BMRB Entry 17437

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17437

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Title:
1H, 13C and 15N backbone chemical shift assignments of the UBC domain of Ube2S
Deposition date:
2011-01-31
Original release date:
2011-03-09
Authors:
Lorenz, Sonja; Wemmer, David; Kuriyan, John; Pelton, Jeffrey
Citation:

Citation: Wickliffe, Katherine; Lorenz, Sonja; Wemmer, David; Kuriyan, John; Rape, Michael. "The mechanism of linkage-specific ubiquitin chain elongation by a single-subunit e2."  Cell 144, 769-781 (2011).
PubMed: 21376237

Assembly members:

Assembly members:
Ube2S, polymer, 156 residues, 17369 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: SMT3- based system (LifeSensors)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ube2S: MNSNVENLPPHIIRLVYKEV TTLTADPPDGIKVFPNEEDL TDLQVTIEGPEGTPYAGGLF RMKLLLGKDFPASPPKGYFL TKIFHPNVGANGEICVNVLK RDWTAELGIRHVLLTIKCLL IHPNPESALNEEAGRLLLEN YEEYAARARLLTEIHG

Data sets:
Data typeCount
13C chemical shifts262
15N chemical shifts136
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ube2S1

Entities:

Entity 1, Ube2S 156 residues - 17369 Da.

1   METASNSERASNVALGLUASNLEUPROPRO
2   HISILEILEARGLEUVALTYRLYSGLUVAL
3   THRTHRLEUTHRALAASPPROPROASPGLY
4   ILELYSVALPHEPROASNGLUGLUASPLEU
5   THRASPLEUGLNVALTHRILEGLUGLYPRO
6   GLUGLYTHRPROTYRALAGLYGLYLEUPHE
7   ARGMETLYSLEULEULEUGLYLYSASPPHE
8   PROALASERPROPROLYSGLYTYRPHELEU
9   THRLYSILEPHEHISPROASNVALGLYALA
10   ASNGLYGLUILECYSVALASNVALLEULYS
11   ARGASPTRPTHRALAGLULEUGLYILEARG
12   HISVALLEULEUTHRILELYSCYSLEULEU
13   ILEHISPROASNPROGLUSERALALEUASN
14   GLUGLUALAGLYARGLEULEULEUGLUASN
15   TYRGLUGLUTYRALAALAARGALAARGLEU
16   LEUTHRGLUILEHISGLY

Samples:

sample_1: Ube2S, [U-99% 13C; U-99% 15N], 804 uM; sodium phosphate 75mM mM; D2O 7.5%; DSS 30 uM; TCEP 2 mM; H2O 92.5%

sample_2: Ube2S, [U-99% 13C; U-99% 15N], 400 uM; sodium phosphate 75mM mM; D2O 7.5%; DSS 30 uM; TCEP 2 mM; H2O 92.5%

sample_3: Ube2S, [U-99% 13C; U-99% 15N], 1.00 mM; sodium phosphate 75mM mM; D2O 7.5%; DSS 30 uM; TCEP 2 mM; H2O 92.5%

sample_conditions_1: ionic strength: 185 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

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

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

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB93484 BAC25019 BAC25523 BAE27035 BAE32323
GB AAA58446 AAH04236 AAH07554 AAH12255 AAH30171
PIR B42856
REF NP_001069940 NP_001091235 NP_001099694 NP_001252933 NP_001273893
SP A1L3K1 B5DFI8 Q16763 Q1RML1 Q921J4
TPG DAA19381
AlphaFold A1L3K1 B5DFI8 Q16763 Q1RML1 Q921J4

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