BMRB Entry 15199

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15199

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for the PDZ2 PDZ3 tandemdomain of PTP-BL
Deposition date:
2007-03-30
Original release date:
2007-06-06
Authors:
Fetzer, Christan P.; Sauvageau, Janelle; Kock, Gerd; Berghaus, Carsten; Bangert, Jan-A.; Heumann, Rolf; Erdmann, Kai; Stoll, Raphael
Citation:

Citation: Fetzer, Christian; Sauvageau, Janelle; Kock, Gerd; Berghaus, Carsten; Bangert, Jan-Amade; Dicks, Markus; Heumann, Rolf; Erdmann, Kai; Stoll, Raphael. "Sequence-specific (1)H, (13)C, and (15)N backbone assignment of the 28 kDa PDZ2/PDZ3 tandem domain of the protein tyrosine phosphatase PTP-BL"  Biomol. NMR Assignments 1, 151-153 (2007).
PubMed: 19636852

Assembly members:

Assembly members:
PDZ2/PDZ3_Tandemdomain, polymer, 252 residues, 26416.7 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PDZ2/PDZ3_Tandemdomain: GSPGSASPPKPGDTFEVELA KTDGSLGISVTGGVNTSVRH GGIYVKAIIPKGAAESDGRI HKGDRVLAVNGVSLEGATHK QAVETLRNTGQVVHLLLEKG QVPTSRERDPAGPQSPPPDQ DAQRQAPEKVAKQTPHVKDY SFVTEDNTFEVKLFKNSSGL GFSFSREDNLIPEQINGSIV RVKKLFPGQPAAESGKIDVG DVILKVNGAPLKGLSQQDVI SALRGTAPEVSLLLCRPAPG VLPEIDTPGNSS

Data sets:
Data typeCount
13C chemical shifts505
15N chemical shifts181
1H chemical shifts181

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1tandemdomain1

Entities:

Entity 1, tandemdomain 252 residues - 26416.7 Da.

1   GLYSERPROGLYSERALASERPROPROLYS
2   PROGLYASPTHRPHEGLUVALGLULEUALA
3   LYSTHRASPGLYSERLEUGLYILESERVAL
4   THRGLYGLYVALASNTHRSERVALARGHIS
5   GLYGLYILETYRVALLYSALAILEILEPRO
6   LYSGLYALAALAGLUSERASPGLYARGILE
7   HISLYSGLYASPARGVALLEUALAVALASN
8   GLYVALSERLEUGLUGLYALATHRHISLYS
9   GLNALAVALGLUTHRLEUARGASNTHRGLY
10   GLNVALVALHISLEULEULEUGLULYSGLY
11   GLNVALPROTHRSERARGGLUARGASPPRO
12   ALAGLYPROGLNSERPROPROPROASPGLN
13   ASPALAGLNARGGLNALAPROGLULYSVAL
14   ALALYSGLNTHRPROHISVALLYSASPTYR
15   SERPHEVALTHRGLUASPASNTHRPHEGLU
16   VALLYSLEUPHELYSASNSERSERGLYLEU
17   GLYPHESERPHESERARGGLUASPASNLEU
18   ILEPROGLUGLNILEASNGLYSERILEVAL
19   ARGVALLYSLYSLEUPHEPROGLYGLNPRO
20   ALAALAGLUSERGLYLYSILEASPVALGLY
21   ASPVALILELEULYSVALASNGLYALAPRO
22   LEULYSGLYLEUSERGLNGLNASPVALILE
23   SERALALEUARGGLYTHRALAPROGLUVAL
24   SERLEULEULEUCYSARGPROALAPROGLY
25   VALLEUPROGLUILEASPTHRPROGLYASN
26   SERSER

Samples:

sample_1: PDZ2/PDZ3 Tandemdomain, [U-100% 13C; U-100% 15N], 1 mM; D2O 10%; H2O 90%; DTT 1 mM; TSP 1 mM; potassium phosphate 1.4 mM; sodium chloride 137 mM; potassium chloride 2.7 mM; sodium phosphat 9 mM; sodium azide 0.02%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing

NMR spectrometers:

  • Bruker DRX 600 MHz

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