BMRB Entry 27540

Name: 1H, 15N, and 13C triple resonance assignments of innate immune evasion protein EapH2 from the S. aureus
Published: 2019-01-02

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PDB ID: 8gdg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27540
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, 15N, and 13C triple resonance assignments of innate immune evasion protein EapH2 from the S. aureus

Deposition date:

2018-07-12

Original release date:

2019-01-02

Authors:

Herrera, Alvaro; Dubey, Abhinav; Geisbrecht, Brian; Arthanari, Haribabu; Prakash, Om

Citation:

Citation: Herrera, Alvaro; Dubey, Abhinav; Geisbrecht, Brian; Arthanari, Haribabu; Prakash, Om. "Backbone resonance assignments of innate immune evasion protein EapH2 from the S. aureus." Biomol. NMR Assign. 13, 219-222 (2019).
PubMed: 30729401

Assembly members:

Assembly members:
Extracellular_Adherence_Protein_Homolog_2, polymer, 117 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pT7HMT

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Extracellular_Adherence_Protein_Homolog_2: GSTAEKDKLPATQKAKEMQN VPYTIAVDGIMAFNQSYLNL PKDSQLSYLDLGNKVKALLY DERGVTPEKIRNAKSAVYTI TWKDGSKKEVDLKKDSYTAN LFDSNSIKQIDINVKTK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	319
15N chemical shifts	111
1H chemical shifts	111

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	EapH2	1

Entities:

Entity 1, EapH2 117 residues - Formula weight is not available

1

GLY

SER

THR

ALA

GLU

LYS

ASP

LYS

LEU

PRO

2

ALA

THR

GLN

LYS

ALA

LYS

GLU

MET

GLN

ASN

3

VAL

PRO

TYR

THR

ILE

ALA

VAL

ASP

GLY

ILE

4

MET

ALA

PHE

ASN

GLN

SER

TYR

LEU

ASN

LEU

5

PRO

LYS

ASP

SER

GLN

LEU

SER

TYR

LEU

ASP

6

LEU

GLY

ASN

LYS

VAL

LYS

ALA

LEU

TYR

7

ASP

GLU

ARG

GLY

VAL

THR

PRO

GLU

LYS

ILE

8

ARG

ASN

ALA

LYS

SER

ALA

VAL

TYR

THR

ILE

9

THR

TRP

LYS

ASP

GLY

SER

LYS

GLU

VAL

10

ASP

LEU

LYS

ASP

SER

TYR

THR

ALA

ASN

11

LEU

PHE

ASP

SER

ASN

SER

ILE

LYS

GLN

ILE

12

ASP

ILE

ASN

VAL

LYS

THR

LYS

Samples:

N15C13: Extracellular Adherence Protein Homolog 2, [U-99% 13C; U-99% 15N], 0.75 mM; sodium phosphate 50 mM

N15: Extracellular Adherence Protein Homolog 2, [U-99% 15N], 0.75 mM; sodium phosphate 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	N15	isotropic	sample_conditions_1
3D HNCA	N15C13	isotropic	sample_conditions_1
3D HN(CO)CA	N15C13	isotropic	sample_conditions_1
3D HNCO	N15C13	isotropic	sample_conditions_1
3D HCACO	N15C13	isotropic	sample_conditions_1
3D HNCACB	N15C13	isotropic	sample_conditions_1

Software:

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

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

NMR spectrometers:

Bruker Avance 800 MHz

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