BMRB Entry 34036

Name: Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid LPPG
Published: 2017-06-22

Click here to enlarge.

PDB ID: 5lqv
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34036
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Spatial structure of the lentil lipid transfer protein in complex with anionic lysolipid LPPG

Deposition date:

2016-08-17

Original release date:

2017-06-22

Authors:

Mineev, K.; Shenkarev, Z.; Arseniev, A.; Melnikova, D.; Finkina, E.; Ovchinnikova, T.

Citation:

Citation: Shenkarev, Z.; Melnikova, D.; Finkina, E.; Sukhanov, S.; Boldyrev, I.; Gizatullina, A.; Mineev, K.; Arseniev, A.; Ovchinnikova, T.. "Ligand Binding Properties of the Lentil Lipid Transfer Protein: Molecular Insight into the Possible Mechanism of Lipid Uptake." Biochemistry 56, 1785-1796 (2017).
PubMed: 28266846

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 9299.694 Da.
entity_PGM, non-polymer, 483.553 Da.

Natural source:

Natural source: Common Name: Lentil Taxonomy ID: 3864 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Lens culinaris

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: AISCGAVTSDLSPCLTYLTG GPGPSPQCCGGVKKLLAAAN TTPDRQAACNCLKSAAGSIT KLNTNNAAALPGKCGVNIPY KISTTTNCNTVKF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	362
15N chemical shifts	97
1H chemical shifts	616

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_PGM	2

Entities:

Entity 1, entity_1 93 residues - 9299.694 Da.

1

ALA

ILE

SER

CYS

GLY

ALA

VAL

THR

SER

ASP

2

LEU

SER

PRO

CYS

LEU

THR

TYR

LEU

THR

GLY

3

GLY

PRO

GLY

PRO

SER

PRO

GLN

CYS

GLY

4

GLY

VAL

LYS

LEU

ALA

ASN

5

THR

PRO

ASP

ARG

GLN

ALA

CYS

ASN

6

CYS

LEU

LYS

SER

ALA

GLY

SER

ILE

THR

7

LYS

LEU

ASN

THR

ASN

ALA

LEU

8

PRO

GLY

LYS

CYS

GLY

VAL

ASN

ILE

PRO

TYR

9

LYS

ILE

SER

THR

ASN

CYS

ASN

THR

10

VAL

LYS

PHE

Entity 2, entity_PGM - C22 H44 O9 P - 483.553 Da.

1

PGM

Samples:

sample_1: LPPG 2 mM; LTP2, [U-99% 13C; U-99% 15N], 0.3 mM; sodium acetate 20 mM; sodium azide 0.01%

sample_conditions_1: ionic strength: 20 mM; pH: 5.6; pressure: 1 bar; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
13C-filtered NOESY-HSQC	sample_1	isotropic	sample_conditions_1

Software:

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment

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

TOPSPIN, Bruker Biospin - processing

NMR spectrometers:

Bruker AvanceIII 600 MHz

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