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BMRB Entry 16879

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16879
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Title: Chemical shift assignments of the 3rd PDZ domain of protein tyrosine phosphatase basophil like (PTP-BL)   PubMed: 20563762

Deposition date: 2010-04-19 Original release date: 2010-07-27

Authors: Kock, Gerd; Dicks, Markus; Stoll, Raphael

Citation: Kock, Gerd; Dicks, Markus; Heumann, Rolf; Erdmann, Kai; Stoll, Raphael. "Sequence-specific 1H, 13C, and 15N assignment of the extended PDZ3 domain of the protein tyrosine phosphatase basophil-like PTP-BL."  Biomol. NMR Assignments 4, 199-202 (2010).

Assembly members:
PDZ3_PTP-BL, polymer, 119 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: pGex-2T

Entity Sequences (FASTA):
PDZ3_PTP-BL: TPHVKDYSFVTEDNTFEVKL FKNSSGLGFSFSREDNLIPE QINGSIVRVKKLFPGQPAAE SGKIDVGDVILKVNGAPLKG LSQQDVISALRGTAPEVSLL LCRPAPGVLPEIDTPGNSS

Data sets:
Data typeCount
13C chemical shifts384
15N chemical shifts100
1H chemical shifts617

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1PDZ3 domain1

Entities:

Entity 1, PDZ3 domain 119 residues - Formula weight is not available

According to the UniProt Database, the coding sequence of PDZ3 of PTP-BL comprises residues Glu17 to Ala105

1   THRPROHISVALLYSASPTYRSERPHEVAL
2   THRGLUASPASNTHRPHEGLUVALLYSLEU
3   PHELYSASNSERSERGLYLEUGLYPHESER
4   PHESERARGGLUASPASNLEUILEPROGLU
5   GLNILEASNGLYSERILEVALARGVALLYS
6   LYSLEUPHEPROGLYGLNPROALAALAGLU
7   SERGLYLYSILEASPVALGLYASPVALILE
8   LEULYSVALASNGLYALAPROLEULYSGLY
9   LEUSERGLNGLNASPVALILESERALALEU
10   ARGGLYTHRALAPROGLUVALSERLEULEU
11   LEUCYSARGPROALAPROGLYVALLEUPRO
12   GLUILEASPTHRPROGLYASNSERSER

Samples:

sample_1: PDZ3, [U-15N], 0.5 – 1.0 mM; TSP 1.0 mM; H2O 90%; D2O 10%; potassium phosphate 1.4 mM; potassium chloride 2.7 mM; sodium chloride 137 mM; sodium phosphate 9 mM

sample_2: PDZ3, [U-100% 13C; U-100% 15N], 0.5 – 1.0 mM; TSP 1.0 mM; H2O 90%; D2O 10%; potassium phosphate 1.4 mM; potassium chloride 2.7 mM; sodium chloride 137 mM; sodium phosphate 9 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRView v5.2.2, Johnson, One Moon Scientific - data analysis, peak picking

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

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

UNP Q64512|1491-1579

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