BMRB Entry 26764

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26764

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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
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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   LYSCYSLEU

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