BMRB Entry 51442

Name: Solution NMR backbone chemical shift assignment for Tetrahymena Ctc1 OB-A and p50 peptide
Published: 2022-07-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51442

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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:

Solution NMR backbone chemical shift assignment for Tetrahymena Ctc1 OB-A and p50 peptide

Deposition date:

2022-05-13

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, 183 residues, Formula weight is not available
entity_2, 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: MEIEEDLNLKILEDVKKLYL QSFDYIKNGISSSLPSDKKF LADDDIDLSRITFLYKFISV NPTLLLINEKTQAKRRIFQG EYLYGKKKIQFNIIAKNLEI ERELIQFFKKPYQCYIMHNV QVFQMLNKNKNNNVVEFMDS EDLQSSVDCQLYYLIDESSH VLEDDSMDFISTLTRLSDSF NSN
entity_2: GCQQDDFGDGCLLQIVNYTH QSLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	39
15N chemical shifts	195
1H chemical shifts	195

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Tetrahymena Ctc1	1
2	Tetrahymena p50	2

Entities:

Entity 1, Tetrahymena Ctc1 183 residues - Formula weight is not available

1

MET

GLU

ILE

GLU

ASP

LEU

ASN

LEU

LYS

2

ILE

LEU

GLU

ASP

VAL

LYS

LEU

TYR

LEU

3

GLN

SER

PHE

ASP

TYR

ILE

LYS

ASN

GLY

ILE

4

SER

LEU

PRO

SER

ASP

LYS

PHE

5

LEU

ALA

ASP

ILE

ASP

LEU

SER

ARG

6

ILE

THR

PHE

LEU

TYR

LYS

PHE

ILE

SER

VAL

7

ASN

PRO

THR

LEU

ILE

ASN

GLU

LYS

8

THR

GLN

ALA

LYS

ARG

ILE

PHE

GLN

GLY

9

GLU

TYR

LEU

TYR

GLY

LYS

ILE

GLN

10

PHE

ASN

ILE

ALA

LYS

ASN

LEU

GLU

ILE

11

GLU

ARG

GLU

LEU

ILE

GLN

PHE

LYS

12

PRO

TYR

GLN

CYS

TYR

ILE

MET

HIS

ASN

VAL

13

GLN

VAL

PHE

GLN

MET

LEU

ASN

LYS

ASN

LYS

14

ASN

VAL

GLU

PHE

MET

ASP

SER

15

GLU

ASP

LEU

GLN

SER

VAL

ASP

CYS

GLN

16

LEU

TYR

LEU

ILE

ASP

GLU

SER

HIS

17

VAL

LEU

GLU

ASP

SER

MET

ASP

PHE

ILE

18

SER

THR

LEU

THR

ARG

LEU

SER

ASP

SER

PHE

19

ASN

SER

ASN

Entity 2, 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 Ctc1, [U-13C; U-15N; U-2H], 0.8 mM; Tetrahymena p50 peptide 0.8 mM; TRIS 20 mM; sodium chloride 50 mM; TCEP 1 mM; sodium azide 3 mM

sample_2: Tetrahymena p50 peptide, [U-13C; U-15N], 0.5 mM; Tetrahymena Ctc1 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 HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
2D 1H-15N TROSY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	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