BMRB Entry 25384

Name: The Beclin 1 N-terminal Domain (BecN-150CSY)
Published: 2016-06-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25384

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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:

The Beclin 1 N-terminal Domain (BecN-150CSY)

Deposition date:

2014-12-08

Original release date:

2016-06-30

Authors:

Yao, Shenggen; Lee, Erinna; Fairlie, Walter; Keizer, David

Citation:

Citation: Yao, Shenggen; Lee, Erinna; Pettikiriarachchi, Anne; Evangelista, Marco; Keizer, David; Fairlie, Walter. "Characterisation of the conformational preference and dynamics of the intrinsically disordered N-terminal region of Beclin 1 by NMR spectroscopy" Biochim. Biophys. Acta 1864, 1128-1137 (2016).

Assembly members:

Assembly members:
BecN-150CSY, polymer, 165 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: pET DUET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BecN-150CSY: MGSSHHHHHHSQDPMEGSKT SNNSTMQVSFVSQRSSQPLK LDTSFKILDRVTIQELTAPL LTTAQAKPGETQEEETNSGE EPFIETPRQDGVSRRFIPPA RMMSTESANSFTLIGEASDG GTMENLSRRLKVTGDLFDIM SGQTDVDHPLSEESTDTLLD QLDTY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	438
15N chemical shifts	142
1H chemical shifts	293

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 165 residues - Formula weight is not available

Residues (-14) - (-1) represent a non-native tag Residue 151 is non-native added to facilitate quantitation by UV spectroscopy

1

MET

GLY

SER

HIS

2

SER

GLN

ASP

PRO

MET

GLU

GLY

SER

LYS

THR

3

SER

ASN

SER

THR

MET

GLN

VAL

SER

PHE

4

VAL

SER

GLN

ARG

SER

GLN

PRO

LEU

LYS

5

LEU

ASP

THR

SER

PHE

LYS

ILE

LEU

ASP

ARG

6

VAL

THR

ILE

GLN

GLU

LEU

THR

ALA

PRO

LEU

7

LEU

THR

ALA

GLN

ALA

LYS

PRO

GLY

GLU

8

THR

GLN

GLU

THR

ASN

SER

GLY

GLU

9

GLU

PRO

PHE

ILE

GLU

THR

PRO

ARG

GLN

ASP

10

GLY

VAL

SER

ARG

PHE

ILE

PRO

ALA

11

ARG

MET

SER

THR

GLU

SER

ALA

ASN

SER

12

PHE

THR

LEU

ILE

GLY

GLU

ALA

SER

ASP

GLY

13

GLY

THR

MET

GLU

ASN

LEU

SER

ARG

LEU

14

LYS

VAL

THR

GLY

ASP

LEU

PHE

ASP

ILE

MET

15

SER

GLY

GLN

THR

ASP

VAL

ASP

HIS

PRO

LEU

16

SER

GLU

SER

THR

ASP

THR

LEU

ASP

17

GLN

LEU

ASP

THR

TYR

Samples:

sample_1: BecN-150CSY, [U-15N], 0.18 mM; H2O 95%; D2O 5%

sample_2: BecN-150CSY, [U-100% 13C; U-100% 15N], 0.12 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 288 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker - processing

XEASY v1.3, Bartels et al. - 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