BMRB Entry 27667

Name: Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime
Published: 2018-11-05

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27667

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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 resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime

Deposition date:

2018-10-30

Original release date:

2018-11-05

Authors:

Zhou, Yuan

Citation:

Citation: Zhou, Yuan. "Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime" Biomol. NMR Assignments ., .-..

Assembly members:

Assembly members:
catalytic_and_ATP-binding_domain_of_HK853, polymer, 171 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet-28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
catalytic_and_ATP-binding_domain_of_HK853: SLQINREKVDLCDLVESAVN AIKEFASSHNVNVLFESNVP CPVEAYIDPTRIRQVLLNLL NNGVKYSKKDAPDKYVKVIL DEKDGGVLIIVEDNGIGIPD HAKDRIFEQFYRVDSSLTYE VPGTGLGLAITKEIVELHGG RIWVESEVGKGSRFFVWIPK DRAGEDNRQDN

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	330
15N chemical shifts	138
1H chemical shifts	490

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	catalytic and ATP-binding domain of HK853	1

Entities:

Entity 1, catalytic and ATP-binding domain of HK853 171 residues - Formula weight is not available

1

SER

LEU

GLN

ILE

ASN

ARG

GLU

LYS

VAL

ASP

2

LEU

CYS

ASP

LEU

VAL

GLU

SER

ALA

VAL

ASN

3

ALA

ILE

LYS

GLU

PHE

ALA

SER

HIS

ASN

4

VAL

ASN

VAL

LEU

PHE

GLU

SER

ASN

VAL

PRO

5

CYS

PRO

VAL

GLU

ALA

TYR

ILE

ASP

PRO

THR

6

ARG

ILE

ARG

GLN

VAL

LEU

ASN

LEU

7

ASN

GLY

VAL

LYS

TYR

SER

LYS

ASP

8

ALA

PRO

ASP

LYS

TYR

VAL

LYS

VAL

ILE

LEU

9

ASP

GLU

LYS

ASP

GLY

VAL

LEU

ILE

10

VAL

GLU

ASP

ASN

GLY

ILE

GLY

ILE

PRO

ASP

11

HIS

ALA

LYS

ASP

ARG

ILE

PHE

GLU

GLN

PHE

12

TYR

ARG

VAL

ASP

SER

LEU

THR

TYR

GLU

13

VAL

PRO

GLY

THR

GLY

LEU

GLY

LEU

ALA

ILE

14

THR

LYS

GLU

ILE

VAL

GLU

LEU

HIS

GLY

15

ARG

ILE

TRP

VAL

GLU

SER

GLU

VAL

GLY

LYS

16

GLY

SER

ARG

PHE

VAL

TRP

ILE

PRO

LYS

17

ASP

ARG

ALA

GLY

GLU

ASP

ASN

ARG

GLN

ASP

18

ASN

Samples:

sample_1: catalytic and ATP-binding domain of HK853, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 20 mM; KCl 50 mM

sample_conditions_1: ionic strength: 0.14 M; pH: 8.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	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 HNCACB	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Keller and Wuthrich - chemical shift assignment, collection

NMR spectrometers:

Bruker Avance 700 MHz

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