BMRB Entry 51443

Name: Solution NMR backbone chemical shift assignment for Tetrahymena p50 peptide
Published: 2022-07-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51443

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution NMR backbone chemical shift assignment for Tetrahymena p50 peptide

Deposition date:

2022-05-14

Original release date:

2022-07-13

Authors:

He, Yao; Song, He; Chan, Henry; Wang, Yaqiang; Liu, Baocheng; Susac, Lukas; Zhou, Hong; Feigon, Juli

Citation:

Citation: He, Yao; Song, He; Chan, Henry; Liu, Baocheng; Wang, Yaqiang; Susac, Lukas; Zhou, Hong; Feigon, Juli. "Structure of Tetrahymena telomerase-bound CST with polymerase a-primase" Nature 608, 813-818 (2022).
PubMed: 35831498

Assembly members:

Assembly members:
entity_1, polymer, 24 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Tetrahymena thermophila Taxonomy ID: 5911 Superkingdom: Eukaryota Kingdom: not available Genus/species: Tetrahymena thermophila

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GCQQDDFGDGCLLQIVNYTH QSLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	39
15N chemical shifts	20
1H chemical shifts	20

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tetrahymena p50	1

Entities:

Entity 1, Tetrahymena p50 24 residues - Formula weight is not available

1

GLY

CYS

GLN

ASP

PHE

GLY

ASP

GLY

2

CYS

LEU

GLN

ILE

VAL

ASN

TYR

THR

HIS

3

GLN

SER

LEU

LYS

Samples:

sample_1: Tetrahymena p50 peptide, [U-13C; U-15N], 0.5 mM; TRIS 20 mM; sodium chloride 50 mM; sodium azide 3 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 7.5; pressure: 1 atm; temperature: 298.15 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY v1.414 - chemical shift assignment

TOPSPIN v4.1 - collection, processing

TOPSPIN v3.5 - collection, processing

CARA - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 800 MHz
Bruker AVANCE III HD 600 MHz

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