BMRB Entry 16989
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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/BMR16989
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Title: Solution structure of the RRM domain of CYP33 PubMed: 20677832
Deposition date: 2010-06-09 Original release date: 2010-08-12
Authors: Park, Sangho; Bushweller, John
Citation: Park, Sangho; Osmers, Ute; Raman, Gayathree; Schwantes, Rebecca; Diaz, Manuel; Bushweller, John. "The PHD3 Domain of MLL Acts as a CYP33-Regulated Switch between MLL-Mediated Activation and Repression ." Biochemistry 49, 6576-6586 (2010).
Assembly members:
CYP33, polymer, 83 residues, 9211.386 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CYP33: GSTTKRVLYVGGLAEEVDDK
VLHAAFIPFGDITDIQIPLD
YETEKHRGFAFVEFELAEDA
AAAIDNMNESELFGRTIRVN
LAK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 330 |
| 15N chemical shifts | 77 |
| 1H chemical shifts | 538 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CYP33 | 1 |
Entities:
Entity 1, CYP33 83 residues - 9211.386 Da.
| 1 | GLY | SER | THR | THR | LYS | ARG | VAL | LEU | TYR | VAL | ||||
| 2 | GLY | GLY | LEU | ALA | GLU | GLU | VAL | ASP | ASP | LYS | ||||
| 3 | VAL | LEU | HIS | ALA | ALA | PHE | ILE | PRO | PHE | GLY | ||||
| 4 | ASP | ILE | THR | ASP | ILE | GLN | ILE | PRO | LEU | ASP | ||||
| 5 | TYR | GLU | THR | GLU | LYS | HIS | ARG | GLY | PHE | ALA | ||||
| 6 | PHE | VAL | GLU | PHE | GLU | LEU | ALA | GLU | ASP | ALA | ||||
| 7 | ALA | ALA | ALA | ILE | ASP | ASN | MET | ASN | GLU | SER | ||||
| 8 | GLU | LEU | PHE | GLY | ARG | THR | ILE | ARG | VAL | ASN | ||||
| 9 | LEU | ALA | LYS |
Samples:
sample_1: potassium phosphate 25 mM; sodium chloride 50 mM; DTT 1 mM; sodium azide 1 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.9; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCAB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY_HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D TROSY_HNCO | sample_1 | anisotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAB25512 BAE01400 BAF85783 BAG36418 BAG73521 |
| EMBL | CAH92437 |
| GB | AAC00006 AAC00007 AAD19906 AAD19907 AAF01030 |
| REF | NP_001041333 NP_001091630 NP_001126436 NP_001156520 NP_001181936 |
| SP | A4FV72 Q5R723 Q9QZH3 Q9UNP9 |
| TPG | DAA31059 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts