BMRB Entry 16967

Name: Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN
Published: 2012-09-20

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PDB ID: 2kyl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16967
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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 MAST2-PDZ complexed with the C-terminus of PTEN

Deposition date:

2010-06-01

Original release date:

2012-09-20

Authors:

TERRIEN, Elouan; WOLFF, Nicolas; CORDIER, Florence; SIMENEL, Catherine; LAFON, Monique; DELEPIERRE, Muriel

Citation:

Citation: Terrien, Elouan; Chaffotte, Alain; Lafage, Mireille; Khan, Zakir; Prehaud, Christophe; Cordier, Florence; Simenel, Catherine; Delepierre, Muriel; Buc, Henri; Lafon, Monique; Wolff, Nicolas. "Interference with the PTEN-MAST2 Interaction by a Viral Protein Leads to Cellular Relocalization of PTEN." Sci. Signal. 5, ra58-ra58 (2012).
PubMed: 22894835

Assembly members:

Assembly members:
MAST2-PDZ, polymer, 96 residues, 10452.032 Da.
PTEN-C_Terminus, polymer, 13 residues, 1559.692 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: pDEST15

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MAST2-PDZ: GGSMRPPIIIHRAGKKYGFT LRAIRVYMGDSDVYTVHHMV WHVEDGGPASEAGLRQGDLI THVNGEPVHGLVHTEVVELI LKSGNKVAISTTPLEN
PTEN-C_Terminus: PFDEDQHTQITKV

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	406
15N chemical shifts	96
1H chemical shifts	664

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1
2	entity_2	2

Entities:

Entity 1, entity_1 96 residues - 10452.032 Da.

Residue 1 is a non residue due to TEV cleavage site

1

GLY

SER

MET

ARG

PRO

ILE

2

HIS

ARG

ALA

GLY

LYS

TYR

GLY

PHE

THR

3

LEU

ARG

ALA

ILE

ARG

VAL

TYR

MET

GLY

ASP

4

SER

ASP

VAL

TYR

THR

VAL

HIS

MET

VAL

5

TRP

HIS

VAL

GLU

ASP

GLY

PRO

ALA

SER

6

GLU

ALA

GLY

LEU

ARG

GLN

GLY

ASP

LEU

ILE

7

THR

HIS

VAL

ASN

GLY

GLU

PRO

VAL

HIS

GLY

8

LEU

VAL

HIS

THR

GLU

VAL

GLU

LEU

ILE

9

LEU

LYS

SER

GLY

ASN

LYS

VAL

ALA

ILE

SER

10

THR

PRO

LEU

GLU

ASN

Entity 2, entity_2 13 residues - 1559.692 Da.

1

PRO

PHE

ASP

GLU

ASP

GLN

HIS

THR

GLN

ILE

2

THR

LYS

VAL

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.6 mM; entity_2 1.2 mM; Tris-HCL 50 mM; NaCl 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.2 M; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D_13C-selected/12C,14N-selected NOESY	sample_1	isotropic	sample_conditions_1
3D_15N-selected/12C,14N-selected NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ARIA v2.2, Linge, O'Donoghue and Nilges - structure solution

VNMRJ, Varian - collection

TALOS, Cornilescu, Delaglio and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

Varian INOVA 600 MHz

BMRB	15972
PDB	2KQF 2KYL
DBJ	BAA34527 BAB40778
EMBL	CAD38775
GB	AAH65499 EAX06948 EAX06949 EFB27522 EHB01606
REF	NP_055927 XP_001105315 XP_002810932 XP_004025774 XP_004285802
SP	Q6P0Q8
AlphaFold	Q6P0Q8 Q6ICT7