BMRB Entry 27316

Name: NMR assignment of the transmembrane helix of BclxL in phospholipid nanodiscs
Published: 2018-07-12

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PDB ID: 6f46
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27316
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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:

NMR assignment of the transmembrane helix of BclxL in phospholipid nanodiscs

Deposition date:

2017-11-24

Original release date:

2018-07-12

Authors:

Raltchev, Kolio; Pipercevic, Joka; Hagn, Franz

Citation:

Citation: Raltchev, Kolio; Pipercevic, Joka; Hagn, Franz. "Structural analysis of natively-folded membrane-anchored proteins obtained by SortaseA-mediated ligation" .

Assembly members:

Assembly members:
BclxL, polymer, 35 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BclxL: GSGESRKGQERFNRWFLTGM TVAGVVLLGSLFSRK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	62
15N chemical shifts	26
1H chemical shifts	26

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BclxL	1

Entities:

Entity 1, BclxL 35 residues - Formula weight is not available

1

GLY

SER

GLY

GLU

SER

ARG

LYS

GLY

GLN

GLU

2

ARG

PHE

ASN

ARG

TRP

PHE

LEU

THR

GLY

MET

3

THR

VAL

ALA

GLY

VAL

LEU

GLY

SER

4

LEU

PHE

SER

ARG

LYS

Samples:

sample_1: BclxL, [U-13C; U-15N; U-2H], 400 mM; DMPC, [U-2H], 15 mM; DPMG, [U-2H], 5 mM; potassium phosphate 20 mM; sodium chloride 50 mM; EDTA 0.5 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N 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

Software:

TOPSPIN, Bruker - collection, processing

SPARKY, Goddard - 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