BMRB Entry 27875

Name: Solution Structure of the RAZUL domain from 26S proteasome subunit hRpn10/S5a complexed with the AZUL domain from E3 ligase E6AP/UBE3A
Published: 2020-03-11

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27875

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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: Solution Structure of the RAZUL domain from 26S proteasome subunit hRpn10/S5a complexed with the AZUL domain from E3 ligase E6AP/UBE3A PubMed: 32157086

Deposition date: 2019-04-08 Original release date: 2020-03-11

Authors: Chen, Xiang; Walters, Kylie

Citation: Buel, Gwen; Chen, Xiang; Chari, Raj; O'Neill, Maura; Ebelle, Danielle; Jenkins, Conor; Sridharan, Vinidhra; Tarasov, Sergey; Tarasova, Nadya; Andresson, Thorkell; Walters, Kylie. "Structure of E3 ligase E6AP with a proteasome-binding site provided by substrate receptor hRpn10" Nat. Commun. 11, 1291-1291 (2020).

Assembly members:
entity_1, polymer, 73 residues, Formula weight is not available
entity_2, polymer, 64 residues, Formula weight is not available

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source: Production method: recombinant technology Host organism: Escherichia coli

Entity Sequences (FASTA):
entity_1: SADIDASSAMDTSEPAKEED DYDVMQDPEFLQSVLENLPG VDPNNEAIRNAMGSLASQAT KDGKKDKKEEDKK
entity_2: MKRAAAKHLIERYYHQLTEG CGNEACTNEFCASCPTFLRM DNNAAAIKALELYKINAKLC DPHP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	549
15N chemical shifts	143
1H chemical shifts	926

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hRpn10	1
2	UBE3A	2

Entities:

Entity 1, hRpn10 73 residues - Formula weight is not available

1

SER

ALA

ASP

ILE

ASP

ALA

SER

ALA

MET

2

ASP

THR

SER

GLU

PRO

ALA

LYS

GLU

ASP

3

ASP

TYR

ASP

VAL

MET

GLN

ASP

PRO

GLU

PHE

4

LEU

GLN

SER

VAL

LEU

GLU

ASN

LEU

PRO

GLY

5

VAL

ASP

PRO

ASN

GLU

ALA

ILE

ARG

ASN

6

ALA

MET

GLY

SER

LEU

ALA

SER

GLN

ALA

THR

7

LYS

ASP

GLY

LYS

ASP

LYS

GLU

8

ASP

LYS

Entity 2, UBE3A 64 residues - Formula weight is not available

1

MET

LYS

ARG

ALA

LYS

HIS

LEU

ILE

2

GLU

ARG

TYR

HIS

GLN

LEU

THR

GLU

GLY

3

CYS

GLY

ASN

GLU

ALA

CYS

THR

ASN

GLU

PHE

4

CYS

ALA

SER

CYS

PRO

THR

PHE

LEU

ARG

MET

5

ASP

ASN

ALA

ILE

LYS

ALA

LEU

6

GLU

LEU

TYR

LYS

ILE

ASN

ALA

LYS

LEU

CYS

7

ASP

PRO

HIS

PRO

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2 0.75 mM; MOPS 10 mM; sodium chloride 50 mM; DTT 10 mM; ZnSO4 10 uM; sodium azide 0.1%; pefabloc 1 mM

sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2 0.75 mM; MOPS 10 mM; sodium chloride 50 mM; DTT 10 mM; ZnSO4 10 uM; sodium azide 0.1%; pefabloc 1 mM

sample_3: entity_2, [U-100% 13C; U-100% 15N], 0.5 mM; entity_1 0.75 mM; MOPS 10 mM; sodium chloride 50 mM; DTT 10 mM; ZnSO4 10 uM; sodium azide 0.1%; pefabloc 1 mM

sample_4: entity_2, [U-100% 15N], 0.5 mM; entity_1 0.75 mM; MOPS 10 mM; sodium chloride 50 mM; DTT 10 mM; ZnSO4 10 uM; sodium azide 0.1%; pefabloc 1 mM

sample_5: entity_2, [U-100% 15N], 0.5 mM; entity_1 0.75 mM; MOPS 10 mM; sodium chloride 50 mM; DTT 10 mM; ZnSO4 10 uM; sodium azide 0.1%; pefabloc 1 mM

sample_conditions_1: ionic strength: 50 mM; 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 1H-15N NOESY	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 HNCO	sample_1	isotropic	sample_conditions_1
3D 13C-half filter NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_3	isotropic	sample_conditions_1
3D HN(CO)CA	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HN(CA)CO	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_4	isotropic	sample_conditions_1
3D 13C-half filter NOESY	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_5	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_5	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_5	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_5	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

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

XEASY, Bartels et al. - data analysis, peak picking

NMR spectrometers:

Bruker Avance 850 MHz
Bruker Avance 700 MHz
Bruker Avance 600 MHz
Bruker Avance 800 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts