BMRB Entry 17950

Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17950

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Title:
Solution structure of DNA binding domain of AtTRB2
Deposition date:
2011-09-20
Original release date:
2012-09-20
Authors:
Yun, Ji-Hye; Lee, Weontae
Citation:

Citation: Lee, Won Kyung; Yun, Ji-Hye; Lee, Weontae; Cho, Myeon Haeng. "DNA-binding domain of AtTRB2 reveals unique features of a single Myb histone protein family that binds to both Arabidopsis- and human-type telomeric DNA sequences."  Mol. Plant 5, 1406-1408 (2012).
PubMed: 22859734

Assembly members:

Assembly members:
AtTRB2, polymer, 64 residues, 7194.347 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: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
AtTRB2: MGAPKQKWTPEEEAALKAGV LKHGTGKWRTILSDTEFSLI LKSRSNVDLKDKWRNISVTA LWGS

Data sets:
Data typeCount
13C chemical shifts260
15N chemical shifts66
1H chemical shifts420

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AtTRB21

Entities:

Entity 1, AtTRB2 64 residues - 7194.347 Da.

1   METGLYALAPROLYSGLNLYSTRPTHRPRO
2   GLUGLUGLUALAALALEULYSALAGLYVAL
3   LEULYSHISGLYTHRGLYLYSTRPARGTHR
4   ILELEUSERASPTHRGLUPHESERLEUILE
5   LEULYSSERARGSERASNVALASPLEULYS
6   ASPLYSTRPARGASNILESERVALTHRALA
7   LEUTRPGLYSER

Samples:

DNA_binding_domain_of_AtTRB2: AtTRB2, [U-13C; U-15N], 1 mM; HEPES 10 mM; sodium chloride 100 mM; sodium azide 1.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D CBCA(CO)NHDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D HNCACBDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D HNCADNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D HNCODNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D HBHA(CO)NHDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D HCCH-TOCSYDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D 1H-15N NOESYDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1
3D 1H-13C NOESYDNA_binding_domain_of_AtTRB2isotropicsample_conditions_1

Software:

CYANA v2.1, Cornilescu, Delaglio and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard, Guntert, Mumenthaler and Wuthrich, Guntert, Mumenthaler and Wuthrich, Koradi, Billeter and Wuthrich, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis, data analysis, data analysis, peak picking, processing, refinement, structure solution

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

DBJ BAB08466
GB AAK63987 AAL73441 AAL73442 AAL76146 AAS10015
REF NP_201559 NP_851286 XP_002864993
SP Q9FJW5
AlphaFold Q9FJW5

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