BMRB Entry 51798

Name: Backbone assignment for N-terminal disordered domain of Tetrahymena telomerase protein p65
Published: 2023-06-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51798

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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 assignment for N-terminal disordered domain of Tetrahymena telomerase protein p65

Deposition date:

2023-01-23

Original release date:

2023-06-19

Authors:

Wang, Yanjiao; Singh, Mahavir; Wang, Yaqiang; Feigon, Juli

Citation:

Citation: Wang, Yaqiang; He, Yao; Wang, Yanjiao; Yang, Yuan; Singh, Mahavir; Eichhom, Catherine; Cheng, Xinyi; Jiang, Yi Xiao; Zhou, Z. Hong; Feigon, Juli. "Structure of LARP7 Protein p65-telomerase RNA Complex in Telomerase Revealed by Cryo-EM and NMR" J. Mol. Biol. 435, 168044-168044 (2023).
PubMed: 37330293

Assembly members:

Assembly members:
entity_1, polymer, 123 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: PET-46

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MAHHHHHHVDDDDKMDEYLE NTNLEELEQECFMEDYQHED VVEQENHQVDANDIYENQQM NDESQLNQDVKISQQKEQAV EMIEEQQQNNQDKFKQFQDC MAHITELNFKRNYQNLTEQS SSN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	347
15N chemical shifts	157
1H chemical shifts	157

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain of Tetrahymena telomerase protein p65	1

Entities:

Entity 1, N-terminal domain of Tetrahymena telomerase protein p65 123 residues - Formula weight is not available

The first 14 residues (-14 to -1) are a polyhistidine tag.

1

MET

ALA

HIS

VAL

ASP

2

ASP

LYS

MET

ASP

GLU

TYR

LEU

GLU

3

ASN

THR

ASN

LEU

GLU

LEU

GLU

GLN

GLU

4

CYS

PHE

MET

GLU

ASP

TYR

GLN

HIS

GLU

ASP

5

VAL

GLU

GLN

GLU

ASN

HIS

GLN

VAL

ASP

6

ALA

ASN

ASP

ILE

TYR

GLU

ASN

GLN

MET

7

ASN

ASP

GLU

SER

GLN

LEU

ASN

GLN

ASP

VAL

8

LYS

ILE

SER

GLN

LYS

GLU

GLN

ALA

VAL

9

GLU

MET

ILE

GLU

GLN

ASN

10

GLN

ASP

LYS

PHE

LYS

GLN

PHE

GLN

ASP

CYS

11

MET

ALA

HIS

ILE

THR

GLU

LEU

ASN

PHE

LYS

12

ARG

ASN

TYR

GLN

ASN

LEU

THR

GLU

GLN

SER

13

SER

ASN

Samples:

sample_1: p65 monomer, [U-98% 13C; U-98% 15N], 0.85 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_2: p65 monomer, [U-98% 13C; U-98% 15N], 0.85 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; D2O, [U-100% 2H], 10%; H2O 90%; SDS 25 mM

sample_conditions_1: ionic strength: 0.07 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN - collection

NMRFAM-SPARKY - chemical shift assignment

NMRDraw - processing

NMR spectrometers:

Bruker AVANCE III 800 MHz

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