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 18297

Title: E2 binding surface on Uba3 beta-grasp domain undergoes a conformational transition   PubMed: 22821745

Deposition date: 2012-02-27 Original release date: 2012-08-29

Authors: Elgin, Emine; Peterson, Francis; Volkman, Brian

Citation: Elgin, E. Sonay; Sokmen, Nazl; Peterson, Francis; Volkman, Brian; Da, Cada; Haas, Arthur. "E2-binding surface on Uba3 -grasp domain undergoes a conformational transition."  Proteins 80, 2482-2487 (2012).

Assembly members:
Uba3, polymer, 97 residues, 10658.173 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Uba3: GSQLPQNIQFSPSAKLQEVL DYLTNSASLQMKSPAITATL EGKNRTLYLQSVTSIEERTR PNLSKTLKELGLVDGQELAV ADVTTPQTVLFKLHFTS

Data sets:
Data typeCount
13C chemical shifts367
15N chemical shifts82
1H chemical shifts591

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Uba31

Entities:

Entity 1, Uba3 97 residues - 10658.173 Da.

The N-terminal GS dipeptide is a cloning artifact.

1   GLYSERGLNLEUPROGLNASNILEGLNPHE
2   SERPROSERALALYSLEUGLNGLUVALLEU
3   ASPTYRLEUTHRASNSERALASERLEUGLN
4   METLYSSERPROALAILETHRALATHRLEU
5   GLUGLYLYSASNARGTHRLEUTYRLEUGLN
6   SERVALTHRSERILEGLUGLUARGTHRARG
7   PROASNLEUSERLYSTHRLEULYSGLULEU
8   GLYLEUVALASPGLYGLNGLULEUALAVAL
9   ALAASPVALTHRTHRPROGLNTHRVALLEU
10   PHELYSLEUHISPHETHRSER

Samples:

sample_1: Uba3, [U-100% 13C; U-100% 15N], 0.4 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 0.02%; sodium azide 90%; sodium azide 10%

sample_conditions_1: ionic strength: 127 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

XEASY, Bartels et al. - chemical shift assignment

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAA33144 BAC27905 BAC33258 BAE35036 BAE38920
EMBL CAB55996 CAG38568 CAH90059 CAH92113 CAH92482
GB AAC27323 AAC27648 AAH02002 AAH22853 AAH80776
REF NP_001069042 NP_001104576 NP_001126234 NP_001128861 NP_001252890
SP Q5R4A0 Q8C878 Q8TBC4 Q99MI7
TPG DAA17089

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