BMRB Entry 25830

Name: Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum
Published: 2016-05-23

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PDB ID: 2n81
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25830
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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:

Solution Structure of Lipid Transfer Protein From Pea Pisum Sativum

Deposition date:

2015-09-30

Original release date:

2016-05-23

Authors:

Paramonov, Alexander; Rumynskiy, Eugene; Bogdanov, Ivan; Ovchinnikova, Tatiana; Shenkarev, Zakhar

Citation:

Citation: Bogdanov, Ivan; Shenkarev, Zakhar; Paramonov, Alexander; Rumynskiy, Eugene; Finkina, Ekaterina; Melnikova, Daria; Arseniev, Alexander; Ovchinnikova, Tatiana. "A novel lipid transfer protein from the pea Pisum sativum: isolation, recombinant expression, solution structure, antifungal activity, lipid binding, and allergenic properties" BMC Plant Biol. 16, 107-107 (2016).
PubMed: 27137920

Assembly members:

Assembly members:
Ps-LTP1, polymer, 95 residues, 9546.055 Da.

Natural source:

Natural source: Common Name: pea Taxonomy ID: 3888 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Pisum sativum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-His8-TrxL-Ps-LTP1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ps-LTP1: ALSCGTVSADLAPCVTYLQA PNNASPPPPCCAGVKKLLAA ATTTPDRQAACNCLKSAAGS IPKLNTNNAAALPGKCGVSI PYKISTSTNCNTVRF

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	96
1H chemical shifts	623

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PS-LTP1	1

Entities:

Entity 1, PS-LTP1 95 residues - 9546.055 Da.

1

ALA

LEU

SER

CYS

GLY

THR

VAL

SER

ALA

ASP

2

LEU

ALA

PRO

CYS

VAL

THR

TYR

LEU

GLN

ALA

3

PRO

ASN

ALA

SER

PRO

CYS

4

CYS

ALA

GLY

VAL

LYS

LEU

ALA

5

ALA

THR

PRO

ASP

ARG

GLN

ALA

6

CYS

ASN

CYS

LEU

LYS

SER

ALA

GLY

SER

7

ILE

PRO

LYS

LEU

ASN

THR

ASN

ALA

8

ALA

LEU

PRO

GLY

LYS

CYS

GLY

VAL

SER

ILE

9

PRO

TYR

LYS

ILE

SER

THR

SER

THR

ASN

CYS

10

ASN

THR

VAL

ARG

PHE

Samples:

sample_1: PS-LTP1, [U-98% 13C; U-98% 15N], 1 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 10 mM; pH: 5.5; pressure: 1 atm; temperature: 303 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 HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.8, Keller and Wuthrich - chemical shift assignment, chemical shift calculation, peak picking

TOPSPIN v2.1, Bruker Biospin - collection, processing

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

Bruker Avance 700 MHz