BMRB Entry 26764

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for hTRF1 in urea
Published: 2016-05-09

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

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	139
15N chemical shifts	50
1H chemical shifts	102

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hTRF1	1

Entities:

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

1

ARG

LYS

ARG

GLN

ALA

TRP

LEU

TRP

GLU

2

ASP

LYS

ASN

LEU

ARG

SER

GLY

VAL

ARG

LYS

3

TYR

GLY

GLU

GLY

ASN

TRP

SER

LYS

ILE

LEU

4

LEU

HIS

TYR

LYS

PHE

ASN

ARG

THR

SER

5

VAL

MET

LEU

LYS

ASP

ARG

TRP

ARG

THR

MET

6

LYS

CYS

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_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