BMRB Entry 27087

Name: 1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 3 from triple resonance NMR experiments
Published: 2018-02-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27087

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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 resonance assignments of Staphylococcus aureus extracellular adherence protein domain 3 from triple resonance NMR experiments

Deposition date:

2017-04-28

Original release date:

2018-02-02

Authors:

Herrera, Alvaro; Geisbrecht, Brian; Prakash, Om

Citation:

Citation: Herrera, Alvaro; Ploscariu, Nicoleta; Geisbrecht, Brian; Prakash, Om. "1H, 15N, and 13C resonance assignments of the third domain from the S. aureus innate immune evasion protein Eap" Biomol. NMR Assignments 12, 175-178 (2018).
PubMed: 29372458

Assembly members:

Assembly members:
Extracellular_Adherence_Protein_domain_3, polymer, 98 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_domain_3: GSTVPYSINLNGTSTNILSN LSFSNKPWTNYKNLTSQIKS VLKHDRGISEQDLKYAKKAY YTVYFKNGGKRILQLNSKNY TANLVHAKDVKRIEITVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	225
15N chemical shifts	81
1H chemical shifts	81

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Extracellular Adherence Protein domain 3	1

Entities:

Entity 1, Extracellular Adherence Protein domain 3 98 residues - Formula weight is not available

1

GLY

SER

THR

VAL

PRO

TYR

SER

ILE

ASN

LEU

2

ASN

GLY

THR

SER

THR

ASN

ILE

LEU

SER

ASN

3

LEU

SER

PHE

SER

ASN

LYS

PRO

TRP

THR

ASN

4

TYR

LYS

ASN

LEU

THR

SER

GLN

ILE

LYS

SER

5

VAL

LEU

LYS

HIS

ASP

ARG

GLY

ILE

SER

GLU

6

GLN

ASP

LEU

LYS

TYR

ALA

LYS

ALA

TYR

7

TYR

THR

VAL

TYR

PHE

LYS

ASN

GLY

LYS

8

ARG

ILE

LEU

GLN

LEU

ASN

SER

LYS

ASN

TYR

9

THR

ALA

ASN

LEU

VAL

HIS

ALA

LYS

ASP

VAL

10

LYS

ARG

ILE

GLU

ILE

THR

VAL

LYS

Samples:

sample_1: Extracellular Adherence Protein domain 3, [U-99% 13C; U-99% 15N], 0.75 mM

sample_conditions_1: ionic strength: 60 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	isotropic	sample_conditions_1

Software:

VNMRJ v4.1, Varian - collection

TOPSPIN, Bruker Biospin - collection

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

Cara, Keller and Wuthrich - data analysis

NMR spectrometers:

Bruker Avance 800 MHz
Varian VNMRS 500 MHz

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