BMRB Entry 15063

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15063
MolProbity Validation Chart

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Title:
NMR structure of the mouse thiamine triphosphatase
Deposition date:
2006-12-05
Original release date:
2007-02-23
Authors:
Song, Jikui; Markley, John
Citation:

Citation: Song, Jikui; Bettendorff, Lucien; Tonelli, Marco; Markley, John. "Structural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphatase."  J. Biol. Chem. 283, 10939-10948 (2008).
PubMed: 18276586

Assembly members:

Assembly members:
ThTPase_MOUSE, polymer, 224 residues, 24253.369 Da.

Natural source:

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PVP13

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ThTPase_MOUSE: SAQGLIEVERKFAPGPDTEE RLQELGATLEHRVTFRDTYY DTSELSLMLSDHWLRQREGS GWELKCPGVTGVSGPHNEYV EVTSEAAIVAQLFELLGSGE QKPAGVAAVLGSLKLQEVAS FITTRSSWKLALSGAHGQEP QLTIDLDSADFGYAVGEVEA MVHEKAEVPAALEKIITVSS MLGVPAQEEAPAKLMVYLQR FRPLDYQRLLEAASSGEATG DSAS

Data typeCount
13C chemical shifts876
15N chemical shifts229
1H chemical shifts1378

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ThTPase mouse1

Entities:

Entity 1, ThTPase mouse 224 residues - 24253.369 Da.

1   SERALAGLNGLYLEUILEGLUVALGLUARG
2   LYSPHEALAPROGLYPROASPTHRGLUGLU
3   ARGLEUGLNGLULEUGLYALATHRLEUGLU
4   HISARGVALTHRPHEARGASPTHRTYRTYR
5   ASPTHRSERGLULEUSERLEUMETLEUSER
6   ASPHISTRPLEUARGGLNARGGLUGLYSER
7   GLYTRPGLULEULYSCYSPROGLYVALTHR
8   GLYVALSERGLYPROHISASNGLUTYRVAL
9   GLUVALTHRSERGLUALAALAILEVALALA
10   GLNLEUPHEGLULEULEUGLYSERGLYGLU
11   GLNLYSPROALAGLYVALALAALAVALLEU
12   GLYSERLEULYSLEUGLNGLUVALALASER
13   PHEILETHRTHRARGSERSERTRPLYSLEU
14   ALALEUSERGLYALAHISGLYGLNGLUPRO
15   GLNLEUTHRILEASPLEUASPSERALAASP
16   PHEGLYTYRALAVALGLYGLUVALGLUALA
17   METVALHISGLULYSALAGLUVALPROALA
18   ALALEUGLULYSILEILETHRVALSERSER
19   METLEUGLYVALPROALAGLNGLUGLUALA
20   PROALALYSLEUMETVALTYRLEUGLNARG
21   PHEARGPROLEUASPTYRGLNARGLEULEU
22   GLUALAALASERSERGLYGLUALATHRGLY
23   ASPSERALASER

Samples:

sample: ThTPase_MOUSE, [U-100% 13C; U-100% 15N], 1.0 mM; MOPS 10 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H,15N-HSQCsampleisotropicsample_conditions_1
1H,13C-HSQCsampleisotropicsample_conditions_1
HNCACBsampleisotropicsample_conditions_1
CBCACONHsampleisotropicsample_conditions_1
CCONHsampleisotropicsample_conditions_1
HCCHTOCSYsampleisotropicsample_conditions_1
HBACONHsampleisotropicsample_conditions_1
13C-EDITED 1H,1H-NOESYsampleisotropicsample_conditions_1
15N-EDITED 1H,1H-NOESYsampleisotropicsample_conditions_1
13C-EDITED AROMATIC 1H,1H-NOESYsampleisotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

xwinnmr v3.5, Bruker - collection

NMRPipe v97.027.12.56, Delagio,F. et al. - processing

SPARKY v3.113, Goddard,T.D. and Kneller,D.G. - data analysis

GARANT v2.1, Bartels,C. et al - data analysis

CYANA v2.1, Guntert,P. et al - structural calculation

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker DMX 750 MHz
  • Varian INOVA 900 MHz

Related Database Links:

PDB
DBJ BAE21189
GB AAH25562 AAM22405 EDL36308
REF NP_694723
SP Q8JZL3
AlphaFold Q8JZL3

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