BMRB Entry 26726

Name: Backbone 1H, 15N, and 13C resonance assignments of the Extracellular Adherence Protein Domain 4
Published: 2016-07-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26726

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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:

Backbone 1H, 15N, and 13C resonance assignments of the Extracellular Adherence Protein Domain 4

Deposition date:

2016-01-08

Original release date:

2016-07-14

Authors:

Woehl, Jordan; Takahashi, Daisuke; Herrera, Alvaro; Geisbrecht, Brian; Prakash, Om

Citation:

Citation: Woehl, Jordan; Takahashi, Daisuke; Herrera, Alvaro; Geisbrecht, Brian; Prakash, Om. "1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4" Biomol. NMR Assignments 10, 301-305 (2016).
PubMed: 27372920

Assembly members:

Assembly members:
Eap4, polymer, 98 residues, Formula weight is not available

Natural source:

Natural source: Common Name: firmicutes 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):
Eap4: GSTVPYTIAVNGTSTPILSK LKISNKQLISYKYLNDKVKS VLKSERGISDLDLKFAKQAK YTVYFKNGKKQVVNLKSDIF TPNLFSAKDIKKIDIDVK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	181
15N chemical shifts	92
1H chemical shifts	92

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Domain 4	1

Entities:

Entity 1, Domain 4 98 residues - Formula weight is not available

1

GLY

SER

THR

VAL

PRO

TYR

THR

ILE

ALA

VAL

2

ASN

GLY

THR

SER

THR

PRO

ILE

LEU

SER

LYS

3

LEU

LYS

ILE

SER

ASN

LYS

GLN

LEU

ILE

SER

4

TYR

LYS

TYR

LEU

ASN

ASP

LYS

VAL

LYS

SER

5

VAL

LEU

LYS

SER

GLU

ARG

GLY

ILE

SER

ASP

6

LEU

ASP

LEU

LYS

PHE

ALA

LYS

GLN

ALA

LYS

7

TYR

THR

VAL

TYR

PHE

LYS

ASN

GLY

LYS

8

GLN

VAL

ASN

LEU

LYS

SER

ASP

ILE

PHE

9

THR

PRO

ASN

LEU

PHE

SER

ALA

LYS

ASP

ILE

10

LYS

ILE

ASP

ILE

ASP

VAL

LYS

Samples:

sample_1: Eap4, [U-99% 13C; U-99% 15N], 0.5 – 1.0 mM; sodium phosphate 50 mM; sodium azide 0.1%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 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
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

VNMRJ, Varian - collection

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

TALOS, Cornilescu, Delaglio and Bax - secondary structure prediction

NMR spectrometers:

Varian VNMR 500 MHz
Bruker Avance III 800 MHz

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