BMRB Entry 25326
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25326
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: The structure of the carboxy-terminal domain of DNTTIP1 PubMed: 25653165
Deposition date: 2014-11-11 Original release date: 2015-02-16
Authors: Schwabe, John; Muskett, Frederick; Itoh, Toshimasa
Citation: Itoh, Toshimasa; Fairall, Louise; Muskett, Frederick; Milano, Charles; Watson, Peter; Arnaudo, Nadia; Martino, Fabrizio; Schwabe, John. "Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting" Nucleic Acids Res. 43, 2033-2044 (2015).
Assembly members:
entity, polymer, 122 residues, 14060.309 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):
entity: GAREGPKWDPARLNESTTFV
LGSRANKALGMGGTRGRIYI
KHPHLFKYAADPQDKHWLAE
QHHMRATGGKMAYLLIEEDI
RDLAASDDYRGCLDLKLEEL
KSFVLPSWMVEKMRKYMETL
RT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 382 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 734 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 122 residues - 14060.309 Da.
| 1 | GLY | ALA | ARG | GLU | GLY | PRO | LYS | TRP | ASP | PRO | ||||
| 2 | ALA | ARG | LEU | ASN | GLU | SER | THR | THR | PHE | VAL | ||||
| 3 | LEU | GLY | SER | ARG | ALA | ASN | LYS | ALA | LEU | GLY | ||||
| 4 | MET | GLY | GLY | THR | ARG | GLY | ARG | ILE | TYR | ILE | ||||
| 5 | LYS | HIS | PRO | HIS | LEU | PHE | LYS | TYR | ALA | ALA | ||||
| 6 | ASP | PRO | GLN | ASP | LYS | HIS | TRP | LEU | ALA | GLU | ||||
| 7 | GLN | HIS | HIS | MET | ARG | ALA | THR | GLY | GLY | LYS | ||||
| 8 | MET | ALA | TYR | LEU | LEU | ILE | GLU | GLU | ASP | ILE | ||||
| 9 | ARG | ASP | LEU | ALA | ALA | SER | ASP | ASP | TYR | ARG | ||||
| 10 | GLY | CYS | LEU | ASP | LEU | LYS | LEU | GLU | GLU | LEU | ||||
| 11 | LYS | SER | PHE | VAL | LEU | PRO | SER | TRP | MET | VAL | ||||
| 12 | GLU | LYS | MET | ARG | LYS | TYR | MET | GLU | THR | LEU | ||||
| 13 | ARG | THR |
Samples:
sample_1: potassium phosphate 40 mM; DTT 1 mM; sodium azide 1 mM; DNTTIP1(197-316), [U-100% 13C; U-100% 15N], 0.3 mM; H2O 90%; D2O 10%
sample_2: potassium phosphate 40 mM; DTT 1 mM; sodium azide 1 mM; DNTTIP1(197-316), [U-100% 13C; U-100% 15N], 0.3 mM; D2O 100%
sample_conditions_1: ionic strength: 80 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 80 mM; pH: 6.0; pressure: 1 atm; temperature: 298 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 HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 3D CCH-TOCSY | sample_2 | isotropic | sample_conditions_2 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_2 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement
SPARKY v3.1, Goddard - chemical shift assignment
TOPSPIN v2.1, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| UNP | Q9H147 |
| PDB | |
| DBJ | BAB62888 BAB82521 BAE26320 BAE40293 BAG36715 |
| EMBL | CAH93071 |
| GB | AAH03486 AAH09535 AAH24290 AAI00641 AAI46176 |
| REF | NP_001092346 NP_001126819 NP_001181292 NP_443183 NP_598524 |
| SP | A6H7A8 Q5R595 Q91Y53 Q99LB0 Q9H147 |
| TPG | DAA23166 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts