BMRB Entry 52693

Name: NMR signal assignment of the Kinase-Fat linker region (KFL) of the non receptor tyrosine kinase Pyk2
Published: 2025-05-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52693

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR signal assignment of the Kinase-Fat linker region (KFL) of the non receptor tyrosine kinase Pyk2

Deposition date:

2024-11-13

Original release date:

2025-05-20

Authors:

Boll, Emmanuelle; Martin, Lucy; Cantrelle, Francois-Xavier; Landrieu, Isabelle

Citation:

Citation: Martin, Lucy; Freitas, Daniela; Boll, Emmanuelle; Brans, Alain; Mortelecque, Justine; Cantrelle, Francois-Xavier; Dourlen, Pierre; Gomes, Claudio; Danis, Clement; Landrieu, Isabelle. "Conformation-Driven Phase Separation in the Linker Domain of Focal Adhesion Kinases" Biochemistry 64, 1797-1806 (2025).
PubMed: 40136251

Assembly members:

Assembly members:
entity_1, polymer, 197 residues, Formula weight is not available
entity_2, polymer, 43 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MQERNARYRTPKILEPTAFQ EPPPKPSRPKYRPPPQTNLL APKLQFQVPEGLCASSPTLT SPMEYPSPVNSLHTPPLHRH NVFKRHSMREEDFIQPSSRE EAQQLWEAEKVKMRQILDKQ QKQMVEDYQWLRQEEKSLDP MVYMNDKSPLTPEKEVGYLE FTGPPQKPPRLGAQSIQ
entity_2: SSREEAQQLWEAEKVKMRQI LDKQQKQMVEDYQWLRQEEK SLD

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2

Data type	Count
13C chemical shifts	477
15N chemical shifts	158
1H chemical shifts	293

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Pyk2 FL	1
2	Pyk2 Helix	2

Entities:

Entity 1, Pyk2 FL 197 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLN

GLU

ARG

ASN

ALA

ARG

TYR

ARG

THR

4

PRO

LYS

ILE

LEU

GLU

PRO

THR

ALA

PHE

GLN

5

GLU

PRO

LYS

PRO

SER

ARG

PRO

LYS

6

TYR

ARG

PRO

GLN

THR

ASN

LEU

7

ALA

PRO

LYS

LEU

GLN

PHE

GLN

VAL

PRO

GLU

8

GLY

LEU

CYS

ALA

SER

PRO

THR

LEU

THR

9

SER

PRO

MET

GLU

TYR

PRO

SER

PRO

VAL

ASN

10

SER

LEU

HIS

THR

PRO

LEU

HIS

ARG

HIS

11

ASN

VAL

PHE

LYS

ARG

HIS

SER

MET

ARG

GLU

12

GLU

ASP

PHE

ILE

GLN

PRO

SER

ARG

GLU

13

GLU

ALA

GLN

LEU

TRP

GLU

ALA

GLU

LYS

14

VAL

LYS

MET

ARG

GLN

ILE

LEU

ASP

LYS

GLN

15

GLN

LYS

GLN

MET

VAL

GLU

ASP

TYR

GLN

TRP

16

LEU

ARG

GLN

GLU

LYS

SER

LEU

ASP

PRO

17

MET

VAL

TYR

MET

ASN

ASP

LYS

SER

PRO

LEU

18

THR

PRO

GLU

LYS

GLU

VAL

GLY

TYR

LEU

GLU

19

PHE

THR

GLY

PRO

GLN

LYS

PRO

ARG

20

LEU

GLY

ALA

GLN

SER

ILE

GLN

Entity 2, Pyk2 Helix 43 residues - Formula weight is not available

1

SER

ARG

GLU

ALA

GLN

LEU

TRP

2

GLU

ALA

GLU

LYS

VAL

LYS

MET

ARG

GLN

ILE

3

LEU

ASP

LYS

GLN

LYS

GLN

MET

VAL

GLU

4

ASP

TYR

GLN

TRP

LEU

ARG

GLN

GLU

LYS

5

SER

LEU

ASP

Samples:

sample_1: Pyk2_FL, [U-100% 13C; U-100% 15N], 250 uM; sodium chloride 200 mM; HEPES 20 mM; DTT 2 mM

sample_2: Pyk2_FL, [U-100% 13C; U-100% 15N], 250 uM; sodium chloride 200 mM; HEPES 20 mM; DTT 2 mM

sample_conditions_1: ionic strength: 205 mM; pH: 6.25; pressure: 1 atm; temperature: 293 K

sample_conditions_2: ionic strength: 205 mM; pH: 7.4; pressure: 1 atm; temperature: 293 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 HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HN(CA)CO	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
3D HN(CO)CACB	sample_2	isotropic	sample_conditions_2

Software:

TOPSPIN v4.4 - collection, processing

CcpNMR v2.5 - chemical shift assignment, peak picking

qMDD v2.6 - processing

NMR spectrometers:

Bruker AVANCE NEO 900 MHz

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