BMRB Entry 27866

Name: A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation
Published: 2019-08-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27866

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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:

A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation

Deposition date:

2019-04-02

Original release date:

2019-08-14

Authors:

Leonard, Thomas

Citation:

Citation: Elsner, Daniel; Siess, Katharina; Gossenreiter, Thomas; Hartl, Markus; Leonard, Thomas. "A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation" J. Biol. Chem. 294, 14422-14441 (2019).
PubMed: 31406020

Assembly members:

Assembly members:
Dkf1, polymer, 153 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Roundworm Taxonomy ID: 6239 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pGST-parallel

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Dkf1: GAMDGSQGSTDYGDHVVLRY GGTREMVPLIRHEQMLDMLM ERARQIVQGFGNLDTRNMYL FRHEYNSPTLLYPITSASQI TSGSILEIILVDRTEAAVIP HVVEPESYMRPTFCDFCGEM LTGLMRQGVKCKNCNGNFHK RCSNAARNNCGAP

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
- assigned_chem_shift_list_2

Data type	Count
13C chemical shifts	115
15N chemical shifts	106
1H chemical shifts	124

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Dkf1, chain 1	1
2	Dkf1, chain 2	1

Entities:

Entity 1, Dkf1, chain 1 153 residues - Formula weight is not available

1

GLY

ALA

MET

ASP

GLY

SER

GLN

GLY

SER

THR

2

ASP

TYR

GLY

ASP

HIS

VAL

LEU

ARG

TYR

3

GLY

THR

ARG

GLU

MET

VAL

PRO

LEU

ILE

4

ARG

HIS

GLU

GLN

MET

LEU

ASP

MET

LEU

MET

5

GLU

ARG

ALA

ARG

GLN

ILE

VAL

GLN

GLY

PHE

6

GLY

ASN

LEU

ASP

THR

ARG

ASN

MET

TYR

LEU

7

PHE

ARG

HIS

GLU

TYR

ASN

SER

PRO

THR

LEU

8

LEU

TYR

PRO

ILE

THR

SER

ALA

SER

GLN

ILE

9

THR

SER

GLY

SER

ILE

LEU

GLU

ILE

LEU

10

VAL

ASP

ARG

THR

GLU

ALA

VAL

ILE

PRO

11

HIS

VAL

GLU

PRO

GLU

SER

TYR

MET

ARG

12

PRO

THR

PHE

CYS

ASP

PHE

CYS

GLY

GLU

MET

13

LEU

THR

GLY

LEU

MET

ARG

GLN

GLY

VAL

LYS

14

CYS

LYS

ASN

CYS

ASN

GLY

ASN

PHE

HIS

LYS

15

ARG

CYS

SER

ASN

ALA

ARG

ASN

CYS

16

GLY

ALA

PRO

Samples:

Dkf1_ULD-C1a: Dkf1, [U-15N], 0.3 mM; KCl 150 mM

DKf1_ULD: Dkf1, [U-13C; U-15N], 1.2 mM; KCl 150 mM

sample_conditions_1: ionic strength: 0.135 M; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	DKf1_ULD	isotropic	sample_conditions_1
3D HNHA	DKf1_ULD	isotropic	sample_conditions_1
3D HNCACB	DKf1_ULD	isotropic	sample_conditions_1
3D CBCA(CO)NH	DKf1_ULD	isotropic	sample_conditions_1
2D 1H-15N HSQC	Dkf1_ULD-C1a	isotropic	sample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

Sparky, Goddard - data analysis

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

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