BMRB Entry 26708

Name: Backbone Assignment of Human NEMO residues 258-350
Published: 2016-01-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26708

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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 Assignment of Human NEMO residues 258-350

Deposition date:

2015-11-24

Original release date:

2016-01-14

Authors:

Halander, Jenny; Messias, Ana; Geerlof, Arie; Sattler, Michael

Citation:

Citation: Vincendeau, Michelle; Kamyar, Hadian; Messias, Ana; Brenke, Jara; Halander, Jenny; Griesbach, Richard; Greczmiel, Ute; Bertossi, Arianna; Stehle, Ralf; Nagel, Daniel; Demski, Kathrin; Velvarska, Hana; Niessing, Dierk; Geerlof, Arie; Sattler, Michael; Krappmann, Daniel. "Inhibition of Canonical NF-kB Signaling by a Small Molecule Targeting NEMO-Ubiquitin Interaction" Sci. Rep. 6, 18934-18934 (2016).
PubMed: 26740240

Assembly members:

Assembly members:
NEMO, polymer, 95 residues, 11011.5 Da.

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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
NEMO: GAMQLEDLKQQLQQAEEALV AKQEVIDKLKEEAEQHKIVM ETVPVLKAQADIYKADFQAE RQAREKLAEKKELLQEQLEQ LQREYSKLKASCQES

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	148
15N chemical shifts	75
1H chemical shifts	75

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NEMO 1	1
2	NEMO 2	1

Entities:

Entity 1, NEMO 1 95 residues - 11011.5 Da.

Residues 1-2 are non-native residues that remain after cleavage of the N-terminal affinity tag.

1

GLY

ALA

MET

GLN

LEU

GLU

ASP

LEU

LYS

GLN

2

GLN

LEU

GLN

ALA

GLU

ALA

LEU

VAL

3

ALA

LYS

GLN

GLU

VAL

ILE

ASP

LYS

LEU

LYS

4

GLU

ALA

GLU

GLN

HIS

LYS

ILE

VAL

MET

5

GLU

THR

VAL

PRO

VAL

LEU

LYS

ALA

GLN

ALA

6

ASP

ILE

TYR

LYS

ALA

ASP

PHE

GLN

ALA

GLU

7

ARG

GLN

ALA

ARG

GLU

LYS

LEU

ALA

GLU

LYS

8

LYS

GLU

LEU

GLN

GLU

GLN

LEU

GLU

GLN

9

LEU

GLN

ARG

GLU

TYR

SER

LYS

LEU

LYS

ALA

10

SER

CYS

GLN

GLU

SER

Samples:

sample_1: NEMO, [U-13C; U-15N; U-2H], 1.2 mM; D2O 10%; H2O 90%; sodium phosphate 50 mM; sodium NaCl 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.0; pressure: 1 atm; temperature: 308 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	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
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

Bruker AV III 800 MHz

UNIPROT	Q9Y6K9
PDB	4BWN
AlphaFold	Q7Z7F1