BMRB Entry 26778

Name: 1H, 13C and 15N resonance assignments for the response regulator CheY3 from Rhodobacter spheroids at pH 4.5 in the absence of BeF3-
Published: 2016-09-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26778

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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 resonance assignments for the response regulator CheY3 from Rhodobacter spheroids at pH 4.5 in the absence of BeF3-

Deposition date:

2016-04-12

Original release date:

2016-09-02

Authors:

Varela-Alvarez, Lorena; Bell, Christian; Armitage, Judith; Redfield, Christina

Citation:

Citation: Varela-Alvarez, Lorena; Bell, Christian; Armitage, Judith; Redfield, Christina. "1H, 13C and 15N resonance assignments for the response regulator CheY3 from Rhodobacter sphaeroides" Biomol. NMR Assign. 10, 373-378 (2016).
PubMed: 27468962

Assembly members:

Assembly members:
CheY3_noBeF3_pH4.5, polymer, 132 residues, Formula weight is not available
entity_MG, non-polymer, 24.305 Da.

Natural source:

Natural source: Common Name: Rhodobacter sphaeroides Taxonomy ID: 1063 Superkingdom: Bacteria Kingdom: not available Genus/species: Rhodobacter sphaeroides

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pQE-80

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CheY3_noBeF3_pH4.5: MRGSHHHHHHGSSRTVLAVD DSPSVRSMVAMTLREAGYRV IEATDGREGLEKALSEPVDA IITDQNMPNLDGLGFIRAFR EHPESKGKPIIFLSTDSADT LKQQAREAGAMGWMVKPFTQ PQLLAVIKKVLG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	511
15N chemical shifts	126
1H chemical shifts	819

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CheY3_noBeF3_pH4.5	1
2	Mg2+	2

Entities:

Entity 1, CheY3_noBeF3_pH4.5 132 residues - Formula weight is not available

The protein contains an N-terminal His6 tag preceded by MRGS. We are providing only limited assignments for the non-native tag residues.

1

MET

ARG

GLY

SER

HIS

2

GLY

SER

ARG

THR

VAL

LEU

ALA

VAL

ASP

3

ASP

SER

PRO

SER

VAL

ARG

SER

MET

VAL

ALA

4

MET

THR

LEU

ARG

GLU

ALA

GLY

TYR

ARG

VAL

5

ILE

GLU

ALA

THR

ASP

GLY

ARG

GLU

GLY

LEU

6

GLU

LYS

ALA

LEU

SER

GLU

PRO

VAL

ASP

ALA

7

ILE

THR

ASP

GLN

ASN

MET

PRO

ASN

LEU

8

ASP

GLY

LEU

GLY

PHE

ILE

ARG

ALA

PHE

ARG

9

GLU

HIS

PRO

GLU

SER

LYS

GLY

LYS

PRO

ILE

10

ILE

PHE

LEU

SER

THR

ASP

SER

ALA

ASP

THR

11

LEU

LYS

GLN

ALA

ARG

GLU

ALA

GLY

ALA

12

MET

GLY

TRP

MET

VAL

LYS

PRO

PHE

THR

GLN

13

PRO

GLN

LEU

ALA

VAL

ILE

LYS

VAL

14

LEU

GLY

Entity 2, Mg2+ - Mg - 24.305 Da.

1

MG

Samples:

sample_1_15N: CheY3_noBeF3_pH4.5, [U-99% 15N], 2 mM; Mg2+ 2 mM; Sodium Acetate 20 mM

sample_2_15N_13C: CheY3_noBeF3_pH4.5, [U-99% 13C; U-99% 15N], 2 mM; Mg2+ 2 mM; Sodium Acetate 20 mM

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1_15N	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1_15N	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2_15N_13C	isotropic	sample_conditions_1
3D HNCA	sample_2_15N_13C	isotropic	sample_conditions_1
3D CBCANH	sample_2_15N_13C	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2_15N_13C	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2_15N_13C	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2_15N_13C	isotropic	sample_conditions_1
3D HNCO	sample_2_15N_13C	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1_15N	isotropic	sample_conditions_1
3D (H)C(CCO)NH	sample_2_15N_13C	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1_15N	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1_15N	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1_15N	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2_15N_13C	isotropic	sample_conditions_1
3D HNCACO	sample_2_15N_13C	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2_15N_13C	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_2_15N_13C	isotropic	sample_conditions_1

Software:

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

CcpNmr_Analysis, CCPN - data analysis

NMR spectrometers:

Bruker Avance 500 MHz
Home-built OMEGA 750 MHz

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