BMRB Entry 15453
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR15453
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Ramirez-Espain, Ximena; Ruiz, Lidia; Martin-Malpartida, Pau; Oschkinat, Hartmut; Macias, Maria. "Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains" J. Mol. Biol. 373, 1255-1268 (2007).
PubMed: 17915251
Assembly members:
FBP28WW2, polymer, 37 residues, 5237.882 Da.
ligand, polymer, 9 residues, 5237.882 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 Vector: petm30
Entity Sequences (FASTA):
FBP28WW2: GATAVSEWTEYKTADGKTYY
YNNRTLESTWEKPQELK
ligand: GPPLIPPPP
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 281 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | FBP28WW2 | 1 |
| 2 | ligand | 2 |
Entities:
Entity 1, FBP28WW2 37 residues - 5237.882 Da.
| 1 | GLY | ALA | THR | ALA | VAL | SER | GLU | TRP | THR | GLU | ||||
| 2 | TYR | LYS | THR | ALA | ASP | GLY | LYS | THR | TYR | TYR | ||||
| 3 | TYR | ASN | ASN | ARG | THR | LEU | GLU | SER | THR | TRP | ||||
| 4 | GLU | LYS | PRO | GLN | GLU | LEU | LYS |
Entity 2, ligand 9 residues - 5237.882 Da.
| 1 | GLY | PRO | PRO | LEU | ILE | PRO | PRO | PRO | PRO |
Samples:
sample_1: FBP28WW2 1 mM; ligand 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM
sample_2: FBP28WW2 1 mM; ligand 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM
sample_3: FBP28WW2, [U-100% 15N], 1 mM; ligand, [U-100% 15N], 1 mM; sodium phosphate 100 mM; sodium chloride 50 mM
sample_conditions_1: ionic strength: 0.100 M; pH: 5.8; pressure: 1 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_2 | isotropic | sample_conditions_1 |
Software:
UXNMR, Bruker Biospin - collection
ARIA, Linge, O'Donoghue and Nilges - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
ProcheckNMR, Laskowski and MacArthur - data validation
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz