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 11260

Title: Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1)

Deposition date: 2010-08-09 Original release date: 2011-08-17

Authors: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.

Citation: Zhao, C.; Tomizawa, T.; Koshiba, S.; Inoue, M.; Kigawa, T.; Yokoyama, S.. "Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1)"  .

Assembly members:
UBA domain, polymer, 63 residues, Formula weight is not available

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

Experimental source:   Production method: cell free synthesis' 'E. coli - cell free' 'E. coli

Entity Sequences (FASTA):
UBA domain: GSSGSSGAYSELQMLSPSER QCVETVVNMGYSYECVLRAM KKKGENIEQILDYLFAHSGP SSG

Data sets:
Data typeCount
13C chemical shifts245
15N chemical shifts57
1H chemical shifts387

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1UBA domain1

Entities:

Entity 1, UBA domain 63 residues - Formula weight is not available

1   GLYSERSERGLYSERSERGLYALATYRSER
2   GLULEUGLNMETLEUSERPROSERGLUARG
3   GLNCYSVALGLUTHRVALVALASNMETGLY
4   TYRSERTYRGLUCYSVALLEUARGALAMET
5   LYSLYSLYSGLYGLUASNILEGLUGLNILE
6   LEUASPTYRLEUPHEALAHISSERGLYPRO
7   SERSERGLY

Samples:

sample_1: UBA domain mM; d-Tris-HCl 20 mM; NaCl 100 mM; d-DTT 1 mM; NaN3 0.02%; H2O 90%; D2O 10%

condition_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298.0 K

Experiments:

NameSampleSample stateSample conditions
3D 13C-separated NOESYsample_1isotropiccondition_1
3D 15N-separated NOESYsample_1isotropiccondition_1

Software:

xwinnmr v2.6, Bruker - collection

NMRPipe v20020425, Delaglio, F. - processing

NMRView v5.0.4, Johnson, B. A. - data analysis

Kujira v0.8996, Kobayashi, N. - data analysis

CYANA v1.0.7, Guntert, P. - refinement, structure solution

NMR spectrometers:

  • Bruker AVANCE 800 MHz

Related Database Links:

PDB
DBJ BAC11162 BAC11176 BAC11224 BAC11323 BAC11342
EMBL CAB66667 CAG38582 CAL38740
GB AAF37827 AAH20950 AAH98141 AAH98316 AAH99726
REF NP_001164672 NP_001164673 NP_001164674 NP_001164675 NP_001253443
SP Q9NZ09

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