BMRB Entry 11595

Name: Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase
Published: 2016-02-01

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PDB ID: 2rvc
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11595
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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:

Solution structure of Zalpha domain of goldfish ZBP-containing protein kinase

Deposition date:

2015-07-07

Original release date:

2016-02-01

Authors:

Lee, Ae-Ree; Park, Chin-Ju; Park, Jin-Wan; Kwon, Mun-Young; Choi, Yong-Geun; Kim, Kyeong Kyu; Choi, Byong-Seok; LEE, Joon-Hwa

Citation:

Citation: Lee, Ae-Ree; Park, Chin-Ju; Park, Jin-Wan; Kwon, Mun-Young; Choi, Yong-Geun; Kim, Kyeong Kyu; Choi, Byong-Seok; Lee, Joon-Hwa. "Solution structure of the Z-DNA binding domain of PKR-like protein kinase from Carassius auratus and quantitative analyses of the intermediate complex during B-Z transition" Nucleic Acids Res. ., .-. (2016).

Assembly members:

Assembly members:
entity, polymer, 64 residues, 7458.576 Da.

Natural source:

Natural source: Common Name: goldfish Taxonomy ID: 7957 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Carassius auratus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MSAETQMERKIIDFLRQNGK SIALTIAKEIGLDKSTVNRH LYNLQRSNQVFNSNEKPPVW DLME

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	169
15N chemical shifts	70
1H chemical shifts	412

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1

Entities:

Entity 1, entity 64 residues - 7458.576 Da.

1

MET

SER

ALA

GLU

THR

GLN

MET

GLU

ARG

LYS

2

ILE

ASP

PHE

LEU

ARG

GLN

ASN

GLY

LYS

3

SER

ILE

ALA

LEU

THR

ILE

ALA

LYS

GLU

ILE

4

GLY

LEU

ASP

LYS

SER

THR

VAL

ASN

ARG

HIS

5

LEU

TYR

ASN

LEU

GLN

ARG

SER

ASN

GLN

VAL

6

PHE

ASN

SER

ASN

GLU

LYS

PRO

VAL

TRP

7

ASP

LEU

MET

GLU

Samples:

sample_1: caZapkz, [U-99% 13C; U-99% 15N], 1.0 mM; sodium chloride 100 mM; sodium phosphate 10 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

Agilent DD2 700 MHz

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