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 17132

Title: Solution Structure of human UBA-like domain of OTUD7A_11_83, NESG target HT6304a/OCSP target OTUD7A_11_83/SGC-Toronto

Deposition date: 2010-08-17 Original release date: 2010-09-02

Authors: Wu, Bin; Yee, Adelinda; Lemak, Alexander; Gutmanas, Aleksandras; Houliston, Scott; Semesi, Anthony; Dhe-Paganon, Sirano; Arrowsmith, Cheryl

Citation: Wu, Bin; Asinas, Abdalin; Yee, Adelinda; Doherty, Ryan; Lemak, Alexander; Gutmanas, Aleksandras; Houliston, Scott; Semesi, Anthony; Arrowsmith, Cheryl; Dhe-Paganon, Sirano. "The amino-terminal UBA domain of OTUD7A"  Not known ., .-..

Assembly members:
OTUD7A_11_83, polymer, 73 residues, 8045.992 Da.

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

Entity Sequences (FASTA):
OTUD7A_11_83: SAECWAALLHDPMTLDMDAV LSDFVRSTGAEPGLARDLLE GKNWDLTAALSDYEQLRQVH TANLPHVFNEGRG

Data typeCount
13C chemical shifts302
15N chemical shifts73
1H chemical shifts483

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1OTUD7A_11_831

Entities:

Entity 1, OTUD7A_11_83 73 residues - 8045.992 Da.

1   SERALAGLUCYSTRPALAALALEULEUHIS
2   ASPPROMETTHRLEUASPMETASPALAVAL
3   LEUSERASPPHEVALARGSERTHRGLYALA
4   GLUPROGLYLEUALAARGASPLEULEUGLU
5   GLYLYSASNTRPASPLEUTHRALAALALEU
6   SERASPTYRGLUGLNLEUARGGLNVALHIS
7   THRALAASNLEUPROHISVALPHEASNGLU
8   GLYARGGLY

Samples:

sample_1: OTUD7A_11_83, [U-100% 13C; U-100% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_2: OTUD7A_11_83, [U-10% 13C; U-99% 15N], 0.5 mM; TRIS, [U-100% 2H], 10 mM; sodium chloride 300 mM; zinc sulphate 10 uM; DTT, [U-100% 2H], 10 mM; benzamidine 10 mM; inhibitor cocktail 1 x; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 300 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1

Software:

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDGUI v1.0, Gutmanas, Arrowsmith - processing

SPARKY v3.95, Goddard - data analysis, peak picking

FMCGUI v2.4, Lemak, Arrowsmith - chemical shift assignment, structure refinement

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

AutoStruct, Huang, Tejero, Powers and Montelione - NMR structure quality assessment

PSVS, Bhattacharya and Montelione - NMR structure quality assessment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
EMBL CAD23047 CAD23048
GB AAH35668 AAI69221 AAI72582 AHW56608 EDL07269
REF NP_001193897 NP_570950 NP_570971 XP_001116351 XP_001492477
SP Q8R554 Q8TE49
TPG DAA17546

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