BMRB Entry 19330

Name: Sequence Specific Backbone 1H, 15N and 13C assignments of the MAPK binding domain of DUSP 16
Published: 2013-08-15

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19330

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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:

Sequence Specific Backbone 1H, 15N and 13C assignments of the MAPK binding domain of DUSP 16

Deposition date:

2013-06-28

Original release date:

2013-08-15

Authors:

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

Citation:

Citation: Kumar, Ganesan Senthil; Zettl, Heiko; Page, Rebecca; Peti, Wolfgang. "Structural Basis for the Regulation of the Mitogen-activated Protein (MAP) Kinase p38 by the Dual Specificity Phosphatase 16 MAP Kinase Binding Domain in Solution." J. Biol. Chem. 288, 28347-28356 (2013).
PubMed: 23926106

Assembly members:

Assembly members:
DUSP16, polymer, 132 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: pet30a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
DUSP16: GTQIVTERLVALLESGTEKV LLIDSRPFVEYNTSHILEAI NINCSKLMKRRLQQDKVLIT ELIQHSAKHKVDIDCSQKVV VYDQSSQDVASLSSDCFLTV LLGKLEKSFNSVHLLAGGFA EFSRCFPGLCEG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	379
15N chemical shifts	123
1H chemical shifts	123

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MAPK	1

Entities:

Entity 1, MAPK 132 residues - Formula weight is not available

GH - N-terminal sequencing artifact; LEHHHHHH - C-terminal cloning artefact and HIS6-tag

1

GLY

THR

GLN

ILE

VAL

THR

GLU

ARG

LEU

VAL

2

ALA

LEU

GLU

SER

GLY

THR

GLU

LYS

VAL

3

LEU

ILE

ASP

SER

ARG

PRO

PHE

VAL

GLU

4

TYR

ASN

THR

SER

HIS

ILE

LEU

GLU

ALA

ILE

5

ASN

ILE

ASN

CYS

SER

LYS

LEU

MET

LYS

ARG

6

ARG

LEU

GLN

ASP

LYS

VAL

LEU

ILE

THR

7

GLU

LEU

ILE

GLN

HIS

SER

ALA

LYS

HIS

LYS

8

VAL

ASP

ILE

ASP

CYS

SER

GLN

LYS

VAL

9

VAL

TYR

ASP

GLN

SER

GLN

ASP

VAL

ALA

10

SER

LEU

SER

ASP

CYS

PHE

LEU

THR

VAL

11

LEU

GLY

LYS

LEU

GLU

LYS

SER

PHE

ASN

12

SER

VAL

HIS

LEU

ALA

GLY

PHE

ALA

13

GLU

PHE

SER

ARG

CYS

PHE

PRO

GLY

LEU

CYS

14

GLU

GLY

Samples:

sample_1: DUSP16, [U-99% 13C; U-99% 15N], 0.5 mM; sodium phosphate 20 mM; sodium chloride 100 mM; TCEP 0.5 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; 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 CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1

Software:

XEASY, Keller and Wuthrich - data analysis

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

Bruker Avance 500 MHz

PDB	2VSW 3TG3
DBJ	BAB21791 BAB40814 BAB47240 BAB71060 BAC29138
GB	AAH31643 AAH42101 AAH57321 AAH59232 AAI09235
REF	NP_001041519 NP_001100094 NP_085143 NP_569714 XP_001084619
SP	Q9BY84
TPG	DAA29345
AlphaFold	Q9BY84