BMRB Entry 15274
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15274
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Title: NMR chemical shift assignments for Arf-binding domain of Hdm2 PubMed: 18809412
Deposition date: 2007-05-31 Original release date: 2008-10-28
Authors: Sivakolundu, Sivashankar; Kriwacki, Richard
Citation: Sivakolundu, Sivashankar; Nourse, Amanda; Moshiach, Simon; Bothner, Brian; Ashley, Chimere; Satumba, John; Lahti, Jill; Kriwacki, Richard. "Intrinsically Unstructured Domains of Arf and Hdm2 Form Bimolecular Oligomeric Structures In Vitro and In Vivo" J. Mol. Biol. 384, 240-254 (2008).
Assembly members:
Hdm2-ABD, polymer, 99 residues, Formula weight is not available
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):
Hdm2-ABD: GSHMSSSSESTGTPSNPDLD
AGVSEHSGDWLDQDSVSDQF
SVEFEVESLDSEDYSLSEEG
QELSDEDDEVYQVTVYQAGE
SDTDSFEEDPEISLADYWK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 276 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 91 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Hdm2-ABD | 1 |
Entities:
Entity 1, Hdm2-ABD 99 residues - Formula weight is not available
| 1 | GLY | SER | HIS | MET | SER | SER | SER | SER | GLU | SER | ||||
| 2 | THR | GLY | THR | PRO | SER | ASN | PRO | ASP | LEU | ASP | ||||
| 3 | ALA | GLY | VAL | SER | GLU | HIS | SER | GLY | ASP | TRP | ||||
| 4 | LEU | ASP | GLN | ASP | SER | VAL | SER | ASP | GLN | PHE | ||||
| 5 | SER | VAL | GLU | PHE | GLU | VAL | GLU | SER | LEU | ASP | ||||
| 6 | SER | GLU | ASP | TYR | SER | LEU | SER | GLU | GLU | GLY | ||||
| 7 | GLN | GLU | LEU | SER | ASP | GLU | ASP | ASP | GLU | VAL | ||||
| 8 | TYR | GLN | VAL | THR | VAL | TYR | GLN | ALA | GLY | GLU | ||||
| 9 | SER | ASP | THR | ASP | SER | PHE | GLU | GLU | ASP | PRO | ||||
| 10 | GLU | ILE | SER | LEU | ALA | ASP | TYR | TRP | LYS |
Samples:
sample_1: Hdm2-ABD, [U-98% 13C; U-98% 15N], 1 mM; sodium phosphate 10 mM; NaCl 10 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.02 M; 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
FELIX, Accelrys Software Inc. - chemical shift assignment, data analysis, peak picking
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
- Varian INOVA 600 MHz
Related Database Links:
| DBJ | BAB11975 BAC78209 BAF83030 BAJ17752 |
| EMBL | CAA78055 CAH89564 CAP16704 CAP16705 CAP16729 |
| GB | AAA60568 AAA75514 AAA75516 AAF28866 AAF42995 |
| PRF | 1814460A |
| REF | NP_001009346 NP_001092577 NP_001124685 NP_001138811 NP_001138812 |
| SP | P56950 P56951 Q00987 Q7YRZ8 |
| TPG | DAA29805 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts