BMRB Entry 27637

Name: Backbone NMR assignment of the apo form of Jug r 3, the non-specific lipid transfer protein from walnut.
Published: 2019-02-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27637

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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:

Backbone NMR assignment of the apo form of Jug r 3, the non-specific lipid transfer protein from walnut.

Deposition date:

2018-10-05

Original release date:

2019-02-22

Authors:

Dubiela, Pawel; del Conte, Rebecca; Cantini, Francesca; Borowski, Tomasz; Aina, Roberta; Radauer, Christian; Bublin, Merima; Hoffmann-Sommergruber, Karin; Alessandri, Stefano

Citation:

Citation: Dubiela, Pawel; del Conte, Rebecca; Cantini, Francesca; Borowski, Tomasz; Aina, Roberta; Radauer, Christian; Bublin, Merima; Hoffmann-Sommergruber, Karin; Alessandri, Stefano. "Impact of lipid binding on the tertiary structure and allergenic potential of Jug r 3, the non-specific lipid transfer protein from walnut" Sci. Rep. 9, .-2007 (2019).
PubMed: 30765752

Assembly members:

Assembly members:
Jug_r_3, polymer, 97 residues, Formula weight is not available

Natural source:

Natural source: Common Name: English walnut Taxonomy ID: 51240 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Juglans regia

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Pichia pastoris Vector: pPICZaA-Jug r 3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Jug_r_3: EAEFVITCGQVASSVGSCIG YLRGTVPTVPPSCCNGVKSL NKAAATTADRQAACECLKKT SGSIPGLNPGLAAGLPGKCG VSVPYKISTSTNCKAVK

Data sets:

assigned_chemical_shifts
- backbone_chemical_shift_oleate_-free_jug_r_3

Data type	Count
13C chemical shifts	220
15N chemical shifts	80
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	jug r 3	1

Entities:

Entity 1, jug r 3 97 residues - Formula weight is not available

EAEF stretch N-terminal residues derived from the signal sequence cleavage site.

1

GLU

ALA

GLU

PHE

VAL

ILE

THR

CYS

GLY

GLN

2

VAL

ALA

SER

VAL

GLY

SER

CYS

ILE

GLY

3

TYR

LEU

ARG

GLY

THR

VAL

PRO

THR

VAL

PRO

4

PRO

SER

CYS

ASN

GLY

VAL

LYS

SER

LEU

5

ASN

LYS

ALA

THR

ALA

ASP

ARG

6

GLN

ALA

CYS

GLU

CYS

LEU

LYS

THR

7

SER

GLY

SER

ILE

PRO

GLY

LEU

ASN

PRO

GLY

8

LEU

ALA

GLY

LEU

PRO

GLY

LYS

CYS

GLY

9

VAL

SER

VAL

PRO

TYR

LYS

ILE

SER

THR

SER

10

THR

ASN

CYS

LYS

ALA

VAL

LYS

Samples:

sample_1: Jug r 3, [U-15N], 0.25 mM; sodium acetate 20 mM; Nacl 0.1 M

sample_2: Jug r 3, [U-13C; U-15N], 0.25 mM; sodium acetate 20 mM; Nacl 0.1 M

sample_conditions_1: ionic strength: 120 mM; pH: 5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 900 MHz

UNIPROT	C5H617 (C5H617_9ROSI)
AlphaFold	C5H617