BMRB Entry 27093

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27093

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Title:
Chemical shift assignment of human MOZART1 protein (mitotic-spindle organizing protein associated with a ring of gamma-tubulin 1)
Deposition date:
2017-05-04
Original release date:
2017-09-15
Authors:
Cukier, Cyprian; Gervais, Virginie; Milon, Alain
Citation:

Citation: Cukier, Cyprian; Tourdes, Audrey; El-Mazouni, Dounia; Guillet, Valerie; Nomme, Julian; Mourey, Lionel; Milon, Alain; Merdes, Andreas; Gervais, Virginie. "NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex"  Protein Sci. 26, 2240-2248 (2017).
PubMed: 28851027

Assembly members:

Assembly members:
MOZART1, polymer, 85 residues, 8760 Da.

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: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MOZART1: GSHMASSSGAGAAAAAAAAN LNAVRETMDVLLEISRILNT GLDMETLSICVRLCEQGINP EALSSVIKELRKATEALKAA ENMTS

Data sets:
Data typeCount
13C chemical shifts298
15N chemical shifts77
1H chemical shifts471

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MOZART11

Entities:

Entity 1, MOZART1 85 residues - 8760 Da.

N-terminal GSH residues are the result of clonic procedure. This is a full-length MOZART1 protein.

1   GLYSERHISMETALASERSERSERGLYALA
2   GLYALAALAALAALAALAALAALAALAASN
3   LEUASNALAVALARGGLUTHRMETASPVAL
4   LEULEUGLUILESERARGILELEUASNTHR
5   GLYLEUASPMETGLUTHRLEUSERILECYS
6   VALARGLEUCYSGLUGLNGLYILEASNPRO
7   GLUALALEUSERSERVALILELYSGLULEU
8   ARGLYSALATHRGLUALALEULYSALAALA
9   GLUASNMETTHRSER

Samples:

sample_1: MOZART1, [U-99% 13C; U-99% 15N], 0.55 mM; sodium phosphate pH 6.0 10 mM; sodium chloride 50 mM; DTT 2 mM; sulfobetaine-12 30-50 mM; DSS 10 uM

sample_2: MOZART1, [U-99% 13C; U-99% 15N], 0.56 mM; sodium phosphate pH 6.0 10 mM; sodium chloride 50 mM; DTT 2 mM; sulfobetaine-12, d25 (25 protons substituted by deuters), 50 mM; DSS 10 uM

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D BEST-HN(CO)CACBsample_1isotropicsample_conditions_1
3D BEST-HNCACBsample_1isotropicsample_conditions_1
3D BEST-HNCOsample_1isotropicsample_conditions_1
3D BEST-HN(CA)COsample_1isotropicsample_conditions_1
3D HC(C)H-TOCSYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

UNP Q08AG7
AlphaFold Q5W0P5

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