BMRB Entry 18814

Name: 13C and 15N NMR chemical shifts of E. coli full-length H-NS protein
Published: 2014-02-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18814

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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:

13C and 15N NMR chemical shifts of E. coli full-length H-NS protein

Deposition date:

2012-10-31

Original release date:

2014-02-14

Authors:

Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel

Citation:

Citation: Renault, Marie; Garcia, Jesus; Cordeiro, Tiago; Baldus, Marc; Pons, Miquel. "Protein oligomers studied by solid-state NMR--the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein." FEBS J. 280, 2916-2928 (2013).
PubMed: 23601147

Assembly members:

Assembly members:
H-NS, polymer, 137 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
H-NS: MSEALKILNNIRTLRAQARE CTLETLEEMLEKLEVVVNER REEESAAAAEVEERTRKLQQ YREMLIADGIDPNELLNSLA AVKSGTKAKRAQRPAKYSYV DENGETKTWTGQGRTPAVIK KAMDEQGKSLDDFLIKQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	155
15N chemical shifts	7

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	H-NS 1-137	1

Entities:

Entity 1, H-NS 1-137 137 residues - Formula weight is not available

1

MET

SER

GLU

ALA

LEU

LYS

ILE

LEU

ASN

2

ILE

ARG

THR

LEU

ARG

ALA

GLN

ALA

ARG

GLU

3

CYS

THR

LEU

GLU

THR

LEU

GLU

MET

LEU

4

GLU

LYS

LEU

GLU

VAL

ASN

GLU

ARG

5

ARG

GLU

SER

ALA

GLU

6

VAL

GLU

ARG

THR

ARG

LYS

LEU

GLN

7

TYR

ARG

GLU

MET

LEU

ILE

ALA

ASP

GLY

ILE

8

ASP

PRO

ASN

GLU

LEU

ASN

SER

LEU

ALA

9

ALA

VAL

LYS

SER

GLY

THR

LYS

ALA

LYS

ARG

10

ALA

GLN

ARG

PRO

ALA

LYS

TYR

SER

TYR

VAL

11

ASP

GLU

ASN

GLY

GLU

THR

LYS

THR

TRP

THR

12

GLY

GLN

GLY

ARG

THR

PRO

ALA

VAL

ILE

LYS

13

LYS

ALA

MET

ASP

GLU

GLN

GLY

LYS

SER

LEU

14

ASP

PHE

LEU

ILE

LYS

GLN

Samples:

H-NS_(1-137): H-NS, [U-100% 13C; U-100% 15N], 10 mg

H-NS_(1-47): H-NS, [U-100% 13C; U-100% 15N], 15 mg

sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 277 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 13C-13C PDSD	H-NS_(1-47)	solid	sample_conditions_1
2D 15N-13C NCACX	H-NS_(1-47)	solid	sample_conditions_1
2D 15N-13C NCOCX	H-NS_(1-47)	solid	sample_conditions_1
2D 13C-13C PDSD	H-NS_(1-137)	solid	sample_conditions_1
2D 15N-13C NCACX	H-NS_(1-137)	solid	sample_conditions_1
2D 15N-13C NCOCX	H-NS_(1-137)	solid	sample_conditions_1
3D 15N-13C-13C NCOCX	H-NS_(1-137)	solid	sample_conditions_1

Software:

SPARKY v3.115, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 700 MHz