BMRB Entry 50765

Name: Assignments of free human Tsg101 UEV domain
Published: 2023-09-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50765

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:

Assignments of free human Tsg101 UEV domain

Deposition date:

2021-02-16

Original release date:

2023-09-11

Authors:

Moschidi, Danai; Cantrelle, Francois-Xavier; Hanoulle, Xavier

Citation:

Citation: Moschidi, Danai; Cantrelle, Francois-Xavier; Boll, Emmanuelle; Hanoulle, Xavier. "Backbone NMR resonance assignment of the apo human Tsg101-UEV domain" Biomol. NMR Assignm. 17, 49-54 (2023).
PubMed: 36740661

Assembly members:

Assembly members:
entity_1, polymer, 147 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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMAVSESQLKKMVSKYKYR DLTVRETVNVITLYKDLKPV LDSYVFNDGSSRELMNLTGT IPVPYRGNTYNIPICLWLLD TYPYNPPICFVKPTSSMTIK TGKHVDANGKIYLPYLHEWK HPQSDLLGLIQVMIVVFGDE PPVFSRP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	441
15N chemical shifts	156
1H chemical shifts	308

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tsg101_UEV	1

Entities:

Entity 1, Tsg101_UEV 147 residues - Formula weight is not available

The author sequence numbering is the Uniprot Q99816 numbering without the 2 first residues from polymer sequence due to cloning tag.

1

GLY

ALA

MET

ALA

VAL

SER

GLU

SER

GLN

LEU

2

LYS

MET

VAL

SER

LYS

TYR

LYS

TYR

ARG

3

ASP

LEU

THR

VAL

ARG

GLU

THR

VAL

ASN

VAL

4

ILE

THR

LEU

TYR

LYS

ASP

LEU

LYS

PRO

VAL

5

LEU

ASP

SER

TYR

VAL

PHE

ASN

ASP

GLY

SER

6

SER

ARG

GLU

LEU

MET

ASN

LEU

THR

GLY

THR

7

ILE

PRO

VAL

PRO

TYR

ARG

GLY

ASN

THR

TYR

8

ASN

ILE

PRO

ILE

CYS

LEU

TRP

LEU

ASP

9

THR

TYR

PRO

TYR

ASN

PRO

ILE

CYS

PHE

10

VAL

LYS

PRO

THR

SER

MET

THR

ILE

LYS

11

THR

GLY

LYS

HIS

VAL

ASP

ALA

ASN

GLY

LYS

12

ILE

TYR

LEU

PRO

TYR

LEU

HIS

GLU

TRP

LYS

13

HIS

PRO

GLN

SER

ASP

LEU

GLY

LEU

ILE

14

GLN

VAL

MET

ILE

VAL

PHE

GLY

ASP

GLU

15

PRO

VAL

PHE

SER

ARG

PRO

Samples:

sample_1: Tsg101_UEV, [U-99% 13C; U-99% 15N], 330 uM; sodium phosphate 50 mM; sodium chloride 50 mM; EDTA 0.1 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 6.1; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCANH	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HN(CA)NNH	sample_1	isotropic	sample_conditions_1
3D HCAN	sample_1	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D (H)CACON	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
2D CACO	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY - chemical shift assignment, data analysis, peak picking

TOPSPIN - collection

NMRPipe - processing

qMDD - processing

NMR spectrometers:

Bruker AVANCE III HD 600 MHz