BMRB Entry 19330

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

Data sets:
Data typeCount
13C chemical shifts379
15N chemical shifts123
1H chemical shifts123

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1MAPK1

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   GLYTHRGLNILEVALTHRGLUARGLEUVAL
2   ALALEULEUGLUSERGLYTHRGLULYSVAL
3   LEULEUILEASPSERARGPROPHEVALGLU
4   TYRASNTHRSERHISILELEUGLUALAILE
5   ASNILEASNCYSSERLYSLEUMETLYSARG
6   ARGLEUGLNGLNASPLYSVALLEUILETHR
7   GLULEUILEGLNHISSERALALYSHISLYS
8   VALASPILEASPCYSSERGLNLYSVALVAL
9   VALTYRASPGLNSERSERGLNASPVALALA
10   SERLEUSERSERASPCYSPHELEUTHRVAL
11   LEULEUGLYLYSLEUGLULYSSERPHEASN
12   SERVALHISLEULEUALAGLYGLYPHEALA
13   GLUPHESERARGCYSPHEPROGLYLEUCYS
14   GLUGLY

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1

Software:

XEASY, Keller and Wuthrich - data analysis

TOPSPIN v3.1, Bruker Biospin - collection, processing

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
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

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