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 PubMed: 19636852
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: 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).
Assembly members:
PDZ2/PDZ3_Tandemdomain, polymer, 252 residues, 26416.7 Da.
Natural source: Common Name: house mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PDZ2/PDZ3_Tandemdomain: GSPGSASPPKPGDTFEVELA
KTDGSLGISVTGGVNTSVRH
GGIYVKAIIPKGAAESDGRI
HKGDRVLAVNGVSLEGATHK
QAVETLRNTGQVVHLLLEKG
QVPTSRERDPAGPQSPPPDQ
DAQRQAPEKVAKQTPHVKDY
SFVTEDNTFEVKLFKNSSGL
GFSFSREDNLIPEQINGSIV
RVKKLFPGQPAAESGKIDVG
DVILKVNGAPLKGLSQQDVI
SALRGTAPEVSLLLCRPAPG
VLPEIDTPGNSS
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 505 |
15N chemical shifts | 181 |
1H chemical shifts | 181 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | tandemdomain | 1 |
Entities:
Entity 1, tandemdomain 252 residues - 26416.7 Da.
1 | GLY | SER | PRO | GLY | SER | ALA | SER | PRO | PRO | LYS | ||||
2 | PRO | GLY | ASP | THR | PHE | GLU | VAL | GLU | LEU | ALA | ||||
3 | LYS | THR | ASP | GLY | SER | LEU | GLY | ILE | SER | VAL | ||||
4 | THR | GLY | GLY | VAL | ASN | THR | SER | VAL | ARG | HIS | ||||
5 | GLY | GLY | ILE | TYR | VAL | LYS | ALA | ILE | ILE | PRO | ||||
6 | LYS | GLY | ALA | ALA | GLU | SER | ASP | GLY | ARG | ILE | ||||
7 | HIS | LYS | GLY | ASP | ARG | VAL | LEU | ALA | VAL | ASN | ||||
8 | GLY | VAL | SER | LEU | GLU | GLY | ALA | THR | HIS | LYS | ||||
9 | GLN | ALA | VAL | GLU | THR | LEU | ARG | ASN | THR | GLY | ||||
10 | GLN | VAL | VAL | HIS | LEU | LEU | LEU | GLU | LYS | GLY | ||||
11 | GLN | VAL | PRO | THR | SER | ARG | GLU | ARG | ASP | PRO | ||||
12 | ALA | GLY | PRO | GLN | SER | PRO | PRO | PRO | ASP | GLN | ||||
13 | ASP | ALA | GLN | ARG | GLN | ALA | PRO | GLU | LYS | VAL | ||||
14 | ALA | LYS | GLN | THR | PRO | HIS | VAL | LYS | ASP | TYR | ||||
15 | SER | PHE | VAL | THR | GLU | ASP | ASN | THR | PHE | GLU | ||||
16 | VAL | LYS | LEU | PHE | LYS | ASN | SER | SER | GLY | LEU | ||||
17 | GLY | PHE | SER | PHE | SER | ARG | GLU | ASP | ASN | LEU | ||||
18 | ILE | PRO | GLU | GLN | ILE | ASN | GLY | SER | ILE | VAL | ||||
19 | ARG | VAL | LYS | LYS | LEU | PHE | PRO | GLY | GLN | PRO | ||||
20 | ALA | ALA | GLU | SER | GLY | LYS | ILE | ASP | VAL | GLY | ||||
21 | ASP | VAL | ILE | LEU | LYS | VAL | ASN | GLY | ALA | PRO | ||||
22 | LEU | LYS | GLY | LEU | SER | GLN | GLN | ASP | VAL | ILE | ||||
23 | SER | ALA | LEU | ARG | GLY | THR | ALA | PRO | GLU | VAL | ||||
24 | SER | LEU | LEU | LEU | CYS | ARG | PRO | ALA | PRO | GLY | ||||
25 | VAL | LEU | PRO | GLU | ILE | ASP | THR | PRO | GLY | ASN | ||||
26 | SER | SER |
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:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment, processing
NMR spectrometers:
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts