BMRB Entry 6092
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                PDB ID: 
                
                
                Entry in NMR Restraints Grid
                Validation report in NRG-CING
            Chem Shift validation:  AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6092
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Title: 1H, 13C, and 15N Chemical Shift Assignments for a complex of PDZ2 from PTP-BL with the C-terminus of RIL (reversion induced LIM) PubMed: 14725761
Deposition date: 2004-02-04 Original release date: 2011-08-11
Authors: Walma, Tine; Vuister, Geerten
Citation: Walma, Tine; Aelen, J.; Nabuurs, S.; Oostendorp, M.; van den Berk, L.; Hendriks, W.; Vuister, Geerten. "A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL" Structure 12, 11-20 (2004).
Assembly members:
Second PDZ domain from PTP-BL, polymer, 102 residues,   9752.07 Da.
C-terminus from RIL, polymer, 12 residues,   1301.55 Da.
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
Entity Sequences (FASTA):
Second PDZ domain from PTP-BL: MHHHHHHMKPGDTFEVELAK
TDGSLGISVTGGVNTSVRHG
GIYVKAIIPKGAAESDGRIH
KGDRVLAVNGVSLEGATHKQ
AVETLRNTGQVVHLLLEKGQ
VP
C-terminus from RIL: VAVYPNAKVELV
- assigned_chemical_shifts
 - heteronucl_T1_relaxation
 - heteronucl_T2_relaxation
 - heteronucl_NOEs
 
| Data type | Count | 
| 13C chemical shifts | 278 | 
| 1H chemical shifts | 622 | 
| 15N chemical shifts | 105 | 
| heteronuclear NOE values | 82 | 
| T1 relaxation values | 82 | 
| T2 relaxation values | 82 | 
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID | 
|---|---|---|
| 1 | PDZ2 from PTP-BL | 1 | 
| 2 | RIL C-terminus | 2 | 
Entities:
Entity 1, PDZ2 from PTP-BL 102 residues - 9752.07 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | MET | LYS | PRO | ||||
| 2 | GLY | ASP | THR | PHE | GLU | VAL | GLU | LEU | ALA | LYS | ||||
| 3 | THR | ASP | GLY | SER | LEU | GLY | ILE | SER | VAL | THR | ||||
| 4 | GLY | GLY | VAL | ASN | THR | SER | VAL | ARG | HIS | GLY | ||||
| 5 | GLY | ILE | TYR | VAL | LYS | ALA | ILE | ILE | PRO | LYS | ||||
| 6 | GLY | ALA | ALA | GLU | SER | ASP | GLY | ARG | ILE | HIS | ||||
| 7 | LYS | GLY | ASP | ARG | VAL | LEU | ALA | VAL | ASN | GLY | ||||
| 8 | VAL | SER | LEU | GLU | GLY | ALA | THR | HIS | LYS | GLN | ||||
| 9 | ALA | VAL | GLU | THR | LEU | ARG | ASN | THR | GLY | GLN | ||||
| 10 | VAL | VAL | HIS | LEU | LEU | LEU | GLU | LYS | GLY | GLN | ||||
| 11 | VAL | PRO | 
Entity 2, RIL C-terminus 12 residues - 1301.55 Da.
| 1 | VAL | ALA | VAL | TYR | PRO | ASN | ALA | LYS | VAL | GLU | ||||
| 2 | LEU | VAL |