BMRB Entry 17569
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17569
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Title: Solution structure of the ADD domain of ATRX complexed with histone tail H3 1-15 K9me3 PubMed: 21666677
Deposition date: 2011-04-08 Original release date: 2011-06-16
Authors: Eustermann, Sebastian; Yang, Ji-Chun; Neuhaus, David
Citation: Eustermann, Sebastian; Yang, Ji-Chun; Law, Martin; Amos, Rachel; Chapman, Lynda; Jelinska, Clare; Garrick, David; Clynes, David; Gibbons, Richard; Rhodes, Daniela; Higgs, Douglas; Neuhaus, David. "Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin." Nat. Struct. Mol. Biol. 18, 777-782 (2011).
Assembly members:
ATRX_ADD_domain, polymer, 142 residues, 16274.673 Da.
H3_tail_1-15_K9me3, polymer, 15 residues, 1607.892 Da.
ZN, non-polymer, 65.409 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):
ATRX_ADD_domain: GAMADKRGDGLHGIVSCTAC
GQQVNHFQKDSIYRHPSLQV
LICKNCFKYYMSDDISRDSD
GMDEQCRWCAEGGNLICCDF
CHNAFCKKCILRNLGRKELS
TIMDENNQWYCYICHPEPLL
DLVTACNSVFENLEQLLQQN
KK
H3_tail_1-15_K9me3: ARTKQTARXSTGGKA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 393 |
| 15N chemical shifts | 148 |
| 1H chemical shifts | 949 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ATRX_ADD_domain | 1 |
| 2 | H3_tail_1-15_K9me3 | 2 |
| 3 | ZN1_1 | 3 |
| 4 | ZN1_2 | 3 |
| 5 | ZN1_3 | 3 |
Entities:
Entity 1, ATRX_ADD_domain 142 residues - 16274.673 Da.
| 1 | GLY | ALA | MET | ALA | ASP | LYS | ARG | GLY | ASP | GLY | ||||
| 2 | LEU | HIS | GLY | ILE | VAL | SER | CYS | THR | ALA | CYS | ||||
| 3 | GLY | GLN | GLN | VAL | ASN | HIS | PHE | GLN | LYS | ASP | ||||
| 4 | SER | ILE | TYR | ARG | HIS | PRO | SER | LEU | GLN | VAL | ||||
| 5 | LEU | ILE | CYS | LYS | ASN | CYS | PHE | LYS | TYR | TYR | ||||
| 6 | MET | SER | ASP | ASP | ILE | SER | ARG | ASP | SER | ASP | ||||
| 7 | GLY | MET | ASP | GLU | GLN | CYS | ARG | TRP | CYS | ALA | ||||
| 8 | GLU | GLY | GLY | ASN | LEU | ILE | CYS | CYS | ASP | PHE | ||||
| 9 | CYS | HIS | ASN | ALA | PHE | CYS | LYS | LYS | CYS | ILE | ||||
| 10 | LEU | ARG | ASN | LEU | GLY | ARG | LYS | GLU | LEU | SER | ||||
| 11 | THR | ILE | MET | ASP | GLU | ASN | ASN | GLN | TRP | TYR | ||||
| 12 | CYS | TYR | ILE | CYS | HIS | PRO | GLU | PRO | LEU | LEU | ||||
| 13 | ASP | LEU | VAL | THR | ALA | CYS | ASN | SER | VAL | PHE | ||||
| 14 | GLU | ASN | LEU | GLU | GLN | LEU | LEU | GLN | GLN | ASN | ||||
| 15 | LYS | LYS |
Entity 2, H3_tail_1-15_K9me3 15 residues - 1607.892 Da.
| 1 | ALA | ARG | THR | LYS | GLN | THR | ALA | ARG | M3L | SER | ||||
| 2 | THR | GLY | GLY | LYS | ALA |
Entity 3, ZN1_1 - Zn - 65.409 Da.
| 1 | ZN |
Samples:
sample_1: ATRX ADD domain, [U-98% 13C; U-98% 15N], 200 uM; H3 tail 1-15 K9me3 200 uM; TRIS, [U-99% 2H], 50 mM; sodium chloride 200 mM; zinc sulfate 150 uM; DTT, [U-99% 2H], 1 mM; H2O 95%; D2O 5%
sample_2: ATRX ADD domain, [U-98% 13C; U-98% 15N], 200 uM; H3 tail 1-15 K9me3 200 uM; TRIS, [U-99% 2H], 50 mM; sodium chloride 200 mM; zinc sulfate 150 uM; DTT, [U-99% 2H], 1 mM; D2O 100%
sample_conditions_1: ionic strength: 250 mM; pH: 7.0; pressure: 1 atm; temperature: 300 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 |
| 2D 1H-13C HSQC aliphatic (constant-time) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic (constant-time) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY (13C-H rejected in F1 and F2) | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H[C]CH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D [H]CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY (13C-H rejected in F1 and F2) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY (15N-H rejected in F2) | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic (rejected 13C-H in F1, 12C-H in F3) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY (13C-H rejected F1, 12C-H rejected F2) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY (13C-H and 15N-H rejected in F1 and F2) | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH v2.19, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY, Goddard - chemical shift assignment
TOPSPIN v2.1, Bruker Biospin - processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker DMX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 15001 |
| PDB | |
| DBJ | BAC28096 BAC40142 BAC81110 BAC81111 BAC81112 |
| EMBL | CAB90351 CAI40710 CAI42674 CAI42675 CAI43115 |
| GB | AAB40698 AAB40699 AAB40700 AAB49969 AAB49970 |
| REF | NP_000480 NP_001009018 NP_033556 NP_612114 XP_001099671 |
| SP | P46100 Q61687 Q7YQM3 Q7YQM4 |
| TPG | DAA12976 DAA12977 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts