BMRB Entry 19614

Title:
The basic-helix-loop-helix region of the transcriptional repressor HES-1 is preorganized to bind DNA
Deposition date:
2013-11-15
Original release date:
2014-02-03
Authors:
Wienk, Hans; Popovic, Matija; Coglievina, Maristella; Boelens, Rolf; Pongor, Sandor; Pintar, Alessandro
Citation:

Citation: Popovic, Matija; Wienk, Hans; Coglievina, Maristella; Boelens, Rolf; Pongor, Sandor; Pintar, Alessandro. "The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA."  Proteins 82, 537-545 (2014).
PubMed: 24403087

Assembly members:

Assembly members:
entity, polymer, 70 residues, 8227.798 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: plasmid

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts604
15N chemical shifts142
1H chemical shifts976

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HES-1_11
2HES-1_21

Entities:

Entity 1, HES-1_1 70 residues - 8227.798 Da.

1   METLYSPROLYSTHRALASERGLUHISARG
2   LYSSERSERLYSPROILEMETGLULYSARG
3   ARGARGALAARGILEASNGLUSERLEUSER
4   GLNLEULYSTHRLEUILELEUASPALALEU
5   LYSLYSASPSERSERARGHISSERLYSLEU
6   GLULYSALAASPILELEUGLUMETTHRVAL
7   LYSHISLEUARGASNLEUGLNARGALAGLN

Samples:

sample_1: entity, [U-99% 13C; U-99% 15N], 2 mM; potassium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
triple resonance assignmentsample_1isotropicsample_conditions_1
relaxationsample_1isotropicsample_conditions_1
DNA titrationsample_1isotropicsample_conditions_1
NOESYsample_1isotropicsample_conditions_1

Software:

CCPN_ANALYSIS, CCPN - chemical shift assignment

CS-Rosetta, Shen, Vernon, Baker and Bax - structure model

TALOS+, Cornilescu, Delaglio and Bax - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CING, Vuister et al - structure validation

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

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

PDB
DBJ BAA02682 BAA03931 BAA91149 BAE21226 BAE21713
EMBL CAA65998 CAG08099 CAG46641 CAJ82991 CDQ79517
GB AAA41307 AAA65220 AAA79185 AAF73060 AAH18375
PRF 1905315A
REF NP_001011194 NP_001029850 NP_001079386 NP_001081396 NP_001098313
SP P35428 Q04666 Q14469 Q3ZBG4 Q5PPM5
TPG DAA33369
AlphaFold Q14469 Q3ZBG4 Q5PPM5 P35428 Q04666

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