BMRB Entry 26852

Name: Partial Backbone 1H, 13C, and 15N Chemical Shift Assignments for VirB8 from Brucella suis
Published: 2017-02-22

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26852

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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:

Partial Backbone 1H, 13C, and 15N Chemical Shift Assignments for VirB8 from Brucella suis

Deposition date:

2016-07-13

Original release date:

2017-02-22

Authors:

Sharifahmadian, Mahzad; Lecoq, Lauriane; Omichinski, James; Baron, Christian

Citation:

Citation: Sharifahmadian, Mahzad; Arya, Tarun; Bessette, Benoit; Lecoq, Lauriane; Ruediger, Edward; Omichinski, James; Baron, Christian. "Monomer-to-dimer transition of Brucella suis type IV secretion system component VirB8 induces conformational changes" FEBS J. 284, 1218-1232 (2017).
PubMed: 28236662

Assembly members:

Assembly members:
VirB8p, polymer, 164 residues, 18202.1504 Da.

Natural source:

Natural source: Common Name: enterobacteria Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pHTVirB8sp

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VirB8p: ARVNAQTGAPDILTSLDEKS VSYDTVMDKYWLSQYVIARE TYDWYTLQKDYETVGMLSSP SEGQSYASQFQGDKALDKQY GSNVRTSVTIVSIVPNGKGI GTVRFAKTTKRTNETGDGET THWIATIGYQYVNPSLMSES ARLTNPLGFNVTSYRVDPEM GVVQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	416
15N chemical shifts	146
1H chemical shifts	146

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VirB8p subunit, 1	1
2	VirB8p subunit, 2	1

Entities:

Entity 1, VirB8p subunit, 1 164 residues - 18202.1504 Da.

1

ALA

ARG

VAL

ASN

ALA

GLN

THR

GLY

ALA

PRO

2

ASP

ILE

LEU

THR

SER

LEU

ASP

GLU

LYS

SER

3

VAL

SER

TYR

ASP

THR

VAL

MET

ASP

LYS

TYR

4

TRP

LEU

SER

GLN

TYR

VAL

ILE

ALA

ARG

GLU

5

THR

TYR

ASP

TRP

TYR

THR

LEU

GLN

LYS

ASP

6

TYR

GLU

THR

VAL

GLY

MET

LEU

SER

PRO

7

SER

GLU

GLY

GLN

SER

TYR

ALA

SER

GLN

PHE

8

GLN

GLY

ASP

LYS

ALA

LEU

ASP

LYS

GLN

TYR

9

GLY

SER

ASN

VAL

ARG

THR

SER

VAL

THR

ILE

10

VAL

SER

ILE

VAL

PRO

ASN

GLY

LYS

GLY

ILE

11

GLY

THR

VAL

ARG

PHE

ALA

LYS

THR

LYS

12

ARG

THR

ASN

GLU

THR

GLY

ASP

GLY

GLU

THR

13

THR

HIS

TRP

ILE

ALA

THR

ILE

GLY

TYR

GLN

14

TYR

VAL

ASN

PRO

SER

LEU

MET

SER

GLU

SER

15

ALA

ARG

LEU

THR

ASN

PRO

LEU

GLY

PHE

ASN

16

VAL

THR

SER

TYR

ARG

VAL

ASP

PRO

GLU

MET

17

GLY

VAL

GLN

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

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

BMRB Entry 26852

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: