BMRB Entry 17636

Title:
1H, 13C, and 15N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR
Deposition date:
2011-05-12
Original release date:
2011-09-13
Authors:
Shumilina, Elena; Solda, Alice; Gerashchenko, Maxim; Gladyshev, Vadim; Dikiy, Alexander
Citation:

Citation: Shumilina, Elena; Solda, Alice; Gerashchenko, Maxim; Gladyshev, Vadim; Dikiy, Alexander. "(1)H, (13)C, and (15)N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR."  Biomol. NMR Assignments 6, 103-107 (2012).
PubMed: 21901408

Assembly members:

Assembly members:
Grx_domain_of_Mus_musculus_TGR, polymer, 124 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: 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: pET28a

Data sets:
Data typeCount
13C chemical shifts472
15N chemical shifts125
1H chemical shifts803

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Grx domain1

Entities:

Entity 1, Grx domain 124 residues - Formula weight is not available

1   METSERSERPROPROGLYARGARGALAARG
2   LEUALASERPROGLYTHRSERARGPROSER
3   SERGLUALAARGGLUGLULEUARGARGARG
4   LEUARGASPLEUILEGLUGLYASNARGVAL
5   METILEPHESERLYSSERTYRCYSPROHIS
6   SERTHRARGVALLYSGLULEUPHESERSER
7   LEUGLYVALVALTYRASNILELEUGLULEU
8   ASPGLNVALASPASPGLYALASERVALGLN
9   GLUVALLEUTHRGLUILESERASNGLNLYS
10   THRVALPROASNILEPHEVALASNLYSVAL
11   HISVALGLYGLYCYSASPARGTHRPHEGLN
12   ALAHISGLNASNGLYLEULEUGLNLYSLEU
13   LEUGLNASPASP

Samples:

sample_1: Grx domain of Mus musculus TGR, [U-13C; U-15N], 1 mM; sodium phosphate 10 mM; beta-mercaptoethanol 10 mM; sodium chloride 10 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HBHANHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

xwinnmr, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 17637
PDB
DBJ BAB28419 BAC37890 BAE22370
GB AAH76605 AAK31172 EDK99269
REF NP_001171529 NP_001171530 NP_001171531 NP_694802
SP Q99MD6
AlphaFold Q99MD6

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