BMRB Entry 27979

Name: Chemical shifts of Bordetella pertussis effector BteA
Published: 2019-07-30

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27979

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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:

Chemical shifts of Bordetella pertussis effector BteA

Deposition date:

2019-07-18

Original release date:

2019-07-30

Authors:

Yahalom, Adi; Shaked, Hadassa; Chill, Jordan

Citation:

Citation: Yahalom, Adi; Davidov, Geula; Kolusheva, Sofiya; Shaked, Hadassa; Barber-Zucker, Shiran; Zarivach, Raz; Chill, Jordan. "Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain" Biochim. Biophys. Acta Biomembr. 1861, 183054-183054 (2019).
PubMed: 31487494

Assembly members:

Assembly members:
BteA131, polymer, 134 residues, 14940.66 Da.

Natural source:

Natural source: Common Name: Bordetella pertussis Taxonomy ID: 520 Superkingdom: Bacteria Kingdom: not available Genus/species: Bordetella pertussis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
BteA131: GSHMLSSNVNPVVGLSYRPL PETPPSGQAAAHPSMRLLEP NNDEFVRSVASPRLHHSSEA LREVKHDVRQFQASGDRSLQ QLRDLEVALNHWEASQPREF AKRGGMVAELRTAIDAYKQQ LHEQAPSHANLDVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	283
15N chemical shifts	101
1H chemical shifts	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	BteA131	1

Entities:

Entity 1, BteA131 134 residues - 14940.66 Da.

1

GLY

SER

HIS

MET

LEU

SER

ASN

VAL

ASN

2

PRO

VAL

GLY

LEU

SER

TYR

ARG

PRO

LEU

3

PRO

GLU

THR

PRO

SER

GLY

GLN

ALA

4

ALA

HIS

PRO

SER

MET

ARG

LEU

GLU

PRO

5

ASN

ASP

GLU

PHE

VAL

ARG

SER

VAL

ALA

6

SER

PRO

ARG

LEU

HIS

SER

GLU

ALA

7

LEU

ARG

GLU

VAL

LYS

HIS

ASP

VAL

ARG

GLN

8

PHE

GLN

ALA

SER

GLY

ASP

ARG

SER

LEU

GLN

9

GLN

LEU

ARG

ASP

LEU

GLU

VAL

ALA

LEU

ASN

10

HIS

TRP

GLU

ALA

SER

GLN

PRO

ARG

GLU

PHE

11

ALA

LYS

ARG

GLY

MET

VAL

ALA

GLU

LEU

12

ARG

THR

ALA

ILE

ASP

ALA

TYR

LYS

GLN

13

LEU

HIS

GLU

GLN

ALA

PRO

SER

HIS

ALA

ASN

14

LEU

ASP

VAL

LYS

Samples:

sample_1: BteA131 mM; bis-Tris 20 ± 0.2 mM; NaCl 100 ± 1 mM

sample_conditions_1: ionic strength: 0.2 M; pH: 6.3; pressure: 1 atm; temperature: 283 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.2, Bruker Biospin - collection, peak picking, processing

NMR spectrometers:

Bruker DRX 700 MHz

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