BMRB Entry 31043

Name: UBE3A isoform 3 AZUL
Published: 2023-10-16

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PDB ID: 8enp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31043
MolProbity Validation Chart

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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:

UBE3A isoform 3 AZUL

Deposition date:

2022-09-30

Original release date:

2023-10-16

Authors:

Bregnard, T.; Bezsonova, I.

Citation:

Citation: Bregnard, T.; Fairchild, D.; Chen, X.; Erlandsen, H.; Walters, K.; Korzhnev, D.; Bezsonova, I.. "Differences in structure, dynamics and Zn-coordination between isoforms of human ubiquitin ligase UBE3A" .

Assembly members:

Assembly members:
entity_1, polymer, 87 residues, 9630.942 Da.
entity_ZN, non-polymer, 65.409 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 BL21 Vector: pET28b+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSHMATACKRSGEPQSDDIE ASRMKRAAAKHLIERYYHQL TEGCGNEACTNEFCASCPTF LRMDNNAAAIKALELYKINA KLCDPHP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list
- spectral_peak_list_1
- spectral_peak_list_2

Data type	Count
13C chemical shifts	331
15N chemical shifts	87
1H chemical shifts	542

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1
2	unit_2	2

Entities:

Entity 1, unit_1 87 residues - 9630.942 Da.

1

GLY

SER

HIS

MET

ALA

THR

ALA

CYS

LYS

ARG

2

SER

GLY

GLU

PRO

GLN

SER

ASP

ILE

GLU

3

ALA

SER

ARG

MET

LYS

ARG

ALA

LYS

4

HIS

LEU

ILE

GLU

ARG

TYR

HIS

GLN

LEU

5

THR

GLU

GLY

CYS

GLY

ASN

GLU

ALA

CYS

THR

6

ASN

GLU

PHE

CYS

ALA

SER

CYS

PRO

THR

PHE

7

LEU

ARG

MET

ASP

ASN

ALA

ILE

8

LYS

ALA

LEU

GLU

LEU

TYR

LYS

ILE

ASN

ALA

9

LYS

LEU

CYS

ASP

PRO

HIS

PRO

Entity 2, unit_2 - Zn - 65.409 Da.

1

ZN

Samples:

sample_1: UBE3A iso 3 AZUL, [U-99% 13C; U-99% 15N], 1.7 mM; MOPS 10 mM; sodium chloride 450 mM; beta-mercaptoethanol 10 mM; zinc sulfate 10 uM

sample_conditions_1: ionic strength: 450 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMRFAM-SPARKY, Lee, Tonelli, and Markley - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

NMR spectrometers:

Agilent VNMRS 800 MHz

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