BMRB Entry 27502

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for Histidine Kinase NsaS from S. aureus
Published: 2018-07-02

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27502

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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, 13C, and 15N Chemical Shift Assignments for Histidine Kinase NsaS from S. aureus

Deposition date:

2018-06-04

Original release date:

2018-07-02

Authors:

Bhate, Manasi

Citation:

Citation: Bhate, Manasi; Lemmin, Thomas; Kuenze, Georg; Mensa, Bruk; Ganguly, Soumya; Peters, Jason; Schmidt, Nathan; Pelton, Jeffrey; Gross, Carol; Meiler, Jens; DeGrado, William. "Structure and Function of the Transmembrane Domain of NsaS, an Antibiotic Sensing Histidine Kinase in Staphylococcus aureus." J. Am. Chem. Soc. 140, 7471-7485 (2018).
PubMed: 29771498

Assembly members:

Assembly members:
NsaS, polymer, 90 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: pEXP5

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NsaS: MTFLKSIQEIAIVIVIFALF GLMFYLYHLLEAYLLALGVI LLLLIFIGIKYLSFVKTISQ QQQIENLENALYQLKNEQIE YKNGGGCGG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	267
15N chemical shifts	89
1H chemical shifts	186

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NsaS	1

Entities:

Entity 1, NsaS 90 residues - Formula weight is not available

1

MET

THR

PHE

LEU

LYS

SER

ILE

GLN

GLU

ILE

2

ALA

ILE

VAL

ILE

VAL

ILE

PHE

ALA

LEU

PHE

3

GLY

LEU

MET

PHE

TYR

LEU

TYR

HIS

LEU

4

GLU

ALA

TYR

LEU

ALA

LEU

GLY

VAL

ILE

5

LEU

ILE

PHE

ILE

GLY

ILE

LYS

6

TYR

LEU

SER

PHE

VAL

LYS

THR

ILE

SER

GLN

7

GLN

ILE

GLU

ASN

LEU

GLU

ASN

ALA

8

LEU

TYR

GLN

LEU

LYS

ASN

GLU

GLN

ILE

GLU

9

TYR

LYS

ASN

GLY

CYS

GLY

Samples:

sample_1: NsaS, [U-100% 13C; U-100% 15N; U-80% 2H], 750 uM; D2O, [U-2H], 10%; DSS 1%; C14 betaine, [U-2H], 100 mM; MES 40 mM

sample_conditions_1: ionic strength: 40 mM; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker DMX 900 MHz
Bruker DMX 800 MHz

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