BMRB Entry 12040

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR12040

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Title:
1H, 13C and 15N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae
Deposition date:
2019-12-24
Original release date:
2020-02-28
Authors:
Niu, Xiaogang; Ma, Shuaipeng; Hu, Yunfei; Jin, Changwen
Citation:

Citation: Niu, Xiaogang; Ma, Shuaipeng; Hu, Yunfei; Jin, Changwen. "Backbone 1H, 13C and 15N resonance assignments of the proteasome lid subunit Rpn12 from Saccharomyces cerevisiae"  Biomol. NMR Assignments ., .-. (2020).
PubMed: 32072453

Assembly members:

Assembly members:
Rpn12_246, polymer, 246 residues, Formula weight is not available

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: pET-24a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rpn12_246: MPSLAELTKSLSIAFENGDY AACEKLLPPIKIELIKNNLL IPDLSIQNDIYLNDLMITKR ILEVGALASIQTFNFDSFEN YFNQLKPYYFSNNHKLSESD KKSKLISLYLLNLLSQNNTT KFHSELQYLDKHIKNLEDDS LLSYPIKLDRWLMEGSYQKA WDLLQSGSQNISEFDSFTDI LKSAIRDEIAKNTELSYDFL PLSNIKALLFFNNEKETEKF ALERNWPIVNSKVYFNNQSK EKADYE

Data sets:
Data typeCount
13C chemical shifts693
15N chemical shifts227
1H chemical shifts227

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rpn12_2461

Entities:

Entity 1, Rpn12_246 246 residues - Formula weight is not available

1   METPROSERLEUALAGLULEUTHRLYSSER
2   LEUSERILEALAPHEGLUASNGLYASPTYR
3   ALAALACYSGLULYSLEULEUPROPROILE
4   LYSILEGLULEUILELYSASNASNLEULEU
5   ILEPROASPLEUSERILEGLNASNASPILE
6   TYRLEUASNASPLEUMETILETHRLYSARG
7   ILELEUGLUVALGLYALALEUALASERILE
8   GLNTHRPHEASNPHEASPSERPHEGLUASN
9   TYRPHEASNGLNLEULYSPROTYRTYRPHE
10   SERASNASNHISLYSLEUSERGLUSERASP
11   LYSLYSSERLYSLEUILESERLEUTYRLEU
12   LEUASNLEULEUSERGLNASNASNTHRTHR
13   LYSPHEHISSERGLULEUGLNTYRLEUASP
14   LYSHISILELYSASNLEUGLUASPASPSER
15   LEULEUSERTYRPROILELYSLEUASPARG
16   TRPLEUMETGLUGLYSERTYRGLNLYSALA
17   TRPASPLEULEUGLNSERGLYSERGLNASN
18   ILESERGLUPHEASPSERPHETHRASPILE
19   LEULYSSERALAILEARGASPGLUILEALA
20   LYSASNTHRGLULEUSERTYRASPPHELEU
21   PROLEUSERASNILELYSALALEULEUPHE
22   PHEASNASNGLULYSGLUTHRGLULYSPHE
23   ALALEUGLUARGASNTRPPROILEVALASN
24   SERLYSVALTYRPHEASNASNGLNSERLYS
25   GLULYSALAASPTYRGLU

Samples:

sample_1: Rpn12_246, [U-2H; U-13C; U-15N], 0.5 mM; H2O 90%; D2O, [U-2H], 10%; sodium phosphate 50 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.5; pressure: 1 atm; temperature: 298 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 HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

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

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 800 MHz

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