BMRB Entry 28111

Name: Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of ALIX-PRD
Published: 2020-08-31

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR28111

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 13C and 15N chemical shift assignments of the N-terminal portion of ALIX-PRD

Deposition date:

2020-03-27

Original release date:

2020-08-31

Authors:

Deshmukh, Lalit; Elias, Ruben

Citation:

Citation: Elias, Ruben; Ma, Wen; Ghirlando, Rodolfo; Schwieters, Charles; Reddy, Vijay; Deshmukh, Lalit. "Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids" Proc. Natl. Acad. Sci. U. S. A. 117, 24274-24284 (2020).
PubMed: 32917811

Assembly members:

Assembly members:
ALIX, polymer, 107 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: pet11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ALIX: GDELLKDLQQSIAREPSAPS IPTPAYQSSPAGGHAPTPPT PAPRTMPPTKPQPPARPPPP VLPANRAPSATAPSPVGAGT AAPAPSQTPGSAPPPQAQGW SHPQFEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	292
15N chemical shifts	106
1H chemical shifts	73

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ALIX	1

Entities:

Entity 1, ALIX 107 residues - Formula weight is not available

1

GLY

ASP

GLU

LEU

LYS

ASP

LEU

GLN

2

SER

ILE

ALA

ARG

GLU

PRO

SER

ALA

PRO

SER

3

ILE

PRO

THR

PRO

ALA

TYR

GLN

SER

PRO

4

ALA

GLY

HIS

ALA

PRO

THR

PRO

THR

5

PRO

ALA

PRO

ARG

THR

MET

PRO

THR

LYS

6

PRO

GLN

PRO

ALA

ARG

PRO

7

VAL

LEU

PRO

ALA

ASN

ARG

ALA

PRO

SER

ALA

8

THR

ALA

PRO

SER

PRO

VAL

GLY

ALA

GLY

THR

9

ALA

PRO

ALA

PRO

SER

GLN

THR

PRO

GLY

10

SER

ALA

PRO

GLN

ALA

GLN

GLY

TRP

11

SER

HIS

PRO

GLN

PHE

GLU

LYS

Samples:

sample_1: ALIX, [U-100% 13C; U-100% 15N], 1.5 mM; D2O, [U-100% 2H], 7%; sodium phosphate 20 mM; sodium chloride 50 mM; EDTA 2 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D (HACA)N(CA)CON	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1

Software:

CCPN, CCPN - data analysis

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 600 MHz

UniProt	Q8WUM4
AlphaFold	Q9UKL5