BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 6318

Title: Solution structure of thioredoxin h1 from Arabidopsis thaliana   PubMed: 15987893

Authors: Peterson, F.; Lytle, B.; Sampath, S.; Vinarov, D.; Tyler, E.; Shahan, M.; Markley, J.; Volkman, B.

Citation: Peterson, F.; Lytle, B.; Sampath, S.; Vinarov, D.; Tyler, E.; Shahan, M.; Markley, J.; Volkman, B.. "Solution structure of thioredoxin h1 from Arabidopsis thaliana"  Protein Sci. 14, 2195-2200 (2005).

Assembly members:
Thioredoxin h1, polymer, 124 residues, Formula weight is not available

Natural source:   Common Name: Thale cress   Taxonomy ID: 3702   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Arabidopsis thaliana

Experimental source:   Production method: recombinant technology   Host organism: Triticum aestivum

Entity Sequences (FASTA):
Thioredoxin h1: MGHHHHHHLEMASEEGQVIA CHTVETWNEQLQKANESKTL VVVDFTASWCGPCRFIAPFF ADLAKKLPNVLFLKVDTDEL KSVASDWAIQAMPTFMFLKE GKILDKVVGAKKDELQSTIA KHLA

Data sets:
Data typeCount
1H chemical shifts831
13C chemical shifts512
15N chemical shifts121

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AtTRXh11

Entities:

Entity 1, AtTRXh1 124 residues - Formula weight is not available

1   METGLYHISHISHISHISHISHISLEUGLU
2   METALASERGLUGLUGLYGLNVALILEALA
3   CYSHISTHRVALGLUTHRTRPASNGLUGLN
4   LEUGLNLYSALAASNGLUSERLYSTHRLEU
5   VALVALVALASPPHETHRALASERTRPCYS
6   GLYPROCYSARGPHEILEALAPROPHEPHE
7   ALAASPLEUALALYSLYSLEUPROASNVAL
8   LEUPHELEULYSVALASPTHRASPGLULEU
9   LYSSERVALALASERASPTRPALAILEGLN
10   ALAMETPROTHRPHEMETPHELEULYSGLU
11   GLYLYSILELEUASPLYSVALVALGLYALA
12   LYSLYSASPGLULEUGLNSERTHRILEALA
13   LYSHISLEUALA

Samples:

sample_1: Thioredoxin h1, [U-13C; U-15N], 0.5 mM; KCl 50 mM; potassium phosphate buffer 10 mM; H20 90%; D20 10%

sample_cond_1: pH: 5.5; temperature: 298 K; ionic strength: 50 mM

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCsample_1not availablesample_cond_1
HNCAsample_1not availablesample_cond_1
HNCOsample_1not availablesample_cond_1
HN(CO)CAsample_1not availablesample_cond_1
HNCACBsample_1not availablesample_cond_1
HN(CA)COsample_1not availablesample_cond_1
C(CO)NHsample_1not availablesample_cond_1
HCCH-TOCSYsample_1not availablesample_cond_1
3D 15N-NOESYsample_1not availablesample_cond_1
3D 13C-NOESY-aliphaticsample_1not availablesample_cond_1
3D 13C-NOESY-aromaticsample_1not availablesample_cond_1

Software:

XWINNMR v3.1 - collection

NMRPipe v2.1 - processing

XEASY v1.3.1 - analysis

SPSCAN v1.1.0 - peak picking

GARANT v2.1 - automated backbone assignments

TALOS - generation of torsion angle restraints

CYANA v1.0.6 - refinement (torsion angle dynamics)

XPLOR-NIH v2.0.6 - refinement (cartesian MD in explicit solvent)

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

PDB
EMBL CAA78462 CAB62625
GB AAC49354 AAM67008 AEE78739 EFH54044
REF NP_190672 XP_002877785
SP P29448