BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 25077

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25077

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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for the PDZ domain and the linker of the Protein Tyrosine phosphatase non-receptor type 4   PubMed: 25158884

Deposition date: 2014-07-04 Original release date: 2014-09-19

Authors: Maisonneuve, Pierre; Caillet-Saguy, Celia; Babault, Nicolas; Cordier, Florence; wolff, Nicolas

Citation: Maisonneuve, Pierre; Caillet-Saguy, Celia; Raynal, Bertrand; Gilquin, Bernard; Chaffotte, Alain; Perez, Javier; Zinn-Justin, Sophie; Delepierre, Muriel; Buc, Henri; Cordier, Florence; Wolff, Nicolas. "Regulation of the Catalytic Activity of the Human Phosphatase PTPN4 by Its PDZ Domain."  FEBS J. ., .-. (2014).

Assembly members:
Protein-tyrosine_phosphatase_4, polymer, 140 residues, 15604.6 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):
Protein-tyrosine_phosphatase_4: MSSPEKPTPNGGIPHDNLVL IRMKPDENGRFGFNVKGGYD QKMPVIVSRVAPGTPADLCV PRLNEGDQVVLINGRDIAEH THDQVVLFIKASCERHSGEL MLLVRPNAVYDVVEEKLENE PDFQYIPEKAPLDSVHQDDH

Data sets:
Data typeCount
13C chemical shifts367
1H chemical shifts116
15N chemical shifts116
T1 relaxation values107
T2 relaxation values103

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTPN4 PDZ-linker1

Entities:

Entity 1, PTPN4 PDZ-linker 140 residues - 15604.6 Da.

Residue 1 is a non residue due to TEV cleavage site

1   METSERSERPROGLULYSPROTHRPROASN
2   GLYGLYILEPROHISASPASNLEUVALLEU
3   ILEARGMETLYSPROASPGLUASNGLYARG
4   PHEGLYPHEASNVALLYSGLYGLYTYRASP
5   GLNLYSMETPROVALILEVALSERARGVAL
6   ALAPROGLYTHRPROALAASPLEUCYSVAL
7   PROARGLEUASNGLUGLYASPGLNVALVAL
8   LEUILEASNGLYARGASPILEALAGLUHIS
9   THRHISASPGLNVALVALLEUPHEILELYS
10   ALASERCYSGLUARGHISSERGLYGLULEU
11   METLEULEUVALARGPROASNALAVALTYR
12   ASPVALVALGLUGLULYSLEUGLUASNGLU
13   PROASPPHEGLNTYRILEPROGLULYSALA
14   PROLEUASPSERVALHISGLNASPASPHIS

Samples:

sample_1: Protein-tyrosine phosphatase 4, [U-100% 13C; U-100% 15N], 450 uM; TRIS 50 mM; sodium chloride 150 mM; TCEP 2 mM; H2O 90%; D2O 10%

sample_2: Protein-tyrosine phosphatase 4, [U-99% 15N], 326 uM; TRIS 50 mM; sodium chloride 150 mM; TCEP 2.5 mM; D2O, [U-100% 2H], 10%; H2O 90%

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

sample_conditions_2: temperature: 298 K; pH: 7.5; ionic strength: 0.2 M; pressure: 1 atm

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2

Software:

VNMRJ, Varian - collection

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

Analysis, CCPN - chemical shift assignment, data analysis

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

EMBL P29074
PDB
DBJ BAG37355 BAH13435
GB AAA36530 AAH10674 AAY24016 ADZ15528 AIC49534
REF NP_001093949 NP_001253553 NP_002821 XP_002712421 XP_002749576
SP P29074

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts