BMRB Entry 6128

Title:
Structure of At3g01050.1, a ubiquitin-fold protein from Arabidopsis thaliana
Deposition date:
2004-03-03
Original release date:
2004-05-15
Authors:
Lytle, B.; Peterson, F.; Volkman, B.; Markley, J.
Citation:

Citation: Vinarov, D.; Lytle, B.; Peterson, F.; Tyler, E.; Volkman, B.; Markley, J.. "Cell-free protein production and labeling protocol for NMR-based structural proteomics"  Nat. Methods 1, 149-153 (2004).
PubMed: 15782178

Assembly members:

Assembly members:
At3g01050.1, polymer, 126 residues, 12821 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: cell free synthesis

Data sets:
Data typeCount
15N chemical shifts116
1H chemical shifts669
13C chemical shifts502

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1At3g01050.11

Entities:

Entity 1, At3g01050.1 126 residues - 12821 Da.

1   METGLYHISHISHISHISHISHISLEUGLU
2   ALAGLUVALHISASNGLNLEUGLUILELYS
3   PHEARGLEUTHRASPGLYSERASPILEGLY
4   PROLYSALAPHEPROASPALATHRTHRVAL
5   SERALALEULYSGLUTHRVALILESERGLU
6   TRPPROARGGLULYSGLUASNGLYPROLYS
7   THRVALLYSGLUVALLYSLEUILESERALA
8   GLYLYSVALLEUGLUASNSERLYSTHRVAL
9   LYSASPTYRARGSERPROVALSERASNLEU
10   ALAGLYALAVALTHRTHRMETHISVALILE
11   ILEGLNALAPROVALTHRGLULYSGLULYS
12   LYSPROLYSGLYASPPROLYSMETASNLYS
13   CYSVALCYSSERVALMET

Samples:

sample_1: At3g01050.1, [U-13C; U-15N], 0.5 mM; KCl 50 mM; phosphate buffer 10 mM; DTT 1 mM; H20 90%; D20 10%

sample_cond_1: pH: 6.5; temperature: 298 K; ionic strength: 60 mM; pressure: 1 atm

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-NOESYsample_1not availablesample_cond_1
3D 13C-NOESY-aromaticsample_1not availablesample_cond_1
diffusionsample_1not availablesample_cond_1
N15 hetNOEsample_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
GB AAF26169 AAR20718 AAS92335 AEE73600
REF NP_186754
SP Q9MAB9
AlphaFold Q9MAB9

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