BMRB Entry 17824

Title:
Rbx1
Deposition date:
2011-08-02
Original release date:
2012-03-26
Authors:
Spratt, Donald; Shaw, Gary
Citation:

Citation: Spratt, Donald; Wu, Kenneth; Kovacev, Jordan; Pan, Zhen-Qiang; Shaw, Gary. "Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase."  J. Biol. Chem. 287, 17374-17385 (2012).
PubMed: 22433864

Assembly members:

Assembly members:
Rbx1, polymer, 100 residues, 11159.5 Da.
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   Vector: pET28a

Data sets:
Data typeCount
13C chemical shifts321
15N chemical shifts76
1H chemical shifts451

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rbx11
2ZINC ION_12
3ZINC ION_22
4ZINC ION_32

Entities:

Entity 1, Rbx1 100 residues - 11159.5 Da.

Residues G9-G11 represent the non-native N-terminus of the protein after TEV cleavage to remove a 6His affinity tag. Residues G1-G8 are spacer residues that were added to maintain proper sequence numbering.

1   GLYGLYGLYGLYTHRASNSERGLYALAGLY
2   LYSLYSARGPHEGLUVALLYSLYSSERASN
3   ALASERALAGLNSERALATRPASPILEVAL
4   VALASPASNCYSALAILECYSARGASNHIS
5   ILEMETASPLEUCYSILEGLUCYSGLNALA
6   ASNGLNALASERALATHRSERGLUGLUCYS
7   THRVALALATRPGLYVALCYSASNHISALA
8   PHEHISPHEHISCYSILESERARGTRPLEU
9   LYSTHRARGGLNVALCYSPROLEUASPASN
10   ARGGLUTRPGLUPHEGLNLYSTYRGLYHIS

Entity 2, ZINC ION_1 - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; entity_1, [U-98% 15N], 700 uM; H2O 90%; D2O 10%

sample_2: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; Rbx1, [U-98% 13C; U-98% 15N], 700 uM; H2O 90%; D2O 10%

sample_3: sodium phosphate 20 mM; sodium chloride 100 mM; DTT 1 mM; Rbx1, [U-98% 13C; U-98% 15N], 700 uM; D2O 100%

sample_conditions_1: ionic strength: 0.120 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_3isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_3isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1

Software:

VNMRJ vVarian VnmrJ 2.2D, Varian - collection

NMRPipe v2009.015.15.35, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw vVer 5.0 Rev 2009.244.15.09, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView v8.0.rc47 with Java 1.6.0_26, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TALOS vTALOSPlus, Cornilescu, Delaglio and Bax - geometry optimization

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB EAW60402 EKC33263 KFM64926 KFP48973 KFQ68825
REF XP_004063570 XP_008474369 XP_010219658 XP_011232809 XP_011232810

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