BMRB Entry 50574

Name: 1H, 15N and 13C sequence-specific backbone assignment of the MAP Kinase Binding Domain of Dual Specificity Phosphatase 1
Published: 2021-07-16

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50574

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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, 15N and 13C sequence-specific backbone assignment of the MAP Kinase Binding Domain of Dual Specificity Phosphatase 1

Deposition date:

2020-11-16

Original release date:

2021-07-16

Authors:

Senthil Kumar, Ganesan; Page, Rebecca; Peti, Wolfgang

Citation:

Citation: Senthil Kumar, Ganesan; Page, Rebecca; Peti, Wolfgang. "1H, 15N and 13C sequence specific backbone assignment of the MAP kinase binding domain of the dual specificity phosphatase 1 and its interaction with the MAPK p38" Biomol. NMR Assignments 15, 243-248 (2021).
PubMed: 34101142

Assembly members:

Assembly members:
entity_1, polymer, 149 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: RP1B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GHMMEVGTLDAGGLRALLGE RAAQCLLLDCRSFFAFNAGH IAGSVNVRFSTIVRRRAKGA MGLEHIVPNAELRGRLLAGA YHAVVLLDERSAALDGAKRD GTLALAAGALCREARAAQVF FLKGGYEAFSASCPELCSKQ STPMGLSLP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	408
15N chemical shifts	142
1H chemical shifts	566

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	DUSP1	1

Entities:

Entity 1, DUSP1 149 residues - Formula weight is not available

1

GLY

HIS

MET

GLU

VAL

GLY

THR

LEU

ASP

2

ALA

GLY

LEU

ARG

ALA

LEU

GLY

GLU

3

ARG

ALA

GLN

CYS

LEU

ASP

CYS

4

ARG

SER

PHE

ALA

PHE

ASN

ALA

GLY

HIS

5

ILE

ALA

GLY

SER

VAL

ASN

VAL

ARG

PHE

SER

6

THR

ILE

VAL

ARG

ALA

LYS

GLY

ALA

7

MET

GLY

LEU

GLU

HIS

ILE

VAL

PRO

ASN

ALA

8

GLU

LEU

ARG

GLY

ARG

LEU

ALA

GLY

ALA

9

TYR

HIS

ALA

VAL

LEU

ASP

GLU

ARG

10

SER

ALA

LEU

ASP

GLY

ALA

LYS

ARG

ASP

11

GLY

THR

LEU

ALA

LEU

ALA

GLY

ALA

LEU

12

CYS

ARG

GLU

ALA

ARG

ALA

GLN

VAL

PHE

13

PHE

LEU

LYS

GLY

TYR

GLU

ALA

PHE

SER

14

ALA

SER

CYS

PRO

GLU

LEU

CYS

SER

LYS

GLN

15

SER

THR

PRO

MET

GLY

LEU

SER

LEU

PRO

Samples:

sample_1: DUSP1, [U-99% 13C; U-99% 15N], 0.4 mM; sodium phosphate 20 mM; NaCl 100 mM; TCEP 0.5 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

TOPSPIN v3.1 - collection, processing

CARA - data analysis

NMRFAM-SPARKY - data analysis

NMR spectrometers:

Bruker Avance 500 MHz

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