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 26764

Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for hTRF1 in urea   PubMed: 27140645

Deposition date: 2016-03-21 Original release date: 2016-05-09

Authors: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis

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).

Assembly members:
human_telomeric_protein_hTRF1, polymer, 53 residues, Formula weight is not available

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

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

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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts