BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 18885

Title: S. cerevisiae proteasome regulatory particle ATPase Rpt6 C-terminal domain   PubMed: 23562395

Deposition date: 2012-12-07 Original release date: 2013-02-15

Authors: Ehlinger, Aaron; Walters, Kylie

Citation: Ehlinger, Aaron; Park, Soyeon; Fahmy, Amr; Lary, Jeffrey; Cole, James; Finley, Daniel; Walters, Kylie. "Conformational dynamics of the rpt6 ATPase in proteasome assembly and rpn14 binding."  Structure 21, 753-765 (2013).

Assembly members:
Rpt6, polymer, 99 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRSF-duet1

Entity Sequences (FASTA):
Rpt6: MHHHHHHSQHMPPSVAARAE ILRIHSRKMNLTRGINLRKV AEKMNGCSGADVKGVCTEAG MYALRERRIHVTQEDFELAV GKVMNKNQETAISVAKLFK

Data sets:
Data typeCount
13C chemical shifts299
15N chemical shifts112
1H chemical shifts112

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rpt6 4-helix bundle1
2Rpt6 partially unfolded1

Entities:

Entity 1, Rpt6 4-helix bundle 99 residues - Formula weight is not available

1   METHISHISHISHISHISHISSERGLNHIS
2   METPROPROSERVALALAALAARGALAGLU
3   ILELEUARGILEHISSERARGLYSMETASN
4   LEUTHRARGGLYILEASNLEUARGLYSVAL
5   ALAGLULYSMETASNGLYCYSSERGLYALA
6   ASPVALLYSGLYVALCYSTHRGLUALAGLY
7   METTYRALALEUARGGLUARGARGILEHIS
8   VALTHRGLNGLUASPPHEGLULEUALAVAL
9   GLYLYSVALMETASNLYSASNGLNGLUTHR
10   ALAILESERVALALALYSLEUPHELYS

Samples:

sample_1: Rpt6, [U-100% 13C; U-100% 15N; U-80% 2H], 0.3 mM; beta-mercaptoethanol 14 mM; sodium chloride 60 mM; sodium phosphate 20 mM; H20 90%; D20 10%

sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACOsample_1isotropicsample_conditions_1
2D ZZ-Exchange Spectroscopysample_1isotropicsample_conditions_1

Software:

XEASY, Bartels et al. - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ GAA23341
EMBL CAA47023 CAA96750 CAY79712 CCD24599
GB AAA35138 AAB35417 AAT93154 AHY79325 AJP38743
PRF 1813279A
REF NP_011467 XP_003669842
SP Q01939
TPG DAA08053
AlphaFold Q01939

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