BMRB Entry 27882

Name: Backbone 1H, 13C, 15N chemical shift assignments for the ShkA kinase Rec2 domain from Caulobacter crescentus
Published: 2019-12-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27882

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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:

Backbone 1H, 13C, 15N chemical shift assignments for the ShkA kinase Rec2 domain from Caulobacter crescentus

Deposition date:

2019-04-23

Original release date:

2019-12-12

Authors:

Boehm, Raphael; Hiller, Sebastian

Citation:

Citation: Boehm, Raphael; Hiller, Sebastian; Dubey, Badri; Agustoni, Elia; Mangia, Francesca; Mazur, Adam; Kaczmarczyk, Andreas; Jenal, Urs; Plaza-Menacho, Ivan; Schirmer, Tilman. "Hybrid Histidine kinase activation by cyclic-di-GMP induced domain liberation" .

Assembly members:

Assembly members:
ShkA-Rec2, polymer, 169 residues, 17700 Da.

Natural source:

Natural source: Common Name: Caulobacter crescentus Taxonomy ID: 155892 Superkingdom: Bacteria Kingdom: not available Genus/species: Caulobacter crescentus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ShkA-Rec2: MGSSHHHHHHSSGLVPRGSH PAHDDRIAGAVASGARVLLA EDNPINALLARTLLEREGCI VDRVADGEQAIAAASAGVYD LILMDLRMPGLTGIEAARAL RAKGVATPIAALTADAFDED RRTCLAAGMDDFLVKPLTQE ALRDALKRWTTGGVSGGWTK PATRAKVAG

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	183
15N chemical shifts	99
1H chemical shifts	99

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rec2	1

Entities:

Entity 1, Rec2 169 residues - 17700 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

PRO

ALA

HIS

ASP

ARG

ILE

ALA

GLY

ALA

4

VAL

ALA

SER

GLY

ALA

ARG

VAL

LEU

ALA

5

GLU

ASP

ASN

PRO

ILE

ASN

ALA

LEU

ALA

6

ARG

THR

LEU

GLU

ARG

GLU

GLY

CYS

ILE

7

VAL

ASP

ARG

VAL

ALA

ASP

GLY

GLU

GLN

ALA

8

ILE

ALA

SER

ALA

GLY

VAL

TYR

ASP

9

LEU

ILE

LEU

MET

ASP

LEU

ARG

MET

PRO

GLY

10

LEU

THR

GLY

ILE

GLU

ALA

ARG

ALA

LEU

11

ARG

ALA

LYS

GLY

VAL

ALA

THR

PRO

ILE

ALA

12

ALA

LEU

THR

ALA

ASP

ALA

PHE

ASP

GLU

ASP

13

ARG

THR

CYS

LEU

ALA

GLY

MET

ASP

14

ASP

PHE

LEU

VAL

LYS

PRO

LEU

THR

GLN

GLU

15

ALA

LEU

ARG

ASP

ALA

LEU

LYS

ARG

TRP

THR

16

THR

GLY

VAL

SER

GLY

TRP

THR

LYS

17

PRO

ALA

THR

ARG

ALA

LYS

VAL

ALA

GLY

Samples:

sample_1: ShkA-Rec2, [U-99% 13C; U-99% 15N], 375 uM

sample_conditions_1: ionic strength: 0.195 M; pH: 7.2; pressure: 1 atm; temperature: 298.15 K

Experiments:

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

Software:

TOPSPIN v3.0, Bruker Biospin - collection

CARA, Keller and Wuthrich - chemical shift assignment

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

NMR spectrometers:

Bruker Avance 700 MHz

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