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 11526

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11526

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Title: Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein operating as proteasome assembly chaperone   PubMed: 24065419

Deposition date: 2013-05-20 Original release date: 2013-10-04

Authors: Uekusa, Yoshinori; Okawa, Keisuke; Yagi-Utsumi, Maho; Serve, Olivier; Nakagawa, Yuki; Mizushima, Tsunehiro; Yagi, Hirokazu; Saeki, Yasushi; Tanaka, Keiji; Kato, Koichi

Citation: Uekusa, Yoshinori; Okawa, Keisuke; Yagi-Utsumi, Maho; Serve, Olivier; Nakagawa, Yuki; Mizushima, Tsunehiro; Yagi, Hirokazu; Saeki, Yasushi; Tanaka, Keiji; Kato, Koichi. "Backbone 1H, 13C, and 15N assignments of yeast Ump1, an intrinsically disordered protein that functions as a proteasome assembly chaperone."  Biomol NMR Assign. ., .-. (2013).

Assembly members:
Ump1, polymer, 148 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: pET28b

Entity Sequences (FASTA):
Ump1: MNIVPQDTFKSQVSTDQDKS VLSSAVPSLPDTLRQQEGGA VPLSTQLNDRHPLESTLKNW ETTQRQRQMEQYRQIFGIAE PMKRTMEMEIVNRTDFNPLS TNGSIHRDILLNKECSIDWE DVYPGTGLQASTMVGDDVHS KIEKQLGI

Data sets:
Data typeCount
13C chemical shifts436
15N chemical shifts140
1H chemical shifts527

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ump11

Entities:

Entity 1, Ump1 148 residues - Formula weight is not available

1   METASNILEVALPROGLNASPTHRPHELYS
2   SERGLNVALSERTHRASPGLNASPLYSSER
3   VALLEUSERSERALAVALPROSERLEUPRO
4   ASPTHRLEUARGGLNGLNGLUGLYGLYALA
5   VALPROLEUSERTHRGLNLEUASNASPARG
6   HISPROLEUGLUSERTHRLEULYSASNTRP
7   GLUTHRTHRGLNARGGLNARGGLNMETGLU
8   GLNTYRARGGLNILEPHEGLYILEALAGLU
9   PROMETLYSARGTHRMETGLUMETGLUILE
10   VALASNARGTHRASPPHEASNPROLEUSER
11   THRASNGLYSERILEHISARGASPILELEU
12   LEUASNLYSGLUCYSSERILEASPTRPGLU
13   ASPVALTYRPROGLYTHRGLYLEUGLNALA
14   SERTHRMETVALGLYASPASPVALHISSER
15   LYSILEGLULYSGLNLEUGLYILE

Samples:

sample_1: Ump1, [U-100% 13C; U-100% 15N], 0.2 mM; sodium dihydrogen phosphate 10 mM; disodium hydrogen phosphate 10 mM; DTT, [U-2H], 1 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

ANALYSIS v2.2.2, CCPN - chemical shift assignment

NMR spectrometers:

  • JEOL ECA 920 MHz
  • JEOL ECA 600 MHz
  • Bruker DMX 500 MHz

Related Database Links:

DBJ GAA21719
EMBL CAA05556 CAA85134 CBK39248
GB AAS56452 AHY74651 AJP37249 AJP82145 AJP82535
REF NP_009732
SP P38293
TPG DAA07289
AlphaFold P38293

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