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 17476

Title: The solution structure of the ZnF UBP domain of USP33/VDU1.   PubMed: 17766394

Deposition date: 2011-02-18 Original release date: 2011-03-08

Authors: Allen, Mark; Bycroft, Mark

Citation: Allen, Mark; Bycroft, Mark. "The solution structure of the ZnF UBP domain of USP33/VDU1."  Protein Sci. 16, 2072-2075 (2007).

Assembly members:
zinc_finger, polymer, 95 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: recombinant technology   Host organism: Escherichia coli   Vector: pRSETa (modified)

Entity Sequences (FASTA):
zinc_finger: RNHCPHLDSVGEITKEDLIQ KSLGTCQDCKVQGPNLWACL ENRCSYVGCGESQVDHSTIH SQETKHYLTVNLTTLRVWCY ACSKEVFLDRKLGTQ

Data sets:
Data typeCount
13C chemical shifts313
15N chemical shifts89
1H chemical shifts664

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1zinc-finger1

Entities:

Entity 1, zinc-finger 95 residues - Formula weight is not available

1   ARGASNHISCYSPROHISLEUASPSERVAL
2   GLYGLUILETHRLYSGLUASPLEUILEGLN
3   LYSSERLEUGLYTHRCYSGLNASPCYSLYS
4   VALGLNGLYPROASNLEUTRPALACYSLEU
5   GLUASNARGCYSSERTYRVALGLYCYSGLY
6   GLUSERGLNVALASPHISSERTHRILEHIS
7   SERGLNGLUTHRLYSHISTYRLEUTHRVAL
8   ASNLEUTHRTHRLEUARGVALTRPCYSTYR
9   ALACYSSERLYSGLUVALPHELEUASPARG
10   LYSLEUGLYTHRGLN

Samples:

sample_1: zinc_finger, [U-99% 13C; U-99% 15N], 1.0 mM; MES 20 mM; NaCl 50 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

ANSIG, Kraulis - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

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