BMRB Entry 17569
Click here to enlarge.
PDB ID: 2lbm
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
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
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).
PubMed: 21666677
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 Vector: pET30a
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 |
Related Database Links:
| BMRB | 15001 |
| PDB | 2JM1 2LBM 2LD1 |
| 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 |
| AlphaFold | P46100 Q61687 Q7YQM3 Q7YQM4 Q93081 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks