BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 26594

Title: Backbone 15N, 1HN, 13CA, 13CB and 13C' Chemical shift Assignments for the DNA-binding domain of Human Telomeric Repeat Binding Factor Protein (hTRF1)   PubMed: 26240333

Deposition date: 2015-06-26 Original release date: 2015-07-29

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

Citation: Sekhar, Ashok; Rosenzweig, Rina; Bouvignies, Guillaume; Kay, Lewis. "Mapping the conformation of a client protein through the Hsp70 functional cycle"  Proc. Natl. Acad. Sci. U.S.A. 112, 10395-10400 (2015).

Assembly members:
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):
hTRF1: RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKKL

Data sets:
Data typeCount
13C chemical shifts141
15N chemical shifts48
1H chemical shifts48

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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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   LYSLYSLEU

Samples:

sample_1: hTRF1, [U-99% 13C; U-99% 15N], 0.8 mM; sodium acetate 50 mM; sodium chloride 50 mM; sodium azide 1 mM; EDTA 1 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 5.7; pressure: 1 atm; temperature: 308 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

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 500 MHz

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