BMRB Entry 16467
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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/BMR16467
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Title: The Solution structure of the eTAFH domain of AML1-ETO complexed with HEB peptide PubMed: 19204326
Deposition date: 2009-08-25 Original release date: 2009-12-11
Authors: Park, Sangho; Cierpicki, Tomasz; Tonelli, Marco; Bushweller, John
Citation: Park, Sangho; Chen, Wei; Cierpicki, Tomasz; Tonelli, Marco; Cai, Xiongwei; Speck, Nancy; Bushweller, John. "Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity." Blood 113, 3558-3567 (2009).
Assembly members:
entity_1, polymer, 103 residues, 11623.564 Da.
entity_2, polymer, 18 residues, 1990.227 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: GAMGSGARQLSKLKRFLTTL
QQFGNDISPEIGERVRTLVL
GLVNSTLTIEEFHSKLQEAT
NFPLRPFVIPFLKANLPLLQ
RELLHCARLAKQNPAQYLAQ
HEQ
entity_2: IGTDKELSDLLDFSAMFS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 456 |
| 15N chemical shifts | 108 |
| 1H chemical shifts | 760 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 2 |
Entities:
Entity 1, entity_1 103 residues - 11623.564 Da.
| 1 | GLY | ALA | MET | GLY | SER | GLY | ALA | ARG | GLN | LEU | ||||
| 2 | SER | LYS | LEU | LYS | ARG | PHE | LEU | THR | THR | LEU | ||||
| 3 | GLN | GLN | PHE | GLY | ASN | ASP | ILE | SER | PRO | GLU | ||||
| 4 | ILE | GLY | GLU | ARG | VAL | ARG | THR | LEU | VAL | LEU | ||||
| 5 | GLY | LEU | VAL | ASN | SER | THR | LEU | THR | ILE | GLU | ||||
| 6 | GLU | PHE | HIS | SER | LYS | LEU | GLN | GLU | ALA | THR | ||||
| 7 | ASN | PHE | PRO | LEU | ARG | PRO | PHE | VAL | ILE | PRO | ||||
| 8 | PHE | LEU | LYS | ALA | ASN | LEU | PRO | LEU | LEU | GLN | ||||
| 9 | ARG | GLU | LEU | LEU | HIS | CYS | ALA | ARG | LEU | ALA | ||||
| 10 | LYS | GLN | ASN | PRO | ALA | GLN | TYR | LEU | ALA | GLN | ||||
| 11 | HIS | GLU | GLN |
Entity 2, entity_2 18 residues - 1990.227 Da.
| 1 | ILE | GLY | THR | ASP | LYS | GLU | LEU | SER | ASP | LEU | ||||
| 2 | LEU | ASP | PHE | SER | ALA | MET | PHE | SER |
Samples:
sample_1: Bis-Tris 25 mM; EDTA 1 mM; sodium chloride 350 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 350 mM; pH: 6; pressure: 1 atm; temperature: 303 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 HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 500 MHz
- Bruker Avance 900 MHz
Related Database Links:
| PDB | |
| DBJ | BAA03089 BAA03247 BAA03558 BAA03559 BAA03560 BAE21989 BAE25324 BAE41376 BAG10617 BAG57800 |
| EMBL | CAA56311 CAF99400 CAG33073 CAH65373 CAA46052 CAD89914 CAG31482 CAL38596 CDQ61893 |
| GB | AAB34819 AAB34820 AAB92651 AAC28931 AAC28932 AAA42115 AAA58632 AAB62389 AAH50556 AAH92888 |
| REF | NP_001025751 NP_001070244 NP_001089065 NP_001101923 NP_001102127 NP_001071353 NP_001187118 NP_001187135 NP_001187247 NP_001240791 |
| SP | O54972 O75081 Q06455 Q5F3B1 Q61909 P51514 Q61286 Q99081 |
| TPG | DAA20254 DAA01129 DAA25320 |
| BMRB | 16851 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts