BMRB Entry 11032
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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/BMR11032
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Title: Solution structure of the knotted tudor domain of the yeast histone acetyltransferase protein, Esa1 PubMed: 18407291
Deposition date: 2008-03-01 Original release date: 2008-04-16
Authors: Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi
Citation: Shimojo, Hideaki; Sano, Norihiko; Moriwaki, Yoshihito; Okuda, Masahiko; Horikoshi, Masami; Nishimura, Yoshifumi. "Novel structural and functional mode of a knot essential for RNA binding activity of the Esa1 presumed chromodomain" J. Mol. Biol. 378, 987-1001 (2008).
Assembly members:
Residues 1-89, polymer, 92 residues, 10791.321 Da.
Natural source: Common Name: baker Taxonomy ID: 4932 Superkingdom: not available Kingdom: not available Genus/species: Eukaryota Fungi
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Residues 1-89: GSHMSHDGKEEPGIAKKINS
VDDIIIKCQCWVQKNDEERL
AEILSINTRKAPPKFYVHYV
NYNKRLDEWITTDRINLDKE
VLYPKLKATDED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 431 |
| 15N chemical shifts | 96 |
| 1H chemical shifts | 676 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Residues 1-89 | 1 |
Entities:
Entity 1, Residues 1-89 92 residues - 10791.321 Da.
| 1 | GLY | SER | HIS | MET | SER | HIS | ASP | GLY | LYS | GLU | ||||
| 2 | GLU | PRO | GLY | ILE | ALA | LYS | LYS | ILE | ASN | SER | ||||
| 3 | VAL | ASP | ASP | ILE | ILE | ILE | LYS | CYS | GLN | CYS | ||||
| 4 | TRP | VAL | GLN | LYS | ASN | ASP | GLU | GLU | ARG | LEU | ||||
| 5 | ALA | GLU | ILE | LEU | SER | ILE | ASN | THR | ARG | LYS | ||||
| 6 | ALA | PRO | PRO | LYS | PHE | TYR | VAL | HIS | TYR | VAL | ||||
| 7 | ASN | TYR | ASN | LYS | ARG | LEU | ASP | GLU | TRP | ILE | ||||
| 8 | THR | THR | ASP | ARG | ILE | ASN | LEU | ASP | LYS | GLU | ||||
| 9 | VAL | LEU | TYR | PRO | LYS | LEU | LYS | ALA | THR | ASP | ||||
| 10 | GLU | ASP |
Samples:
sample_1: Residues 1-89, [U-99% 13C; U-99% 15N], 0.35 mM; potassium phosphate 200 mM; H2O 95%; D2O 5%
sample_2: Residues 1-89 0.35 mM; potassium phosphate 200 mM; D2O 100%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 295 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
CYANA v2.1, P.GUNTERT ET AL. - refinement
Olivia, Yokochi, M., Sekiguchi, S. and Inagaki, F. - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker DRX 800 MHz
- Varian INOVA 900 MHz
Related Database Links:
| BMRB | 11033 |
| PDB | |
| DBJ | GAA26555 |
| EMBL | CAA99465 CAY86525 |
| GB | AHY77525 AJP41755 AJT71177 AJT71665 AJT72155 |
| REF | NP_014887 |
| SP | Q08649 |
| TPG | DAA11012 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts