BMRB Entry 50901

Name: SH3-PRR2 peptide complex
Published: 2022-07-09

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PDB ID: 7pll
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50901
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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: SH3-PRR2 peptide complex

Deposition date: 2021-04-19 Original release date: 2022-07-09

Authors: Sokolik, Chana; Chill, Jordan

Citation: Twafra, Shams; Sokolik, Chana; Sneh, Tal; Srikanth, Kolluru; Genna, Alessandro; Samson, Avraham; Dessau, Moshe; Chill, Jordan; Gil-Henn, Hava. "Molecular and cellular aspects of cortactin inhibition by a Pyk2-derived peptide" Mol. Cell ., .-..

Assembly members:
entity_1, polymer, 57 residues, Formula weight is not available
entity_2, polymer, 19 residues, Formula weight is not available

Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus

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

Entity Sequences (FASTA):
entity_1: GITAIALYDYQAAGDDEISF DPDDIITNIEMIDDGWWRGV CKGRYGLFPANYVELRQ
entity_2: TAFQEPPPKPSRPKYRPPP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	133
15N chemical shifts	60
1H chemical shifts	467

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SH3	1
2	PRR2	2

Entities:

Entity 1, SH3 57 residues - Formula weight is not available

1

GLY

ILE

THR

ALA

ILE

ALA

LEU

TYR

ASP

TYR

2

GLN

ALA

GLY

ASP

GLU

ILE

SER

PHE

3

ASP

PRO

ASP

ILE

THR

ASN

ILE

GLU

4

MET

ILE

ASP

GLY

TRP

ARG

GLY

VAL

5

CYS

LYS

GLY

ARG

TYR

GLY

LEU

PHE

PRO

ALA

6

ASN

TYR

VAL

GLU

LEU

ARG

GLN

Entity 2, PRR2 19 residues - Formula weight is not available

1

THR

ALA

PHE

GLN

GLU

PRO

LYS

PRO

2

SER

ARG

PRO

LYS

TYR

ARG

PRO

Samples:

sample_1: Cortactin SH3 domain 0.75 ± 0.02 mM; Pyk2 PRR2 peptide 0.75 ± 0.02 mM; D2O 5 ± 0.1 %; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_2: Cortactin SH3 domain 0.75 ± 0.02 mM; Pyk2 PRR2 peptide 0.75 ± 0.02 mM; D2O 100 ± 0.1 %; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_3: Cortactin SH3 domain, [U-98% 13C; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_4: Cortactin SH3 domain, [U-98% 13C; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_5: Cortactin SH3 domain, [U-98% 2H; U-98% 15N], 0.45 ± 0.02 mM; Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_6: Pyk2 PRR2 peptide 0.45 ± 0.02 mM; NaPi pH 6.5 30 ± 0.06 mM; NaN3 0.02 ± 0.002 %

sample_conditions_1: ionic strength: 96 mM; pH: 6.5; pressure: 1 atm; temperature: 296 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_4	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H COSY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_4	isotropic	sample_conditions_1
3D 15N-separated NOESY	sample_6	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_6	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_5	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_5	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_6	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_6	isotropic	sample_conditions_1

Software:

TOPSPIN v3.6.1 - chemical shift assignment, collection, data analysis, peak picking, processing

NMR spectrometers:

Bruker DRX 700 MHz

UniProt	Q8BNA5 Q14289
AlphaFold	Q8BNA5 Q6PID4

Biological Magnetic Resonance Data Bank