BMRB Entry 26655

Name: 1H, 13C and 15N resonance assignments of the intrinsically disordered region of the nuclear envelope protein emerin
Published: 2016-02-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26655

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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, 13C and 15N resonance assignments of the intrinsically disordered region of the nuclear envelope protein emerin

Deposition date:

2015-09-11

Original release date:

2016-02-12

Authors:

Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie

Citation:

Citation: Samson, Camille; Herrada, Isaline; Celli, Florian; Theillet, Francois-Xavier; Zinn-Justin, Sophie. "1H, 13C and 15N backbone resonance assignment of the intrinsically disordered region of the nuclear envelope protein emerin" Biomol. NMR Assign. 10, 179-182 (2016).
PubMed: 26725056

Assembly members:

Assembly members:
emerin_67-170, polymer, 105 residues, Formula weight is not available

Natural source:

Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM-13

Entity Sequences (FASTA):

Entity Sequences (FASTA):
emerin_67-170: GTRGDADMYDLPKKEDALLY QSKGYNDDYYEESYFTTRTY GEPESAGPSRAVRQSVTSFP DADAFHHQVHDDDLLSSSEE ECKDRERPMYGRDSAYQSIT HYRPV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	202
15N chemical shifts	96
1H chemical shifts	96

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	emerin 67-170	1

Entities:

Entity 1, emerin 67-170 105 residues - Formula weight is not available

1

GLY

THR

ARG

GLY

ASP

ALA

ASP

MET

TYR

ASP

2

LEU

PRO

LYS

GLU

ASP

ALA

LEU

TYR

3

GLN

SER

LYS

GLY

TYR

ASN

ASP

TYR

4

GLU

SER

TYR

PHE

THR

ARG

THR

TYR

5

GLY

GLU

PRO

GLU

SER

ALA

GLY

PRO

SER

ARG

6

ALA

VAL

ARG

GLN

SER

VAL

THR

SER

PHE

PRO

7

ASP

ALA

ASP

ALA

PHE

HIS

GLN

VAL

HIS

8

ASP

LEU

SER

GLU

9

GLU

CYS

LYS

ASP

ARG

GLU

ARG

PRO

MET

TYR

10

GLY

ARG

ASP

SER

ALA

TYR

GLN

SER

ILE

THR

11

HIS

TYR

ARG

PRO

VAL

Samples:

sample_1: emerin 67-170, [U-100% 13C; U-100% 15N], 500 uM; urea 8 M; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 30 mM; pH: 6.5; pressure: 1 atm; temperature: 303 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 HCACO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker Avance 750 MHz

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