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 27442

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for residues 1-136 of yeast Rpn5.   PubMed: 30177392

Deposition date: 2018-04-04 Original release date: 2018-09-19

Authors: Zhang, Wenbo; Zhao, Cong; Hu, Yunfei; Jin, Changwen

Citation: Zhang, Wenbo; Zhao, Cong; Hu, Yunfei; Jin, Changwen. "Solution structure of the N-terminal domain of proteasome lid subunit Rpn5"  Biochem. Biophys. Res. Commun. 504, 225-230 (2018).

Assembly members:
Rpn5, polymer, 136 residues, 15.6 Da.

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: pET-28a (+)

Entity Sequences (FASTA):
Rpn5: MSRDAPIKADKDYSQILKEE FPKIDSLAQNDCNSALDQLL VLEKKTRQASDLASSKEVLA KIVDLLASRNKWDDLNEQLT LLSKKHGQLKLSIQYMIQKV MEYLKSSKSLDLNTRISVIE TIRVVTENKIFVEVER

Data sets:
Data typeCount
13C chemical shifts557
15N chemical shifts144
1H chemical shifts866

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rpn51

Entities:

Entity 1, Rpn5 136 residues - 15.6 Da.

1   METSERARGASPALAPROILELYSALAASP
2   LYSASPTYRSERGLNILELEULYSGLUGLU
3   PHEPROLYSILEASPSERLEUALAGLNASN
4   ASPCYSASNSERALALEUASPGLNLEULEU
5   VALLEUGLULYSLYSTHRARGGLNALASER
6   ASPLEUALASERSERLYSGLUVALLEUALA
7   LYSILEVALASPLEULEUALASERARGASN
8   LYSTRPASPASPLEUASNGLUGLNLEUTHR
9   LEULEUSERLYSLYSHISGLYGLNLEULYS
10   LEUSERILEGLNTYRMETILEGLNLYSVAL
11   METGLUTYRLEULYSSERSERLYSSERLEU
12   ASPLEUASNTHRARGILESERVALILEGLU
13   THRILEARGVALVALTHRGLUASNLYSILE
14   PHEVALGLUVALGLUARG

Samples:

sample_1: Rpn5, [U-95% 13C; U-95% 15N], 0.3 mM; D2O, [U-99% 2H], 10 % v/v; DSS 0.1 mg/mL; DTT 1 mM; sodium phosphate 50 mM; sodium sulfate 50 mM; trifluoroethanol 2 % v/v; sucrose 5 % w/v

sample_conditions_1: ionic strength: 194 mM; pH: 6.0; 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 HNCAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 950 MHz

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