BMRB Entry 25677
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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/BMR25677
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Title: Solution NMR structure of CBX8 in complex with AF9 (CBX8-AF9)
Deposition date: 2015-06-30 Original release date: 2016-07-18
Authors: Kuntimaddi, Aravinda; Leach, Benjamin; Bushweller, John
Citation: Kuntimaddi, Aravinda; Leach, Benjamin; Bushweller, John. "Solution NMR Structure of CBX8 in complex with AF9 (CBX8-AF9)" Not known ., .-..
Assembly members:
Chromobox_protein_homolog_8, polymer, 24 residues, 2577.936 Da.
Protein_AF-9, polymer, 70 residues, 8278.482 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):
Chromobox_protein_homolog_8: TQGGRPSLIARIPVARILGD
PEEE
Protein_AF-9: MDKAYLDELVELHRRLMTLR
ERHILQQIVNLIEETGHFHI
TNTTFDFDLCSLDKTTVRKL
QSYLETSGTS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 406 |
| 15N chemical shifts | 88 |
| 1H chemical shifts | 542 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 24 residues - 2577.936 Da.
RESIDUES 327-349
| 1 | THR | GLN | GLY | GLY | ARG | PRO | SER | LEU | ILE | ALA | ||||
| 2 | ARG | ILE | PRO | VAL | ALA | ARG | ILE | LEU | GLY | ASP | ||||
| 3 | PRO | GLU | GLU | GLU |
Entity 2, entity_2 70 residues - 8278.482 Da.
RESIDUES 500-568
| 1 | MET | ASP | LYS | ALA | TYR | LEU | ASP | GLU | LEU | VAL | |
| 2 | GLU | LEU | HIS | ARG | ARG | LEU | MET | THR | LEU | ARG | |
| 3 | GLU | ARG | HIS | ILE | LEU | GLN | GLN | ILE | VAL | ASN | |
| 4 | LEU | ILE | GLU | GLU | THR | GLY | HIS | PHE | HIS | ILE | |
| 5 | THR | ASN | THR | THR | PHE | ASP | PHE | ASP | LEU | CYS | |
| 6 | SER | LEU | ASP | LYS | THR | THR | VAL | ARG | LYS | LEU | |
| 7 | GLN | SER | TYR | LEU | GLU | THR | SER | GLY | THR | SER |
Samples:
sample_1: Chromobox protein homolog 8, [U-100% 13C; U-100% 15N], 750 uM; Protein AF-9, [U-100% 13C; U-100% 15N], 750 uM; BIS-TRIS 9.5 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O 5%; H2O 95%
sample_conditions_1: ionic strength: 100 mM; pH: 6; pressure: 1 atm; temperature: 298 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | 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 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
CCPNMR_Analysis, CCPN - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts