BMRB Entry 52562

Name: NMR resonance assignment for the Rtt103 CID domain from C. thermophilum
Published: 2024-08-27

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52562

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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:

NMR resonance assignment for the Rtt103 CID domain from C. thermophilum

Deposition date:

2024-07-19

Original release date:

2024-08-27

Authors:

Overbeck, Jan; Sprangers, Remco

Citation:

Citation: Dikunova, Alzbeta; Noskova, Nikola; Overbeck, Jan; Polak, Martin; Stelzig, David; Zapletal, David; Kubicek, Karel; Novacek, Jiri; Sprangers, Remco; Stefl, Richard. "Assembly of the Xrn2/Rat1-Rai1-Rtt103 termination complexes in mesophilic and thermophilic organisms" Structure 33, 300-310 (2025).
PubMed: 39657659

Assembly members:

Assembly members:
entity_1, polymer, 141 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Chaetomium thermophilum Taxonomy ID: 209285 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Chaetomium thermophilum

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMAYTDDAVLSKLSALNES HDSIATTAQWIMFHRRHASQ TVHLWLTKLKDLPSHKRLNM IYLANEVTQQSKARHKDDFL NAFSPYIADATALAYKGAPP DIQAKLRRVLDVWKERCIFD RDILQDIEAKFAEIDRSRPQ A

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	440
15N chemical shifts	120
1H chemical shifts	505

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rtt103 CID	1

Entities:

Entity 1, Rtt103 CID 141 residues - Formula weight is not available

1

GLY

ALA

MET

ALA

TYR

THR

ASP

ALA

VAL

2

LEU

SER

LYS

LEU

SER

ALA

LEU

ASN

GLU

SER

3

HIS

ASP

SER

ILE

ALA

THR

ALA

GLN

TRP

4

ILE

MET

PHE

HIS

ARG

HIS

ALA

SER

GLN

5

THR

VAL

HIS

LEU

TRP

LEU

THR

LYS

LEU

LYS

6

ASP

LEU

PRO

SER

HIS

LYS

ARG

LEU

ASN

MET

7

ILE

TYR

LEU

ALA

ASN

GLU

VAL

THR

GLN

8

SER

LYS

ALA

ARG

HIS

LYS

ASP

PHE

LEU

9

ASN

ALA

PHE

SER

PRO

TYR

ILE

ALA

ASP

ALA

10

THR

ALA

LEU

ALA

TYR

LYS

GLY

ALA

PRO

11

ASP

ILE

GLN

ALA

LYS

LEU

ARG

VAL

LEU

12

ASP

VAL

TRP

LYS

GLU

ARG

CYS

ILE

PHE

ASP

13

ARG

ASP

ILE

LEU

GLN

ASP

ILE

GLU

ALA

LYS

14

PHE

ALA

GLU

ILE

ASP

ARG

SER

ARG

PRO

GLN

15

ALA

Samples:

sample_1: Rtt103 CID, [U-100% 13C; U-100% 15N], 800 uM; DTT 1 mM; sodium azide 0.03%; HEPES 25 mM

sample_conditions_1: ionic strength: 0.125 M; pH: 7.3; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N TROSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 13C-separated NOESY	sample_1	isotropic	sample_conditions_1

Software:

CARA - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 600 MHz

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