BMRB Entry 26764

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for hTRF1 in urea
Deposition date:
2016-03-21
Original release date:
2016-05-09
Authors:
Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis
Citation:

Citation: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis. "Hsp70 biases the folding pathways of client proteins"  Proc. Natl. Acad. Sci. U.S.A. 113, E2794-E2801 (2016).
PubMed: 27140645

Assembly members:

Assembly members:
human_telomeric_protein_hTRF1, polymer, 53 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: pET29b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human_telomeric_protein_hTRF1: RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKCL

Data sets:
Data typeCount
13C chemical shifts139
15N chemical shifts50
1H chemical shifts102

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hTRF11

Entities:

Entity 1, hTRF1 53 residues - Formula weight is not available

1   ARGLYSARGGLNALATRPLEUTRPGLUGLU
2   ASPLYSASNLEUARGSERGLYVALARGLYS
3   TYRGLYGLUGLYASNTRPSERLYSILELEU
4   LEUHISTYRLYSPHEASNASNARGTHRSER
5   VALMETLEULYSASPARGTRPARGTHRMET
6   LYSCYSLEU

Samples:

sample_1: human telomeric protein hTRF1, [U-99% 13C; U-99% 15N], 0.6 mM; urea 3500 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

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