BMRB Entry 51096

Name: 1H, 13C and 15N chemical shift assignments of the GYF cytoplasmic domain of the GltJ protein from Myxococcus xanthus
Published: 2022-04-20

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PDB ID: 7z3c
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51096
MolProbity Validation Chart

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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 chemical shift assignments of the GYF cytoplasmic domain of the GltJ protein from Myxococcus xanthus

Deposition date:

2021-09-23

Original release date:

2022-04-20

Authors:

Attia, Bouchra; Serrano, Bastien; Bornet, Olivier; Guerlesquin, Francoise; Elantak, Latifa

Citation:

Citation: Attia, Bouchra; Serrano, Bastien; Bornet, Olivier; Guerlesquin, Francoise; My, Laetitia; Castaing, Jean-Philippe; Mignot, Tam; Elantak, Latifa. "1H, 13C and 15N chemical shift assignments of the ZnR and GYF cytoplasmic domains of the GltJ protein from Myxococcus xanthus" Biomol. NMR Assignments 16, 219-223 (2022).
PubMed: 35445965

Assembly members:

Assembly members:
entity_1, polymer, 88 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Myxococcus xanthus Taxonomy ID: 34 Superkingdom: Bacteria Kingdom: not available Genus/species: Myxococcus xanthus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMDKEEAKANAAAHEWYV AIDEKQVGPFNVEKVKDLWD RGEVGPDSLCWRSGFSDWIP LSETAELASVLAPRPSKPVI VAPEPVSG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	341
15N chemical shifts	85
1H chemical shifts	521

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	GltJ-GYF	1

Entities:

Entity 1, GltJ-GYF 88 residues - Formula weight is not available

1

GLY

SER

HIS

MET

ASP

LYS

GLU

ALA

LYS

2

ALA

ASN

ALA

HIS

GLU

TRP

TYR

VAL

3

ALA

ILE

ASP

GLU

LYS

GLN

VAL

GLY

PRO

PHE

4

ASN

VAL

GLU

LYS

VAL

LYS

ASP

LEU

TRP

ASP

5

ARG

GLY

GLU

VAL

GLY

PRO

ASP

SER

LEU

CYS

6

TRP

ARG

SER

GLY

PHE

SER

ASP

TRP

ILE

PRO

7

LEU

SER

GLU

THR

ALA

GLU

LEU

ALA

SER

VAL

8

LEU

ALA

PRO

ARG

PRO

SER

LYS

PRO

VAL

ILE

9

VAL

ALA

PRO

GLU

PRO

VAL

SER

GLY

Samples:

sample_1: GltJ-GYF, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection, processing

CcpNMR - chemical shift assignment, data analysis

NMR spectrometers:

Bruker AVANCE III 600 MHz

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