BMRB Entry 30157

Name: NMR structure of the E. coli protein NPr, residues 1-85
Published: 2016-09-23

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PDB ID: 5t17
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30157
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR structure of the E. coli protein NPr, residues 1-85 PubMed: 18421563

Deposition date: 2016-08-18 Original release date: 2016-09-23

Authors: Wang, G.; Li, X.; Peterkofsky, A.

Citation: Li, X.; Peterkofsky, A.; Wang, G.. "Solution structure of NPr, a bacterial signal-transducing protein that controls the phosphorylation state of the potassium transporter-regulating protein IIA Ntr." Amino Acids 35, 531-539 (2008).

Assembly members:
entity_1, polymer, 85 residues, 9254.570 Da.

Natural source: Common Name: E. coli Taxonomy ID: 83334 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
entity_1: MTVKQTVEITNKLGMHARPA MKLFELMQGFDAEVLLRNDE GTEAEANSVIALLMLDSAKG RQIEVEATGPQEEEALAAVI ALFNS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	312
15N chemical shifts	88
1H chemical shifts	417

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 85 residues - 9254.570 Da.

1

MET

THR

VAL

LYS

GLN

THR

VAL

GLU

ILE

THR

2

ASN

LYS

LEU

GLY

MET

HIS

ALA

ARG

PRO

ALA

3

MET

LYS

LEU

PHE

GLU

LEU

MET

GLN

GLY

PHE

4

ASP

ALA

GLU

VAL

LEU

ARG

ASN

ASP

GLU

5

GLY

THR

GLU

ALA

GLU

ALA

ASN

SER

VAL

ILE

6

ALA

LEU

MET

LEU

ASP

SER

ALA

LYS

GLY

7

ARG

GLN

ILE

GLU

VAL

GLU

ALA

THR

GLY

PRO

8

GLN

GLU

ALA

LEU

ALA

VAL

ILE

9

ALA

LEU

PHE

ASN

SER

Samples:

sample_1: NPr, [U-13C; U-15N], 1 mM; Tris 25 mM

sample_conditions_1: ionic strength: 25 mM; pH: 7; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
4D HNHC NOESY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1

Software:

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

PIPP, Garrett - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

VNMR, Varian - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

Varian INOVA 600 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts