BMRB Entry 17050
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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/BMR17050
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Title: Tudor domain from Drosophila Polycomblike PubMed: 20669242
Deposition date: 2010-07-08 Original release date: 2010-08-12
Authors: Friberg, A.; Oddone, A.; Klymenko, T.; Mueller, J.; Sattler, M.
Citation: Friberg, Anders; Oddone, Anna; Klymenko, Tetyana; Muller, Jurg; Sattler, Michael. "Structure of an atypical Tudor domain in the Drosophila Polycomblike protein." Protein Sci. 19, 1906-1916 (2010).
Assembly members:
POLYCOMB_PROTEIN_PCL, polymer, 69 residues, 7578.4194 Da.
Natural source: Common Name: FRUIT FLY Taxonomy ID: 7227 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Drosophila melanogaster
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
POLYCOMB_PROTEIN_PCL: GAMAPPVAAPSPAVTYALQE
DVFIKCNDGRFYLGTIIDQT
SDQYLIRFDDQSEQWCEPDK
LRKLGGGSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 220 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 442 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | POLYCOMB PROTEIN PCL | 1 |
Entities:
Entity 1, POLYCOMB PROTEIN PCL 69 residues - 7578.4194 Da.
Three first residues is a cloning artifact.
| 1 | GLY | ALA | MET | ALA | PRO | PRO | VAL | ALA | ALA | PRO | ||||
| 2 | SER | PRO | ALA | VAL | THR | TYR | ALA | LEU | GLN | GLU | ||||
| 3 | ASP | VAL | PHE | ILE | LYS | CYS | ASN | ASP | GLY | ARG | ||||
| 4 | PHE | TYR | LEU | GLY | THR | ILE | ILE | ASP | GLN | THR | ||||
| 5 | SER | ASP | GLN | TYR | LEU | ILE | ARG | PHE | ASP | ASP | ||||
| 6 | GLN | SER | GLU | GLN | TRP | CYS | GLU | PRO | ASP | LYS | ||||
| 7 | LEU | ARG | LYS | LEU | GLY | GLY | GLY | SER | SER |
Samples:
sample_1: POLYCOMB PROTEIN PCL, [U-13C; U-15N], 0.25 – 1.0 mM; salt 25 mM; buffer 20 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 25.000 mM; pH: 6.300; pressure: 1.000 atm; temperature: 298.500 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HNCA | sample_1 | solution | sample_conditions_1 |
| HNCACB | sample_1 | solution | sample_conditions_1 |
| CBCA(CO)NH | sample_1 | solution | sample_conditions_1 |
| (H)CC(CO)NH-TOCSY | sample_1 | solution | sample_conditions_1 |
| H(CC)(CO)NH-TOCSY | sample_1 | solution | sample_conditions_1 |
| H(C)CH-TOCSY | sample_1 | solution | sample_conditions_1 |
| (HB)CB(CGCD)HD | sample_1 | solution | sample_conditions_1 |
| (HB)CB(CGCDCE)HE | sample_1 | solution | sample_conditions_1 |
| 1H-15N HSQC-NOESY | sample_1 | solution | sample_conditions_1 |
| 1H-13C HMQC-NOESY | sample_1 | solution | sample_conditions_1 |
Software:
CNS vany, BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- - refinement
NMRView vany, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker DMX 0 MHz
Related Database Links:
| UNP | PCL_DROME |
| PDB | |
| GB | AAA64457 AAF57748 AAL68389 ACL83738 ACL88860 |
| REF | NP_001261067 NP_476672 XP_001974621 XP_002034393 XP_002082031 |
| SP | Q24459 |
Download simulated HSQC data in one of the following formats:
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