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 19251

Title: Structure, function, and tethering of DNA-binding domains in 54 transcriptional activators   PubMed: 23818155

Deposition date: 2013-05-19 Original release date: 2013-08-26

Authors: HONG, EUNMI; Wemmer, David E

Citation: Vidangos, Natasha; Maris, Ann; Young, Anisa; Hong, Eunmi; Pelton, Jeffrey; Batchelor, Joseph; Wemmer, David. "Structure, function, and tethering of DNA-binding domains in (54) transcriptional activators."  Biopolymers 99, 1082-1096 (2013).

Assembly members:
entity, polymer, 70 residues, 8334.906 Da.

Natural source:   Common Name: aquificales   Taxonomy ID: 63363   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Aquifex aeolicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Rosetta.pLysS

Entity Sequences (FASTA):
entity: TSSELPELLRKRERKTGDLP KFIEETEKKRIIEALEKTGY VKSRAAKLLGYTLRQLDYRI KKYGIELKKF

Data sets:
Data typeCount
13C chemical shifts187
15N chemical shifts58
1H chemical shifts413

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Nlh21

Entities:

Entity 1, Nlh2 70 residues - 8334.906 Da.

1   THRSERSERGLULEUPROGLULEULEUARG
2   LYSARGGLUARGLYSTHRGLYASPLEUPRO
3   LYSPHEILEGLUGLUTHRGLULYSLYSARG
4   ILEILEGLUALALEUGLULYSTHRGLYTYR
5   VALLYSSERARGALAALALYSLEULEUGLY
6   TYRTHRLEUARGGLNLEUASPTYRARGILE
7   LYSLYSTYRGLYILEGLULEULYSLYSPHE

Samples:

sample_1: Nlh2, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate, [U-100% 15N], 1 mM; H2O 95%; D2O 5%

sample_2: Nlh2, [U-100% 13C; U-100% 15N], 1 mM; D2O 100%

sample_conditions_1: ionic strength: 100 mM; pH: 7; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

Molmol, Koradi, Billeter and Wuthrich - refinement

TALOS, Cornilescu, Delaglio and Bax - chemical shift calculation

NMR spectrometers:

  • Bruker DRX 800 MHz
  • Bruker DRX 900 MHz

Related Database Links:

PDB
GB AAC07620
REF NP_214227 WP_010881164

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