BMRB Entry 19516
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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/BMR19516
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Title: Solution NMR structure of Dot1L in complex with AF9 (Dot1L-AF9).
Deposition date: 2013-09-20 Original release date: 2015-04-20
Authors: Kuntimaddi, Aravinda; Bushweller, John
Citation: Kuntimaddi, Aravinda; Bushweller, John. "Solution NMR structure of Dot1L in complex with AF9 (Dot1L-AF9)." Not known ., .-..
Assembly members:
Protein_AF-9, polymer, 69 residues, 8147.291 Da.
Dot1L_Histone-lysine_N-methyltransferase, polymer, 25 residues, 2667.140 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):
Protein_AF-9: DKAYLDELVELHRRLMTLRE
RHILQQIVNLIEETGHFHIT
NTTFDFDLCSLDKTTVRKLQ
SYLETSGTS
Dot1L_Histone-lysine_N-methyltransferase: TNKLPVSIPLASVVLPSRAE
RARST
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 414 |
| 15N chemical shifts | 89 |
| 1H chemical shifts | 638 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AF9 protein | 1 |
| 2 | Dot1L Histone lysine N-methyltransferase | 2 |
Entities:
Entity 1, AF9 protein 69 residues - 8147.291 Da.
| 1 | ASP | LYS | ALA | TYR | LEU | ASP | GLU | LEU | VAL | GLU | ||||
| 2 | LEU | HIS | ARG | ARG | LEU | MET | THR | LEU | ARG | GLU | ||||
| 3 | ARG | HIS | ILE | LEU | GLN | GLN | ILE | VAL | ASN | LEU | ||||
| 4 | ILE | GLU | GLU | THR | GLY | HIS | PHE | HIS | ILE | THR | ||||
| 5 | ASN | THR | THR | PHE | ASP | PHE | ASP | LEU | CYS | SER | ||||
| 6 | LEU | ASP | LYS | THR | THR | VAL | ARG | LYS | LEU | GLN | ||||
| 7 | SER | TYR | LEU | GLU | THR | SER | GLY | THR | SER |
Entity 2, Dot1L Histone lysine N-methyltransferase 25 residues - 2667.140 Da.
| 1 | THR | ASN | LYS | LEU | PRO | VAL | SER | ILE | PRO | LEU | ||||
| 2 | ALA | SER | VAL | VAL | LEU | PRO | SER | ARG | ALA | GLU | ||||
| 3 | ARG | ALA | ARG | SER | THR |
Samples:
Dot1L-AF9: Protein AF-9, [U-100% 13C; U-100% 15N], 750 uM; Histone-lysine N-methyltransferase, H3 lysine-79 specific, [U-100% 13C; U-100% 15N], 750 uM; Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O 10%; H2O 95%
Dot1L-AF9_RDC_sample_1: Protein AF-9, [U-100% 13C; U-100% 15N], 750 uM; Histone-lysine N-methyltransferase, H3 lysine-79 specific, [U-100% 13C; U-100% 15N], 750 uM; Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O 10%; H2O 95%; (3-acrylamidopropyl)-trimethylammonium chloride 3.5%; acrylic acid 3.5%
Dot1L-AF9_RDC_sample_2: Protein AF-9, [U-100% 13C; U-100% 15N], 750 uM; Histone-lysine N-methyltransferase, H3 lysine-79 specific, [U-100% 13C; U-100% 15N], 750 uM; Bis-Tris 9.3 mM; MES 15.8 mM; sodium chloride 100 mM; DTT 1 mM; D2O 10%; H2O 95%; (3-acrylamidopropyl)-trimethylammonium chloride 3.5%; acrylamide 3.5%
Dot1L-AF9_NMR_Sample_Conditions: ionic strength: 100 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 2D 1H-15N HSQC | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 2D 1H-13C HSQC | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D CBCA(CO)NH | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D C(CO)NH | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNCO | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNCA | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNCACB | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HCCH-TOCSY | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNHA | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D 1H-15N NOESY | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D 1H-13C NOESY aliphatic | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D 1H-13C NOESY aromatic | Dot1L-AF9 | isotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNCO IPAP | Dot1L-AF9_RDC_sample_1 | anisotropic | Dot1L-AF9_NMR_Sample_Conditions |
| 3D HNCO IPAP | Dot1L-AF9_RDC_sample_2 | anisotropic | Dot1L-AF9_NMR_Sample_Conditions |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment
SPARKY, Goddard - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
X-PLOR NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution
Molmol, Koradi, Billeter and Wuthrich - data analysis
VNMRJ, Varian - collection
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 18094 |
| PDB | |
| DBJ | BAA04090 BAB31731 BAE27603 BAG35760 BAG72836 |
| EMBL | CAA06960 CDQ62412 CDQ68675 |
| GB | AAA58361 AAH21420 AAH36089 AAI29090 AAK28536 |
| REF | NP_001179478 NP_001273087 NP_001273620 NP_004520 NP_081602 |
| SP | A2AM29 P42568 |
| TPG | DAA26970 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts