BMRB Entry 27488

Name: ASK1-TBD
Published: 2020-10-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27488

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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:

ASK1-TBD

Deposition date:

2018-05-22

Original release date:

2020-10-06

Authors:

Psenakova, Katarina; Veverka, Vaclav

Citation:

Citation: Psenakova, Katarina; Hexnerova, Rozalie; Srb, Pavel; Obsilova, Veronika; Veverka, Vaclav; Obsil, Tomas. "The redox-active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress" FEBS J. 287, 1626-1644 (2020).
PubMed: 31623019

Assembly members:

Assembly members:
ASK1-TBD, polymer, 185 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ASK1-TBD: GAMGSSRRTTVAYVINEASQ GQLVVAESEALQSLREACET VGATLETLHFGKLDFGETTV LDRFYNADIAVVEMSDAFRQ PSLFYHLGVRESFSMANNII LYCDTNSDSLQSLKEIICQK NTMCTGNYTFVPYMITPHNK VYCCDSSFMKGLTELMQPNF ELLLGPICLPLVDRFIQLLK VAQAS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	374
15N chemical shifts	120
1H chemical shifts	468

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ASK1-TBD	1

Entities:

Entity 1, ASK1-TBD 185 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

SER

ARG

THR

2

VAL

ALA

TYR

VAL

ILE

ASN

GLU

ALA

SER

GLN

3

GLY

GLN

LEU

VAL

ALA

GLU

SER

GLU

ALA

4

LEU

GLN

SER

LEU

ARG

GLU

ALA

CYS

GLU

THR

5

VAL

GLY

ALA

THR

LEU

GLU

THR

LEU

HIS

PHE

6

GLY

LYS

LEU

ASP

PHE

GLY

GLU

THR

VAL

7

LEU

ASP

ARG

PHE

TYR

ASN

ALA

ASP

ILE

ALA

8

VAL

GLU

MET

SER

ASP

ALA

PHE

ARG

GLN

9

PRO

SER

LEU

PHE

TYR

HIS

LEU

GLY

VAL

ARG

10

GLU

SER

PHE

SER

MET

ALA

ASN

ILE

11

LEU

TYR

CYS

ASP

THR

ASN

SER

ASP

SER

LEU

12

GLN

SER

LEU

LYS

GLU

ILE

CYS

GLN

LYS

13

ASN

THR

MET

CYS

THR

GLY

ASN

TYR

THR

PHE

14

VAL

PRO

TYR

MET

ILE

THR

PRO

HIS

ASN

LYS

15

VAL

TYR

CYS

ASP

SER

PHE

MET

LYS

16

GLY

LEU

THR

GLU

LEU

MET

GLN

PRO

ASN

PHE

17

GLU

LEU

GLY

PRO

ILE

CYS

LEU

PRO

18

LEU

VAL

ASP

ARG

PHE

ILE

GLN

LEU

LYS

19

VAL

ALA

GLN

ALA

SER

Samples:

sample_1: ASK1-TBD, [U-100% 13C; U-100% 15N; U-80% 2H], 300 uM

sample_conditions_1: ionic strength: 0.2 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz

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