BMRB Entry 27354

Name: 1H, 13C, and 15N Chemical Shift Assignments for the Thermus thermophilus HB8 TTHA1718 protein in sf9 cells by in-cell NMR spectroscopy
Published: 2020-05-29

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PDB ID: 5zcz
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27354
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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:

1H, 13C, and 15N Chemical Shift Assignments for the Thermus thermophilus HB8 TTHA1718 protein in sf9 cells by in-cell NMR spectroscopy

Deposition date:

2018-01-10

Original release date:

2020-05-29

Authors:

Ito, Yutaka; Ikeya, Teppei; Tanaka, Takashi; Kamoshida, Hajime; Mishima, Masaki; Shirakawa, Masahiro; Guentert, Peter

Citation:

Citation: Tanaka, Takashi; Ikeya, Teppei; Kamoshida, Hajime; Suemoto, Yusuke; Mishima, Masaki; Shirakawa, Masahiro; Guntert, Peter; Ito, Yutaka. "High-Resolution Protein 3D Structure Determination in Living Eukaryotic Cells" Angew. Chem. Int. Ed. Engl. 58, 7284-7288 (2019).
PubMed: 30938016

Assembly members:

Assembly members:
TTHA1718, polymer, 66 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermus thermophilus Taxonomy ID: 274 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermus thermophilus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Spodoptera frugiperda Vector: pFastBac

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TTHA1718: MLKLKVEGMTCNHCVMAVTK ALKKVPGVEKVEVSLEKGEA LVEGTADPKALVQAVEEEGY KAEVLA

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	89
15N chemical shifts	56
1H chemical shifts	287

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	the Thermus thermophilus HB8 TTHA1718 protein	1

Entities:

Entity 1, the Thermus thermophilus HB8 TTHA1718 protein 66 residues - Formula weight is not available

1

MET

LEU

LYS

LEU

LYS

VAL

GLU

GLY

MET

THR

2

CYS

ASN

HIS

CYS

VAL

MET

ALA

VAL

THR

LYS

3

ALA

LEU

LYS

VAL

PRO

GLY

VAL

GLU

LYS

4

VAL

GLU

VAL

SER

LEU

GLU

LYS

GLY

GLU

ALA

5

LEU

VAL

GLU

GLY

THR

ALA

ASP

PRO

LYS

ALA

6

LEU

VAL

GLN

ALA

VAL

GLU

GLY

TYR

7

LYS

ALA

GLU

VAL

LEU

ALA

Samples:

sample_1: TTHA1718, [U-100% 15N], 50 ± 12 uM; TTHA1718, [U-100% 13C; U-100% 15N], 50 ± 12 uM

sample_conditions_1: pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	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 HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - data analysis

AZARA v2.8.1, Boucher - processing

TOPSPIN v3.0, Bruker Biospin - collection

Analysis v2.4.2, CCPN - chemical shift assignment

TALOS-N v4.12, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Bruker AvanceIII 600 MHz