BMRB Entry 30757

Name: Structure of the C-terminal domain of BCL-XL in membrane
Published: 2020-06-26

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PDB ID: 6x7i
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30757
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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:

Structure of the C-terminal domain of BCL-XL in membrane

Deposition date:

2020-05-30

Original release date:

2020-06-26

Authors:

Yao, Y.; Tian, Y.; Marassi, F.

Citation:

Citation: Ryzhov, Pavel; Tian, Ye; Yao, Yong; Bobkov, Andrey; Im, Wonpil; Marassi, Francesca. "Conformational States of the Cytoprotective Protein Bcl-xL" Biophys. J. 119, 1324-1334 (2020).
PubMed: 32888404

Assembly members:

Assembly members:
entity_1, polymer, 28 residues, 3174.721 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GQERFNRWFLTGMTVAGVVL LGSLFSRK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1

Data type	Count
13C chemical shifts	43
15N chemical shifts	23
1H chemical shifts	134

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 28 residues - 3174.721 Da.

1

GLY

GLN

GLU

ARG

PHE

ASN

ARG

TRP

PHE

LEU

2

THR

GLY

MET

THR

VAL

ALA

GLY

VAL

LEU

3

LEU

GLY

SER

LEU

PHE

SER

ARG

LYS

Samples:

sample_1: C-terminal domain of BCL-XL, [U-99% 15N], 0.2 mM

sample_2: C-terminal domain of BCL-XL, [U-99% 13C; U-99% 15N], 0.2 mM

sample_3: C-terminal domain of BCL-XL, [selectively 15N Leu labeled], 4 mg/mL

sample_4: C-terminal domain of BCL-XL, [selectively 15N Leu labeled], 10 mg/mL

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 bar; temperature: 318 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
2D SLF	sample_3	anisotropic	sample_conditions_1
2D SLF	sample_4	anisotropic	sample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation

NMR spectrometers:

Bruker AVANCE 600 MHz
Bruker AVANCE 500 MHz
Bruker AVANCE 700 MHz

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