BMRB Entry 50948

Name: NEDD8_Q40E
Published: 2021-09-18

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50948

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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:

NEDD8_Q40E

Deposition date:

2021-05-19

Original release date:

2021-09-18

Authors:

Chatterjee, Kiran Sankar; Das, Ranabir

Citation:

Citation: Mohanty, Priyesh; Chatterjee, Kiran Sankar; Das, Ranabir. "NEDD8 Deamidation Inhibits Cullin RING Ligase Dynamics" Front. Immunol. 12, 695331-695331 (2021).
PubMed: 34489942

Assembly members:

Assembly members:
entity_1, polymer, 96 residues, 10724 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: pET-28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MLIKVKTLTGKEIEIDIEPT DKVERIKERVEEKEGIPPQE QRLIYSGKQMNDEKTAADYK ILGGSVLHLVLALRGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
15N chemical shifts	69
1H chemical shifts	69

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	NEDD8_Q40E	1

Entities:

Entity 1, NEDD8_Q40E 96 residues - 10724 Da.

HIS tagged human NEDD8_Q40E sequence. Residues -16 to -10 represent HIS tag followed by (-10 to 0) enzymatic cleavage site.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

LEU

ILE

LYS

VAL

LYS

THR

LEU

THR

GLY

4

LYS

GLU

ILE

GLU

ILE

ASP

ILE

GLU

PRO

THR

5

ASP

LYS

VAL

GLU

ARG

ILE

LYS

GLU

ARG

VAL

6

GLU

LYS

GLU

GLY

ILE

PRO

GLN

GLU

7

GLN

ARG

LEU

ILE

TYR

SER

GLY

LYS

GLN

MET

8

ASN

ASP

GLU

LYS

THR

ALA

ASP

TYR

LYS

9

ILE

LEU

GLY

SER

VAL

LEU

HIS

LEU

VAL

10

LEU

ALA

LEU

ARG

GLY

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 225 mM

sample_conditions_1: ionic strength: 0.162 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRPipe - processing

NMRFAM-SPARKY - chemical shift assignment

NMR spectrometers:

Bruker Avance 800 MHz

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