BMRB Entry 15092

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15092

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Title:
1H, 13C, 15N chemical shift assignments for the human E2 ubiquitin conjugating enzyme Ubc13
Deposition date:
2007-01-03
Original release date:
2007-04-24
Authors:
Mercier, Pascal; Lewis, Michael; Hau, D.; Saltibus, Linda; Xiao, Wei; Spyracopoulos, Leo
Citation:

Citation: Mercier, Pascal; Lewis, Michael; Hau, D.; Saltibus, Linda; Xiao, Wei; Spyracopoulos, Leo. "Structure, Interactions, and Dynamics of the RING Domain from Human TRAF6"  Protein Sci. 16, 602-614 (2007).
PubMed: 17327397

Assembly members:

Assembly members:
Ubc13, polymer, 157 residues, Formula weight is not available

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: pGEX6P1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ubc13: GPLGSMAGLPRRIIKETQRL LAEPVPGIKAEPDESNARYF HVVIAGPQDSPFEGGTFKLE LFLPEEYPMAAPKVRFMTKI YHPNVDKLGRICLDILKDKW SPALQIRTVLLSIQALLSAP NPDDPLANDVAEQWKTNEAQ AIETARAWTRLYAMNNI

Data sets:
Data typeCount
13C chemical shifts423
15N chemical shifts124
1H chemical shifts721

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ubc131

Entities:

Entity 1, Ubc13 157 residues - Formula weight is not available

Residues 1-5 represent a cloning artifact from an affinity tag

1   GLYPROLEUGLYSERMETALAGLYLEUPRO
2   ARGARGILEILELYSGLUTHRGLNARGLEU
3   LEUALAGLUPROVALPROGLYILELYSALA
4   GLUPROASPGLUSERASNALAARGTYRPHE
5   HISVALVALILEALAGLYPROGLNASPSER
6   PROPHEGLUGLYGLYTHRPHELYSLEUGLU
7   LEUPHELEUPROGLUGLUTYRPROMETALA
8   ALAPROLYSVALARGPHEMETTHRLYSILE
9   TYRHISPROASNVALASPLYSLEUGLYARG
10   ILECYSLEUASPILELEULYSASPLYSTRP
11   SERPROALALEUGLNILEARGTHRVALLEU
12   LEUSERILEGLNALALEULEUSERALAPRO
13   ASNPROASPASPPROLEUALAASNASPVAL
14   ALAGLUGLNTRPLYSTHRASNGLUALAGLN
15   ALAILEGLUTHRALAARGALATRPTHRARG
16   LEUTYRALAMETASNASNILE

Samples:

sample_1: Ubc13, [U-13C; U-15N], 0.5 mM; DSS, none, 1 mM; DTT, none, 1 mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, F Delaglio, S Grzesiek, GW Vuister, G Zhu, J Pfeifer and A Bax - processing

SPARKY, T Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAA11675 BAB20414 BAB23941 BAB24239 BAE01994
EMBL CAA71001 CAH65129 CAH92264 CAJ82488 CAK04885
GB AAH00396 AAH03365 AAH34898 AAH44461 AAH53141
REF NP_001012828 NP_001069726 NP_001127530 NP_001156530 NP_001180523
SP P61088 P61089 Q0P5K3 Q4R4I1 Q5R7J6
TPG DAA30062
AlphaFold P61088 P61089 Q0P5K3 Q4R4I1 Q5R7J6

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