BMRB Entry 27875

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27875
MolProbity Validation Chart

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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
Deposition date:
2019-04-08
Original release date:
2020-03-11
Authors:
Chen, Xiang; Walters, Kylie
Citation:

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).
PubMed: 32157086

Assembly members:

Assembly members:
entity_1, polymer, 73 residues, Formula weight is not available
entity_2, polymer, 64 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: pGEX6P3

Entity Sequences (FASTA):

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

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts143
1H chemical shifts926

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1hRpn101
2UBE3A2

Entities:

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

1   SERALAASPILEASPALASERSERALAMET
2   ASPTHRSERGLUPROALALYSGLUGLUASP
3   ASPTYRASPVALMETGLNASPPROGLUPHE
4   LEUGLNSERVALLEUGLUASNLEUPROGLY
5   VALASPPROASNASNGLUALAILEARGASN
6   ALAMETGLYSERLEUALASERGLNALATHR
7   LYSASPGLYLYSLYSASPLYSLYSGLUGLU
8   ASPLYSLYS

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

1   METLYSARGALAALAALALYSHISLEUILE
2   GLUARGTYRTYRHISGLNLEUTHRGLUGLY
3   CYSGLYASNGLUALACYSTHRASNGLUPHE
4   CYSALASERCYSPROTHRPHELEUARGMET
5   ASPASNASNALAALAALAILELYSALALEU
6   GLULEUTYRLYSILEASNALALYSLEUCYS
7   ASPPROHISPRO

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 13C-half filter NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D HNCAsample_3isotropicsample_conditions_1
3D HN(CO)CAsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HN(CA)COsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_4isotropicsample_conditions_1
3D 13C-half filter NOESYsample_5isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_5isotropicsample_conditions_1
3D HCCH-TOCSYsample_5isotropicsample_conditions_1
3D CCH-TOCSYsample_5isotropicsample_conditions_1
2D 1H-15N HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_5isotropicsample_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 HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks