BMRB Entry 25979

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25979
MolProbity Validation Chart

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Title:
protein complex
Deposition date:
2016-02-25
Original release date:
2017-06-19
Authors:
Lu, Xiuxiu; Walters, Kylie
Citation:

Citation: Lu, Xiuxiu; Nowicka, Urszula; Sridharan, Vinidhra; Liu, Fen; Randles, Leah; Hymel, David; Dyba, Marzena; Tarasov, Sergey; Tarasova, Nadya; Zhao, Xue Zhi; Hamazaki, Jun; Murata, Shigeo; Burke, Terrence; Walters, Kylie. "Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets."  Nat. Commun. 8, 15540-15540 (2017).
PubMed: 28598414

Assembly members:

Assembly members:
entity_1, polymer, 111 residues, 13104.049 Da.
entity_2, polymer, 14 residues, 1704.760 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   Vector: pRSET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NKYLVEFRAGKMSLKGTTVT PDKRKGLVYIQQTDDSLIHF CWKDRTSGNVEDDLIIFPDD CEFKRVPQCPSGRVYVLKFK AGSKRLFFWMQEPKTDQDEE HCRKVNEYLNN
entity_2: QEPEPPEPFEYIDD

Data sets:
Data typeCount
13C chemical shifts545
15N chemical shifts128
1H chemical shifts836

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 111 residues - 13104.049 Da.

1   ASNLYSTYRLEUVALGLUPHEARGALAGLY
2   LYSMETSERLEULYSGLYTHRTHRVALTHR
3   PROASPLYSARGLYSGLYLEUVALTYRILE
4   GLNGLNTHRASPASPSERLEUILEHISPHE
5   CYSTRPLYSASPARGTHRSERGLYASNVAL
6   GLUASPASPLEUILEILEPHEPROASPASP
7   CYSGLUPHELYSARGVALPROGLNCYSPRO
8   SERGLYARGVALTYRVALLEULYSPHELYS
9   ALAGLYSERLYSARGLEUPHEPHETRPMET
10   GLNGLUPROLYSTHRASPGLNASPGLUGLU
11   HISCYSARGLYSVALASNGLUTYRLEUASN
12   ASNPROPRO

Entity 2, entity_2 14 residues - 1704.760 Da.

1   GLNGLUPROGLUPROPROGLUPROPHEGLU
2   TYRILEASPASP

Samples:

sample_1: entity_1, [U-13C; U-15N], 0.7 mM; entity_2, [U-13C; U-15N], 0.7 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%; H2O 90%; D2O, [U-2H], 10%

sample_2: entity_1, [U-13C; U-15N], 0.7 mM; entity_2, [U-13C; U-15N], 0.7 mM; potassium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; sodium azide 0.1%; D2O, [U-2H], 100%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298.2 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D half-filtered NOESYsample_2isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking

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

X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

NMR spectrometers:

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

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