BMRB Entry 27587

Name: Backbone 1H, 13C and 15N Chemical Shift Assignments for UBE2E1 core domain
Published: 2019-06-04

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27587

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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 1H, 13C and 15N Chemical Shift Assignments for UBE2E1 core domain

Deposition date:

2018-08-24

Original release date:

2019-06-04

Authors:

Anandapadamanaban, Madhanagopal; Csizmok, Veronika; Ahlner, Alexandra; Sunnerhagen, Maria

Citation:

Citation: Anandapadamanaban, Madhanagopal; Kyriakidis, Nikolaos; Csizmok, Veronika; Wallenhammar, Amelie; Espinosa, Alexander; Ahlner, Alexandra; Round, Adam; Trewella, Jill; Moche, Martin; Wahren-Herlenius, Marie; Sunnerhagen, Maria. "E3 ubiquitin-protein ligase TRIM21-mediated lysine capture by UBE2E1 reveals substrate-targeting mode of a ubiquitin-conjugating E2" J. Biol. Chem. 294, 11404-11419 (2019).
PubMed: 31160341

Assembly members:

Assembly members:
UBE2E1, polymer, 157 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: pET28b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
UBE2E1: SMSKNSKLLSTSAARIKQEL ADITLDPPPNCAAGPPGDNI YEWRSTILGPPGSVYEGGVF FLDITFTPEYPFFPPKVTFR TRIYHCNINSQGVISLDILL DNWSPALTISSVLLSICSLL TDCNPADPLVGSIATQYMTN RAEHDRMARQWTTRYAT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	368
15N chemical shifts	123
1H chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	UBE2E1 core domain, subunit 1	1
2	UBE2E1 core domain, subunit 2	1

Entities:

Entity 1, UBE2E1 core domain, subunit 1 157 residues - Formula weight is not available

1

SER

MET

SER

LYS

ASN

SER

LYS

LEU

SER

2

THR

SER

ALA

LYS

ARG

ILE

LYS

GLU

LEU

3

ALA

ASP

ILE

THR

LEU

ASP

PRO

ASN

4

CYS

ARG

ALA

GLY

PRO

LYS

GLY

ASP

ASN

ILE

5

TYR

GLU

TRP

ARG

SER

THR

ILE

LEU

GLY

PRO

6

PRO

GLY

SER

VAL

TYR

GLU

GLY

VAL

PHE

7

PHE

LEU

ASP

ILE

THR

PHE

THR

PRO

GLU

TYR

8

PRO

PHE

LYS

PRO

LYS

VAL

THR

PHE

ARG

9

THR

ARG

ILE

TYR

HIS

CYS

ASN

ILE

ASN

SER

10

GLN

GLY

VAL

ILE

SER

LEU

ASP

ILE

LEU

LYS

11

ASP

ASN

TRP

SER

PRO

ALA

LEU

THR

ILE

SER

12

LYS

VAL

LEU

SER

ILE

CYS

SER

LEU

13

THR

ASP

CYS

ASN

PRO

ALA

ASP

PRO

LEU

VAL

14

GLY

SER

ILE

ALA

THR

GLN

TYR

MET

THR

ASN

15

ARG

ALA

GLU

HIS

ASP

ARG

MET

ALA

ARG

GLN

16

TRP

THR

LYS

ARG

TYR

ALA

THR

Samples:

sample_1: UBE2E1, [U-100% 13C; U-100% 15N], 0.4 mM; TRIS 50 mM; sodium chloride 100 mM; sodium azide 0.02 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 8.0; pressure: 1 atm; temperature: 303.73 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

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