BMRB Entry 52627

Name: NMR signal assignment of the Kinase-Fat linker region (KFL) of the non receptor tyrosine kinase FAK1
Published: 2025-05-20

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52627

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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 FAK1

Deposition date:

2024-10-04

Original release date:

2025-05-20

Authors:

Martin, Lucy; Boll, Emmanuelle; 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, 241 residues, 26569.353 Da.
entity_2, polymer, 47 residues, 5580.34 Da.

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 MESRRQATVSWDSGGSDEAP PKPSRPGYPSPRSSEGFYPS PQHMVQTNHYQVSGYPGSHG ITAMAGSIYPGQASLLDQTD SWNHRPQEIAMWQPNVEDST VLDLRGIGQVLPTHLMEERL IRQQQEMEEDQRWLEKEERF LKPDVRLSRGSIDREDGSLQ GPIGNQHIYQPVGKPDPAAP PKKPPRPGAPGHLGSLASLS SPADSYNEGVKLQPQEISPP P
entity_2: GGGSTVLDLRGIGQVLPTHL MEERLIRQQQEMEEDQRWLE KEERFLK

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
- assigned_chemical_shifts_2
spectral_peak_list

Data type	Count
13C chemical shifts	500
15N chemical shifts	171
1H chemical shifts	206

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	LK2 FAK1	1
2	Helix LK2 FAK1	2

Entities:

Entity 1, LK2 FAK1 241 residues - 26569.353 Da.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

GLU

SER

ARG

GLN

ALA

THR

VAL

SER

4

TRP

ASP

SER

GLY

SER

ASP

GLU

ALA

PRO

5

PRO

LYS

PRO

SER

ARG

PRO

GLY

TYR

PRO

SER

6

PRO

ARG

SER

GLU

GLY

PHE

TYR

PRO

SER

7

PRO

GLN

HIS

MET

VAL

GLN

THR

ASN

HIS

TYR

8

GLN

VAL

SER

GLY

TYR

PRO

GLY

SER

HIS

GLY

9

ILE

THR

ALA

MET

ALA

GLY

SER

ILE

TYR

PRO

10

GLY

GLN

ALA

SER

LEU

ASP

GLN

THR

ASP

11

SER

TRP

ASN

HIS

ARG

PRO

GLN

GLU

ILE

ALA

12

MET

TRP

GLN

PRO

ASN

VAL

GLU

ASP

SER

THR

13

VAL

LEU

ASP

LEU

ARG

GLY

ILE

GLY

GLN

VAL

14

LEU

PRO

THR

HIS

LEU

MET

GLU

ARG

LEU

15

ILE

ARG

GLN

GLU

MET

GLU

ASP

16

GLN

ARG

TRP

LEU

GLU

LYS

GLU

ARG

PHE

17

LEU

LYS

PRO

ASP

VAL

ARG

LEU

SER

ARG

GLY

18

SER

ILE

ASP

ARG

GLU

ASP

GLY

SER

LEU

GLN

19

GLY

PRO

ILE

GLY

ASN

GLN

HIS

ILE

TYR

GLN

20

PRO

VAL

GLY

LYS

PRO

ASP

PRO

ALA

PRO

21

PRO

LYS

PRO

ARG

PRO

GLY

ALA

PRO

22

GLY

HIS

LEU

GLY

SER

LEU

ALA

SER

LEU

SER

23

SER

PRO

ALA

ASP

SER

TYR

ASN

GLU

GLY

VAL

24

LYS

LEU

GLN

PRO

GLN

GLU

ILE

SER

PRO

25

PRO

Entity 2, Helix LK2 FAK1 47 residues - 5580.34 Da.

1

GLY

SER

THR

VAL

LEU

ASP

LEU

ARG

2

GLY

ILE

GLY

GLN

VAL

LEU

PRO

THR

HIS

LEU

3

MET

GLU

ARG

LEU

ILE

ARG

GLN

4

GLU

MET

GLU

ASP

GLN

ARG

TRP

LEU

GLU

5

LYS

GLU

ARG

PHE

LEU

LYS

Samples:

sample_1: KFL_FAK1, [U-100% 13C; U-100% 15N], 250 uM; sodium chloride 50 mM; imidazole 170 mM; potassium chloride 17 mM

sample_2: Helix_KFL_Fak1, [U-100% 13C; U-100% 15N], 256 uM; HEPES 20 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 178 mM; pH: 7.4; 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/HMQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC/HMQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
104 (H[N[co[{CA\|ca[C]}]]])	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
116 (H[N[ca[CO]]])	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC/HMQC	sample_2	isotropic	sample_conditions_2
108 (H[N[ca[CO]]])	sample_2	isotropic	sample_conditions_2
3D HNCO	sample_2	isotropic	sample_conditions_2
3D HNCACB	sample_2	isotropic	sample_conditions_2
106 (H[N[co[{CA\|ca[C]}]]])	sample_2	isotropic	sample_conditions_2

Software:

CcpNmr Analysis v2.5 - chemical shift assignment

TOPSPIN v4.4 - collection, processing

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