BMRB Entry 27025

Title:
Ascl1 fragment C
Deposition date:
2017-02-06
Original release date:
2017-04-21
Authors:
Baronti, Lorenzo; Hosek, Tomas; Gil-Caballero, Sergio; Raveh-Amit, Hadas; Calcada, Eduardo; Ayala, Isabel; Dinnyes, Andras; Felli, Isabella; Pierattelli, Roberta; Brutscher, Bernhard
Citation:

Citation: Baronti, Lorenzo; Hosek, Tomas; Gil-Caballero, Sergio; Raveh-Amit, Hadas; Calcada, Eduardo; Ayala, Isabel; Dinnyes, Andras; Felli, Isabella; Pierattelli, Roberta; Brutscher, Bernhard. "Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1'"  Biophys. J. 112, 1366-1373 (2017).
PubMed: 28402879

Assembly members:

Assembly members:
Ascl1_fragment_C, polymer, 79 residues, Formula weight is not available

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: pET21a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts208
15N chemical shifts67
1H chemical shifts67

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ascl1 trascription factor, Fragment C1

Entities:

Entity 1, Ascl1 trascription factor, Fragment C 79 residues - Formula weight is not available

Residues 1-9 represent the artificial affinity tag. Ascl1 fragment C chemical shift assignment start from residue 10 (residue 1 in the assignment file).

1   METALASERHISHISHISHISHISHISGLN
2   GLNGLNPROALAALAVALALAARGARGASN
3   GLUARGGLUARGASNARGVALLYSLEUVAL
4   ASNLEUGLYPHEALATHRLEUARGGLUHIS
5   VALPROASNGLYALAALAASNLYSLYSMET
6   SERLYSVALGLUTHRLEUARGSERALAVAL
7   GLUTYRILEARGALALEUGLNGLNLEULEU
8   ASPGLUHISASPALAVALSERALAALA

Samples:

sample_1: Ascl1 fragment C, [U-100% 13C; U-100% 15N], 250 uM; TRIS 50 mM; DTT 5 mM; SDS 2 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
3D BEST-TROSY HCNssample_1isotropicsample_conditions_1
3D BEST-TROSY HNNssample_1isotropicsample_conditions_1
HADAMACsample_1isotropicsample_conditions_1

Software:

CCPNMR, CCPN - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 950 MHz
  • Bruker Avance 850 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

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