BMRB Entry 17637

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:
shortened_Grx_domain_of_Mus_musculus_TGR, polymer, 102 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: pET24a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts312
15N chemical shifts112
1H chemical shifts697

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1short Grx domain1

Entities:

Entity 1, short Grx domain 102 residues - Formula weight is not available

Shortened Grx domain of Mus musculus TGR, lacking first 22 N-terminal amino acids

1   ALAARGGLUGLULEUARGARGARGLEUARG
2   ASPLEUILEGLUGLYASNARGVALMETILE
3   PHESERLYSSERTYRCYSPROHISSERTHR
4   ARGVALLYSGLULEUPHESERSERLEUGLY
5   VALVALTYRASNILELEUGLULEUASPGLN
6   VALASPASPGLYALASERVALGLNGLUVAL
7   LEUTHRGLUILESERASNGLNLYSTHRVAL
8   PROASNILEPHEVALASNLYSVALHISVAL
9   GLYGLYCYSASPARGTHRPHEGLNALAHIS
10   GLNASNGLYLEULEUGLNLYSLEULEUGLN
11   ASPASP

Samples:

sample_1: shortened Grx domain of Mus musculus TGR, [U-13C; U-15N], 1 mM; sodium phosphate 10 mM; sodium chloride 10 mM; beta-mercaptoethanol 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 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 17636
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