BMRB Entry 19221

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19221
MolProbity Validation Chart

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Title:
solution structure of a proteasome related subunit C terminal domain
Deposition date:
2013-05-03
Original release date:
2015-02-02
Authors:
Wu, Yujie; Hu, Yunfei; Jin, Changwen
Citation:

Citation: Wu, Yujie; Hu, Yunfei; Jin, Changwen. "Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly"  J. Biol. Chem. ., .-. (2015).
PubMed: 25631053

Assembly members:

Assembly members:
entity, polymer, 176 residues, 20247.520 Da.

Natural source:

Natural source:   Common Name: baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: FKNDFNSFYYTSLLYLSTLE PSTSITLAERQQLAYDLSIS ALLGDKIYNFGELLHHPIME TIVNDSNYDWLFQLLNALTV GDFDKFDSLIKVQISKIPIL AQHESFLRQKICLMTLIETV FVKNIRMLSFEDISKATHLP KDNVEHLVMRAISLGLLKGS IDQVNELVTISWVQPR

Data sets:
Data typeCount
13C chemical shifts785
15N chemical shifts187
1H chemical shifts1244

Additional metadata:

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

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

Entities:

Entity 1, proteasome related subunit C terminal domain 176 residues - 20247.520 Da.

1   PHELYSASNASPPHEASNSERPHETYRTYR
2   THRSERLEULEUTYRLEUSERTHRLEUGLU
3   PROSERTHRSERILETHRLEUALAGLUARG
4   GLNGLNLEUALATYRASPLEUSERILESER
5   ALALEULEUGLYASPLYSILETYRASNPHE
6   GLYGLULEULEUHISHISPROILEMETGLU
7   THRILEVALASNASPSERASNTYRASPTRP
8   LEUPHEGLNLEULEUASNALALEUTHRVAL
9   GLYASPPHEASPLYSPHEASPSERLEUILE
10   LYSVALGLNILESERLYSILEPROILELEU
11   ALAGLNHISGLUSERPHELEUARGGLNLYS
12   ILECYSLEUMETTHRLEUILEGLUTHRVAL
13   PHEVALLYSASNILEARGMETLEUSERPHE
14   GLUASPILESERLYSALATHRHISLEUPRO
15   LYSASPASNVALGLUHISLEUVALMETARG
16   ALAILESERLEUGLYLEULEULYSGLYSER
17   ILEASPGLNVALASNGLULEUVALTHRILE
18   SERTRPVALGLNPROARG

Samples:

sample_1: protein, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS 20 mM; sodium chloride 50 mM; DTT 10 mM; DSS 0.03%

sample_conditions_1: ionic strength: 0.07 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_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Bruker Avance 500 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
AlphaFold Q04062

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