BMRB Entry 19006

Name: 1H, 13C and 15N backbone and side chain resonance assignment of the phosphorelay protein VanU from Vibrio anguillarum
Published: 2013-08-14

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19006

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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:

1H, 13C and 15N backbone and side chain resonance assignment of the phosphorelay protein VanU from Vibrio anguillarum

Deposition date:

2013-02-05

Original release date:

2013-08-14

Authors:

Bobay, Benjamin; Thompson, Richele; Cavanagh, John

Citation:

Citation: Bobay, Benjamin; Thompson, Richele; Milton, Debra; Cavanagh, John. "Chemical shift assignments and secondary structure prediction of the phosphorelay protein VanU from Vibrio anguillarum." Biomol. NMR Assignments 8, 177-179 (2014).
PubMed: 23604692

Assembly members:

Assembly members:
VanU, polymer, 114 residues, Formula weight is not available

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 55601 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio anguillarum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGEX-4T2

Entity Sequences (FASTA):

Entity Sequences (FASTA):
VanU: GSMELINKNKIAHLAQEIGE ENVPILLDIFLSELSAYTQK LADQNLPDKIEYLKDISHAL KSSAASFGADKLCAKAVDID SKGKANCIFDEAEEVAAMRA LIEETHRCYCHLMD

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	461
15N chemical shifts	111
1H chemical shifts	705

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	VanU	1

Entities:

Entity 1, VanU 114 residues - Formula weight is not available

Residues 1-2 represent a non-native affinity tag

1

GLY

SER

MET

GLU

LEU

ILE

ASN

LYS

ASN

LYS

2

ILE

ALA

HIS

LEU

ALA

GLN

GLU

ILE

GLY

GLU

3

GLU

ASN

VAL

PRO

ILE

LEU

ASP

ILE

PHE

4

LEU

SER

GLU

LEU

SER

ALA

TYR

THR

GLN

LYS

5

LEU

ALA

ASP

GLN

ASN

LEU

PRO

ASP

LYS

ILE

6

GLU

TYR

LEU

LYS

ASP

ILE

SER

HIS

ALA

LEU

7

LYS

SER

ALA

SER

PHE

GLY

ALA

ASP

8

LYS

LEU

CYS

ALA

LYS

ALA

VAL

ASP

ILE

ASP

9

SER

LYS

GLY

LYS

ALA

ASN

CYS

ILE

PHE

ASP

10

GLU

ALA

GLU

VAL

ALA

MET

ARG

ALA

11

LEU

ILE

GLU

THR

HIS

ARG

CYS

TYR

CYS

12

HIS

LEU

MET

ASP

Samples:

sample_1: VanU, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; TRIS 25 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: VanU, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; TRIS 25 mM; potassium chloride 100 mM; DTT 1 mM; sodium azide 0.02%; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_2
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_2

Software:

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

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 700 MHz

EMBL	AAS98244.1 CDQ49815
GB	AAS98244 AEH33638 AGU58069
REF	WP_010320685 WP_013857261 WP_017048414 WP_047690702