BMRB Entry 52051

Name: Backbone resonance assignments for UBE2T
Published: 2023-09-30

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52051

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 resonance assignments for UBE2T

Deposition date:

2023-07-21

Original release date:

2023-09-30

Authors:

Wei, Qi; Kang, Congbao

Citation:

Citation: Huang, Qiwei; Ng, Hui Qi; Loh, Yong Yao; Ke, Zhiyuan; Lim, Wan Hsin; Kang, CongBao. "Backbone 1H, 15N and 13C resonance assignments for an E2 ubiquitin conjugating enzyme-UBE2T" Biomol. NMR Assignments 17, 269-274 (2023).
PubMed: 37773242

Assembly members:

Assembly members:
entity_1, polymer, 154 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MQRASRLKRELHMLATEPPP GITCWQDKDQMDDLRAQILG GANTPYEKGVFKLEVIIPER YPFEPPQIRFLTPIYHPNID SAGRICLDVLKLPPKGAWRP SLNIATVLTSIQLLMSEPNP DDPLMADISSEFKYNKPAFL KNARQWTEKHARQK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	399
15N chemical shifts	132
1H chemical shifts	347

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBE2T	1

Entities:

Entity 1, UBE2T 154 residues - Formula weight is not available

1

MET

GLN

ARG

ALA

SER

ARG

LEU

LYS

ARG

GLU

2

LEU

HIS

MET

LEU

ALA

THR

GLU

PRO

3

GLY

ILE

THR

CYS

TRP

GLN

ASP

LYS

ASP

GLN

4

MET

ASP

LEU

ARG

ALA

GLN

ILE

LEU

GLY

5

GLY

ALA

ASN

THR

PRO

TYR

GLU

LYS

GLY

VAL

6

PHE

LYS

LEU

GLU

VAL

ILE

PRO

GLU

ARG

7

TYR

PRO

PHE

GLU

PRO

GLN

ILE

ARG

PHE

8

LEU

THR

PRO

ILE

TYR

HIS

PRO

ASN

ILE

ASP

9

SER

ALA

GLY

ARG

ILE

CYS

LEU

ASP

VAL

LEU

10

LYS

LEU

PRO

LYS

GLY

ALA

TRP

ARG

PRO

11

SER

LEU

ASN

ILE

ALA

THR

VAL

LEU

THR

SER

12

ILE

GLN

LEU

MET

SER

GLU

PRO

ASN

PRO

13

ASP

PRO

LEU

MET

ALA

ASP

ILE

SER

14

GLU

PHE

LYS

TYR

ASN

LYS

PRO

ALA

PHE

LEU

15

LYS

ASN

ALA

ARG

GLN

TRP

THR

GLU

LYS

HIS

16

ALA

ARG

GLN

LYS

Samples:

sample_1: UBE2T, [U-100% 13C; U-100% 15N], 0.75 mM; sodium phosphate 20 mM; NaCl 150 mM; DTT 1 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.5; pressure: 1 atm; temperature: 298 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(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1 - collection

NMRPipe - processing

CYANA v3.98 - processing

NMRViewJ - chemical shift assignment

NMR spectrometers:

Bruker Avance 600 MHz

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