BMRB Entry 18000
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PDB ID: 2lkm
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18000
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: Xie, Tao; Graveline, Richard; Kumar, Ganesan Senthil; Zhang, Yongbo; Krishnan, Arvind; David, Gregory; Radhakrishnan, Ishwar. "Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology." Structure 20, 151-160 (2012).
PubMed: 22244764
Assembly members:
Pf1, polymer, 42 residues, 4721.391 Da.
MRG15, polymer, 172 residues, 19870.898 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: pMCSG7
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 870 |
| 15N chemical shifts | 204 |
| 1H chemical shifts | 1387 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Pf1 | 1 |
| 2 | MRG15 | 2 |
Entities:
Entity 1, Pf1 42 residues - 4721.391 Da.
This is the MRG binding domain of PHD factor 1 (Pf1) protein
| 1 | ASP | TYR | VAL | GLN | PRO | GLN | LEU | ARG | ARG | PRO | ||||
| 2 | PHE | GLU | LEU | LEU | ILE | ALA | ALA | ALA | MET | GLU | ||||
| 3 | ARG | ASN | PRO | THR | GLN | PHE | GLN | LEU | PRO | ASN | ||||
| 4 | GLU | LEU | THR | CYS | THR | THR | ALA | LEU | PRO | GLY | ||||
| 5 | SER | SER |
Entity 2, MRG15 172 residues - 19870.898 Da.
Residues 1-3 is from a non-native affinity tag. This is the MRG domain of MRG15
| 1 | SER | ASN | ALA | GLU | VAL | LYS | VAL | LYS | ILE | PRO | ||||
| 2 | GLU | GLU | LEU | LYS | PRO | TRP | LEU | VAL | ASP | ASP | ||||
| 3 | TRP | ASP | LEU | ILE | THR | ARG | GLN | LYS | GLN | LEU | ||||
| 4 | PHE | TYR | LEU | PRO | ALA | LYS | LYS | ASN | VAL | ASP | ||||
| 5 | SER | ILE | LEU | GLU | ASP | TYR | ALA | ASN | TYR | ARG | ||||
| 6 | LYS | SER | ARG | GLY | ASN | THR | ASP | ASN | LYS | GLU | ||||
| 7 | TYR | ALA | VAL | ASN | GLU | VAL | VAL | ALA | GLY | ILE | ||||
| 8 | LYS | GLU | TYR | PHE | ASN | VAL | MET | LEU | GLY | THR | ||||
| 9 | GLN | LEU | LEU | TYR | LYS | PHE | GLU | ARG | PRO | GLN | ||||
| 10 | TYR | ALA | GLU | ILE | LEU | ALA | ASP | HIS | PRO | ASP | ||||
| 11 | ALA | PRO | MET | SER | GLN | VAL | TYR | GLY | ALA | PRO | ||||
| 12 | HIS | LEU | LEU | ARG | LEU | PHE | VAL | ARG | ILE | GLY | ||||
| 13 | ALA | MET | LEU | ALA | TYR | THR | PRO | LEU | ASP | GLU | ||||
| 14 | LYS | SER | LEU | ALA | LEU | LEU | LEU | ASN | TYR | LEU | ||||
| 15 | HIS | ASP | PHE | LEU | LYS | TYR | LEU | ALA | LYS | ASN | ||||
| 16 | SER | ALA | THR | LEU | PHE | SER | ALA | SER | ASP | TYR | ||||
| 17 | GLU | VAL | ALA | PRO | PRO | GLU | TYR | HIS | ARG | LYS | ||||
| 18 | ALA | VAL |
Related Database Links:
| BMRB | 17485 |
| PDB | 2L9S 2LKM 2AQL 2F5J |
| DBJ | BAD18713 BAE00370 BAE24837 BAE33212 BAE41602 BAB30219 BAB58904 BAC37546 BAD90270 BAE00783 |
| GB | AAH01657 AAH43080 AAI10883 AAI21044 AAI21045 AAD20058 AAD20970 AAD29872 AAF29033 AAF80854 |
| REF | NP_001013135 NP_001028733 NP_001179060 NP_001253214 NP_001277060 NP_001011999 NP_001030525 NP_001034236 NP_001127679 NP_001240678 |
| SP | Q5SPL2 Q96QT6 P60762 Q5NVP9 Q6AYU1 Q9UBU8 |
| TPG | DAA18992 DAA17605 |
| EMBL | CAB70879 CAI29614 |
| AlphaFold | Q5SPL2 Q96QT6 P60762 Q5NVP9 Q6AYU1 Q9UBU8 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks