BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 19220

Title: solution structure of a proteasome related subunit N terminal domain   PubMed: 25631053

Deposition date: 2013-05-03 Original release date: 2015-02-02

Authors: Wu, Yujie; Hu, Yunfei; Jin, Changwen

Citation: Wu, Yujie; Hu, Yunfei; Jin, Changwen. "Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly"  J. Biol. Chem. ., .-. (2015).

Assembly members:
entity, polymer, 163 residues, 18924.596 Da.

Natural source:   Common Name: not available   Taxonomy ID: 4932   Superkingdom: Fungi   Kingdom: Saccharomyces   Genus/species: cerevisiae not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli

Entity Sequences (FASTA):
entity: GSHMFNNHEIDTILSTLRME ADPSLHPLFEQFEKFYEEKL WFQLSESLTKFFDDAKSTPL RLRLYDNFVSKFYDKINQLS VVKYLLASLKDSKDFDESLK YLDDLKAQFQELDSKKQRNN GSKDHGDGILLIDSEIARTY LLKNDLVKARDLLDDLEKTL DKK

Data sets:
Data typeCount
13C chemical shifts670
15N chemical shifts170
1H chemical shifts1045

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1proteasome related subunit N terminal domain1

Entities:

Entity 1, proteasome related subunit N terminal domain 163 residues - 18924.596 Da.

1   GLYSERHISMETPHEASNASNHISGLUILE
2   ASPTHRILELEUSERTHRLEUARGMETGLU
3   ALAASPPROSERLEUHISPROLEUPHEGLU
4   GLNPHEGLULYSPHETYRGLUGLULYSLEU
5   TRPPHEGLNLEUSERGLUSERLEUTHRLYS
6   PHEPHEASPASPALALYSSERTHRPROLEU
7   ARGLEUARGLEUTYRASPASNPHEVALSER
8   LYSPHETYRASPLYSILEASNGLNLEUSER
9   VALVALLYSTYRLEULEUALASERLEULYS
10   ASPSERLYSASPPHEASPGLUSERLEULYS
11   TYRLEUASPASPLEULYSALAGLNPHEGLN
12   GLULEUASPSERLYSLYSGLNARGASNASN
13   GLYSERLYSASPHISGLYASPGLYILELEU
14   LEUILEASPSERGLUILEALAARGTHRTYR
15   LEULEULYSASNASPLEUVALLYSALAARG
16   ASPLEULEUASPASPLEUGLULYSTHRLEU
17   ASPLYSLYS

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.5 mM; sodium phosphate' 'natural abundance; .; .

sample_conditions_1: ionic strength: 0.21 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19219
PDB
DBJ GAA22644
EMBL CAY78927
GB AAB64853 AHY75380 AJP38106 AJU58228 AJU58921
REF NP_010715
SP Q04062
TPG DAA12266

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