BMRB Entry 25556
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR25556
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Title: Solution structure of the MRG15-MRGBP complex PubMed: 25960410
Deposition date: 2015-03-27 Original release date: 2015-05-26
Authors: Xie, Tao; Zmysloski, Adam; Zhang, Yongbo; Radhakrishnan, Ishwar
Citation: Xie, Tao; Zmysloski, Adam; Zhang, Yongbo; Radhakrishnan, Ishwar. "Structural Basis for Multi-specificity of MRG Domains" Structure 23, 1049-1057 (2015).
Assembly members:
entity_1, polymer, 54 residues, 6284.132 Da.
entity_2, polymer, 172 residues, 19842.887 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_1: SNAGRQVPSKVIWDHLSTMY
DMQALHESEILPFPNPERNF
VLPEEIIQEVREGK
entity_2: SNAEVKVKIPEELKPWLVDD
WDLITRQKQLFYLPAKKNVD
SILEDYANYKKSRGNTDNKE
YAVNEVVAGIKEYFNVMLGT
QLLYKFERPQYAEILADHPD
APMSQVYGAPHLLRLFVRIG
AMLAYTPLDEKSLALLLNYL
HDFLKYLAKNSATLFSASDY
EVAPPEYHRKAV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 925 |
| 15N chemical shifts | 217 |
| 1H chemical shifts | 1476 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | MRGBP | 1 |
| 2 | MRG15 | 2 |
Entities:
Entity 1, MRGBP 54 residues - 6284.132 Da.
| 1 | SER | ASN | ALA | GLY | ARG | GLN | VAL | PRO | SER | LYS | ||||
| 2 | VAL | ILE | TRP | ASP | HIS | LEU | SER | THR | MET | TYR | ||||
| 3 | ASP | MET | GLN | ALA | LEU | HIS | GLU | SER | GLU | ILE | ||||
| 4 | LEU | PRO | PHE | PRO | ASN | PRO | GLU | ARG | ASN | PHE | ||||
| 5 | VAL | LEU | PRO | GLU | GLU | ILE | ILE | GLN | GLU | VAL | ||||
| 6 | ARG | GLU | GLY | LYS |
Entity 2, MRG15 172 residues - 19842.887 Da.
| 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 | LYS | ||||
| 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 |
Samples:
sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 0.8 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%
sample_2: entity_1, [U-100% 13C; U-100% 15N], 0.8 mM; entity_2 0.8 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%
sample_3: entity_1 0.9 mM; entity_2, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%
sample_4: entity_1 0.9 mM; entity_2, [U-100% 13C; U-100% 15N], 0.9 mM; sodium phosphate 50 mM; dithiothreitol-d10 3 mM; NaN3 0.2%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.9; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D double half-filtered 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 15N,13C-filtered, 15N,13C-edited 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_4 | isotropic | sample_conditions_1 |
| 2D double half-filtered 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
| 3D 15N,13C-filtered, 15N,13C-edited 1H-1H NOESY | sample_4 | isotropic | sample_conditions_1 |
Software:
ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
Felix, Accelrys Software Inc. - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Agilent INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts