GLY

TYR

GLN

ILE

THR

ASN

6

ARG

GLU

ALA

GLY

CYS

VAL

ILE

LEU

CYS

LEU

7

ALA

LYS

LEU

GLU

LEU

ASP

GLN

ASP

8

MET

ASN

LEU

HIS

GLY

LYS

ALA

MET

GLU

9

PHE

ALA

MET

LYS

HIS

GLY

ALA

ASP

GLU

ALA

10

MET

ALA

LYS

GLN

LEU

ASP

ILE

LYS

HIS

11

SER

CYS

GLU

LYS

VAL

ILE

THR

ILE

VAL

ALA

12

ASP

PRO

CYS

GLN

THR

MET

LEU

ASN

LEU

13

ALA

MET

CYS

PHE

LYS

ALA

GLU

ILE

HIS

LYS

14

LEU

ASP

TRP

ALA

PRO

THR

LEU

ASP

VAL

ALA

15

VAL

GLY

GLU

LEU

ALA

ASP

THR

Samples:

sample_1: PBP1, [U-100% 13C; U-100% 15N], 1.2 mM; sodium acetate 50 mM; EDTA 1 mM; sodium azide 0.05 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 4.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

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

SPARKY, Goddard - data analysis

NMR spectrometers:

Bruker AMX 600 MHz

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