BMRB Entry 52378

Name: BELL2 1H 13C 15N_assignment
Published: 2024-07-22

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52378

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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:

BELL2 1H 13C 15N_assignment

Deposition date:

2024-03-29

Original release date:

2024-07-22

Authors:

Delcourte, Loic; Sanchez, Corinne; Morvan, Estelle; Berbon, Melanie; Grelard, Axelle; Saragaglia, Claire; Dakhli, Thiery; Bardiaux, Benjamin; Habenstein, Birgit; Kauffmann, Brice; Saupe, Sven; Loquet, Antoine

Citation:

Citation: Delcourte, Loic; Sanchez, Corinne; Morvan, Estelle; Berbon, Melanie; Grelard, Axelle; Saragaglia, Claire; Dakhli, Thierry; Thore, Stephane; Bardiaux, Benjamin; Habenstein, Birgit; Kauffmann, Brice; Saupe, Sven; Loquet, Antoine. "NMR resonance assignment of the cell death execution domain BELL2 from multicellular bacterial signalosomes" Biomol. NMR Assign. 18, 159-164 (2024).
PubMed: 38907837

Assembly members:

Assembly members:
entity_1, polymer, 102 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Streptomyces olivochromogenes Taxonomy ID: 1963 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptomyces olivochromogenes

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-24

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: DPISVALLAALAGGAGGELG RQAWVNLTALARRPFGRGHG ESAQAPAVSSGEAELVRLQE TPGDAARAQALSTALAVRAA FDAEFSSGLQQWHEQAKVVR TG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	376
15N chemical shifts	101
1H chemical shifts	576

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BELL2	1

Entities:

Entity 1, BELL2 102 residues - Formula weight is not available

1

ASP

PRO

ILE

SER

VAL

ALA

LEU

ALA

2

LEU

ALA

GLY

ALA

GLY

GLU

LEU

GLY

3

ARG

GLN

ALA

TRP

VAL

ASN

LEU

THR

ALA

LEU

4

ALA

ARG

PRO

PHE

GLY

ARG

GLY

HIS

GLY

5

GLU

SER

ALA

GLN

ALA

PRO

ALA

VAL

SER

6

GLY

GLU

ALA

GLU

LEU

VAL

ARG

LEU

GLN

GLU

7

THR

PRO

GLY

ASP

ALA

ARG

ALA

GLN

ALA

8

LEU

SER

THR

ALA

LEU

ALA

VAL

ARG

ALA

9

PHE

ASP

ALA

GLU

PHE

SER

GLY

LEU

GLN

10

GLN

TRP

HIS

GLU

GLN

ALA

LYS

VAL

ARG

11

THR

GLY

Samples:

sample_1: HEPES 20 mM; sodium chloride 80 mM; BELL2 domain, [U-100% 13C; U-100% 15N], 1 mM

sample_conditions_1: ionic strength: 0.08 M; pH: 7.5; pressure: 1 atm; temperature: 298 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 HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

Bruker Bruker Avance NEO 700 MHz MHz

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