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 16876

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16876

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Title: 1HN, 1HA, 13CA, 13CB, 13CO and 15N Chemical Shift Assignments for Intrinsically Disordered Dehydrin ERD14   PubMed: 21336827

Deposition date: 2010-04-16 Original release date: 2011-05-05

Authors: Szalaine Agoston, Bianka; Tompa, Peter; Perczel, Andras

Citation: Szalaine Agoston, Bianka; Kovacs, Denes; Tompa, Peter; Perczel, Andras. "Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14."  Biomol. NMR Assignments 5, 189-193 (2011).

Assembly members:
ERD14, polymer, 185 residues, 20786.3 Da.

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: Escherichia coli

Entity Sequences (FASTA):
ERD14: MAEEIKNVPEQEVPKVATEE SSAEVTDRGLFDFLGKKKDE TKPEETPIASEFEQKVHISE PEPEVKHESLLEKLHRSDSS SSSSSEEEGSDGEKRKKKKE KKKPTTEVEVKEEEKKGFME KLKEKLPGHKKPEDGSAVAA APVVVPPPVEEAHPVEKKGI LEKIKEKLPGYHPKTTVEEE KKDKE

Data sets:
Data typeCount
13C chemical shifts532
15N chemical shifts182
1H chemical shifts328
heteronuclear NOE values167
T1 relaxation values167
T1rho relaxation values167
T2 relaxation values167

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1ERD141

Entities:

Entity 1, ERD14 185 residues - 20786.3 Da.

1   METALAGLUGLUILELYSASNVALPROGLU
2   GLNGLUVALPROLYSVALALATHRGLUGLU
3   SERSERALAGLUVALTHRASPARGGLYLEU
4   PHEASPPHELEUGLYLYSLYSLYSASPGLU
5   THRLYSPROGLUGLUTHRPROILEALASER
6   GLUPHEGLUGLNLYSVALHISILESERGLU
7   PROGLUPROGLUVALLYSHISGLUSERLEU
8   LEUGLULYSLEUHISARGSERASPSERSER
9   SERSERSERSERSERGLUGLUGLUGLYSER
10   ASPGLYGLULYSARGLYSLYSLYSLYSGLU
11   LYSLYSLYSPROTHRTHRGLUVALGLUVAL
12   LYSGLUGLUGLULYSLYSGLYPHEMETGLU
13   LYSLEULYSGLULYSLEUPROGLYHISLYS
14   LYSPROGLUASPGLYSERALAVALALAALA
15   ALAPROVALVALVALPROPROPROVALGLU
16   GLUALAHISPROVALGLULYSLYSGLYILE
17   LEUGLULYSILELYSGLULYSLEUPROGLY
18   TYRHISPROLYSTHRTHRVALGLUGLUGLU
19   LYSLYSASPLYSGLU

Samples:

sample_1: ERD14, [U-99% 13C; U-99% 15N], 1 mM; MES 10 mM; H2O 90%; D2O 10%

sample_2: ERD14, [U-99% 15N], 1 mM; MES 10 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 6.54; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CACBsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1
3D HN(CA)Nsample_1isotropicsample_conditions_1
3D HNN-COSYsample_1isotropicsample_conditions_1
13C-det. H(CA)CONsample_1isotropicsample_conditions_1
R1-measurementsample_2isotropicsample_conditions_1
hetNOE measurementsample_2isotropicsample_conditions_1
R2 measurementsample_2isotropicsample_conditions_1
R1rho measurementsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Swiss NMR - chemical shift assignment

SPARKY, Goddard - data analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz
  • Bruker DRX 600 MHz

Related Database Links:

BMRB 26636
DBJ BAA04569 BAE98985
GB AAF17644 AAG40050 AAG41486 AAK00404 AAK62649
REF NP_001185408 NP_177745
SP P42763

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts