BMRB Entry 51184

Name: 1H, 13C, and 15N backbone resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis
Published: 2022-06-08

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51184

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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 resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis

Deposition date:

2021-11-21

Original release date:

2022-06-08

Authors:

Davis, Jessica; Hounslow, Andrea; Baxter, Nicola; Mesnage, Stephane; Williamson, Mike

Citation:

Citation: Davis, Jessica; Hounslow, Andrea; Baxter, Nicola; Mesnage, Stephane; Williamson, Mike. "1H, 13C and 15N resonance assignments of a conserved putative cell wall binding domain from Enterococcus faecalis" Biomol. NMR Assignments 16, 247-251 (2022).
PubMed: 35665899

Assembly members:

Assembly members:
entity_1, polymer, 86 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Enterococcus faecalis Taxonomy ID: 1351 Superkingdom: Bacteria Kingdom: not available Genus/species: Enterococcus faecalis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET2818

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAAISNIDNYYTENPVKIVM LVNDRYYTDLEFKTPGSPVK KGTTIRVQGIEYSKNGYPRL KTSQGYITSNKRYVQKVNGS HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	325
15N chemical shifts	88
1H chemical shifts	556

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	R6	1

Entities:

Entity 1, R6 86 residues - Formula weight is not available

1

MET

ALA

ILE

SER

ASN

ILE

ASP

ASN

TYR

2

TYR

THR

GLU

ASN

PRO

VAL

LYS

ILE

VAL

MET

3

LEU

VAL

ASN

ASP

ARG

TYR

THR

ASP

LEU

4

GLU

PHE

LYS

THR

PRO

GLY

SER

PRO

VAL

LYS

5

LYS

GLY

THR

ILE

ARG

VAL

GLN

GLY

ILE

6

GLU

TYR

SER

LYS

ASN

GLY

TYR

PRO

ARG

LEU

7

LYS

THR

SER

GLN

GLY

TYR

ILE

THR

SER

ASN

8

LYS

ARG

TYR

VAL

GLN

LYS

VAL

ASN

GLY

SER

9

HIS

Samples:

sample_1: AtlE C-terminal repeat 6, [U-100% 13C; U-100% 15N], 1 mM; Phosphate buffer 40 mM; sodium azide 2 mM; TSP 1 mM

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCOCA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCOCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

FELIX v2007 - peak picking

ASSTOOLS - chemical shift assignment

TOPSPIN v4.0.5 - collection, processing

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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