BMRB Entry 16293
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16293
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Murphy, James; Hansen, D. Flemming; Wiesner, Silke; Muhandiram, D. Ranjith; Borg, Mikael; Smith, Matthew; Sicheri, Frank; Kay, Lewis; Forman-Kay, Julie; Pawson, Tony. "Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays." J. Mol. Biol. 393, 409-424 (2009).
PubMed: 19715701
Assembly members:
CA150_FF1+linker, polymer, 71 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: pProEX Htb
Entity Sequences (FASTA):
CA150_FF1+linker: GAMGSLEARMKQFKDMLLER
GVSAFSTWEKELHKIVFDPR
YLLLNPKERKQVFDQYVKTR
AEEERREKKNK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 251 |
| 15N chemical shifts | 78 |
| 1H chemical shifts | 941 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CA150 FF1+linker | 1 |
Entities:
Entity 1, CA150 FF1+linker 71 residues - Formula weight is not available
First 5 residues, GAMGS, arise from a cloning artifact. Remainder corresponds to residues 618-683 of murine CA150
| 1 | GLY | ALA | MET | GLY | SER | LEU | GLU | ALA | ARG | MET | ||||
| 2 | LYS | GLN | PHE | LYS | ASP | MET | LEU | LEU | GLU | ARG | ||||
| 3 | GLY | VAL | SER | ALA | PHE | SER | THR | TRP | GLU | LYS | ||||
| 4 | GLU | LEU | HIS | LYS | ILE | VAL | PHE | ASP | PRO | ARG | ||||
| 5 | TYR | LEU | LEU | LEU | ASN | PRO | LYS | GLU | ARG | LYS | ||||
| 6 | GLN | VAL | PHE | ASP | GLN | TYR | VAL | LYS | THR | ARG | ||||
| 7 | ALA | GLU | GLU | GLU | ARG | ARG | GLU | LYS | LYS | ASN | ||||
| 8 | LYS |
Samples:
sample_1: CA150_FF1+linker, [U-99% 13C; U-99% 15N], 1.0 – 1.7 mM; H20 95%; D20 5%
sample_conditions_1: ionic strength: 0.137 M; pH: 6.5; pressure: 1.0 atm; temperature: 285 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA v1.1, Dr. Michael Nilges, Institut Pasteur - Automated NOE assignment, NMR structure calculation
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 500 MHz