BMRB Entry 50961

Name: 1H, 15N and 13C chemical shift assignments of the PYK2(728-839) polypeptide
Published: 2022-10-12

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50961

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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:

1H, 15N and 13C chemical shift assignments of the PYK2(728-839) polypeptide

Deposition date:

2021-06-05

Original release date:

2022-10-12

Authors:

Momin, Afaque Ahmad; Mendes, Tiago; Barthe, Philippe; Faure, Camille; Hong, SeungBeom; Jaremko, Mariusz; Girault, Jean-Antoine; Jaremko, Lukasz; Arold, Stefan

Citation:

Citation: Momin, Afaque; Mendes, Tiago; Barthe, Philippe; Faure, Camille; Hong, SeungBeom; Yu, Piao; Kadare, Gress; Jaremko, Mariusz; Girault, Jean-Antoine; Jaremko, Lukasz; Arold, Stefan. "PYK2 senses calcium through a disordered dimerization and calmodulin-binding element" Commun. Biol. 5, 800-800 (2022).
PubMed: 35945264

Assembly members:

Assembly members:
entity_1, polymer, 128 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: pET32a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MHHHHHHSSGLVPRGSTNLL APKLQFQVPEGLCASSPTLT SPMEYPSPVNSLHTPPLHRH NVFKRHSMREEDFIQPSSRE EAQQLWEAEKVKMRQILDKQ QKQMVEDYQWLRQEEKSLDP MVYMNDKS

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	331
15N chemical shifts	94
1H chemical shifts	708

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PYK2(728-839) polypeptide	1

Entities:

Entity 1, PYK2(728-839) polypeptide 128 residues - Formula weight is not available

1

MET

HIS

SER

GLY

2

LEU

VAL

PRO

ARG

GLY

SER

THR

ASN

LEU

3

ALA

PRO

LYS

LEU

GLN

PHE

GLN

VAL

PRO

GLU

4

GLY

LEU

CYS

ALA

SER

PRO

THR

LEU

THR

5

SER

PRO

MET

GLU

TYR

PRO

SER

PRO

VAL

ASN

6

SER

LEU

HIS

THR

PRO

LEU

HIS

ARG

HIS

7

ASN

VAL

PHE

LYS

ARG

HIS

SER

MET

ARG

GLU

8

GLU

ASP

PHE

ILE

GLN

PRO

SER

ARG

GLU

9

GLU

ALA

GLN

LEU

TRP

GLU

ALA

GLU

LYS

10

VAL

LYS

MET

ARG

GLN

ILE

LEU

ASP

LYS

GLN

11

GLN

LYS

GLN

MET

VAL

GLU

ASP

TYR

GLN

TRP

12

LEU

ARG

GLN

GLU

LYS

SER

LEU

ASP

PRO

13

MET

VAL

TYR

MET

ASN

ASP

LYS

SER

Samples:

sample_1: PYK2KFL, [U-100% 15N], 0.25 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_2: PYK2KFL, [U-100% 13C; U-100% 15N], 0.25 mM; HEPES 20 mM; sodium chloride 150 mM; TCEP 1 mM

sample_conditions_1: ionic strength: 0.15 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 HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D CBCACONH	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.2 - processing

CINDY v2.1 - data analysis

NMR spectrometers:

Bruker AVANCE III 950 MHz

UniProt	Q14289
AlphaFold	Q6PID4