BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16967

Title: Solution structure of MAST2-PDZ complexed with the C-terminus of PTEN   PubMed: 22894835

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

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).

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

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

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

Data sets:
Data typeCount
13C chemical shifts406
15N chemical shifts96
1H chemical shifts664

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 96 residues - 10452.032 Da.

Residue 1 is a non residue due to TEV cleavage site

1   GLYGLYSERMETARGPROPROILEILEILE
2   HISARGALAGLYLYSLYSTYRGLYPHETHR
3   LEUARGALAILEARGVALTYRMETGLYASP
4   SERASPVALTYRTHRVALHISHISMETVAL
5   TRPHISVALGLUASPGLYGLYPROALASER
6   GLUALAGLYLEUARGGLNGLYASPLEUILE
7   THRHISVALASNGLYGLUPROVALHISGLY
8   LEUVALHISTHRGLUVALVALGLULEUILE
9   LEULYSSERGLYASNLYSVALALAILESER
10   THRTHRPROLEUGLUASN

Entity 2, entity_2 13 residues - 1559.692 Da.

1   PROPHEASPGLUASPGLNHISTHRGLNILE
2   THRLYSVAL

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D_13C-selected/12C,14N-selected NOESYsample_1isotropicsample_conditions_1
3D_15N-selected/12C,14N-selected NOESYsample_1isotropicsample_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, . - 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

Related Database Links:

BMRB 15972
PDB 2KQF 2KYL
DBJ BAA34527 BAB40778
EMBL CAD38775
GB AAH65499 EAX06948 EAX06949 EFB27522 EHB01606
REF NP_055927 XP_001105315 XP_002810932 XP_002919519 XP_003259187
SP Q6P0Q8