BMRB Entry 16155
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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/BMR16155
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Title: Solution NMR structure of protein HS00059 from Homo Sapiens. Northeast Structural Genomics Consortium (NESG) target HT98A.
Deposition date: 2009-01-30 Original release date: 2009-03-12
Authors: Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl
Citation: Lemak, Alexander; Gutmanas, Aleksandras; Fares, Christophe; Quyang, Hui; Dhe-Paganon, Sirano; Montelione, Gaetano; Arrowsmith, Cheryl. "Solution NMR Structure of human protein HS00059" Not known ., .-..
Assembly members:
hs00059, polymer, 112 residues, 14686.104 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):
hs00059: MHHHHHHSSGRENLYFQGNN
EKVTLVRIADLENHNNDGGF
WTVIDGKVYDIKDFQTQSLT
ENSILAQFAGEDPVVALEAA
LQFEDTRESMHAFCVGQYLE
PDQEGVTIPDLG
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 374 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 620 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | hs00059 | 1 |
Entities:
Entity 1, hs00059 112 residues - 14686.104 Da.
| 1 | MET | HIS | HIS | HIS | HIS | HIS | HIS | SER | SER | GLY | ||||
| 2 | ARG | GLU | ASN | LEU | TYR | PHE | GLN | GLY | ASN | ASN | ||||
| 3 | GLU | LYS | VAL | THR | LEU | VAL | ARG | ILE | ALA | ASP | ||||
| 4 | LEU | GLU | ASN | HIS | ASN | ASN | ASP | GLY | GLY | PHE | ||||
| 5 | TRP | THR | VAL | ILE | ASP | GLY | LYS | VAL | TYR | ASP | ||||
| 6 | ILE | LYS | ASP | PHE | GLN | THR | GLN | SER | LEU | THR | ||||
| 7 | GLU | ASN | SER | ILE | LEU | ALA | GLN | PHE | ALA | GLY | ||||
| 8 | GLU | ASP | PRO | VAL | VAL | ALA | LEU | GLU | ALA | ALA | ||||
| 9 | LEU | GLN | PHE | GLU | ASP | THR | ARG | GLU | SER | MET | ||||
| 10 | HIS | ALA | PHE | CYS | VAL | GLY | GLN | TYR | LEU | GLU | ||||
| 11 | PRO | ASP | GLN | GLU | GLY | VAL | THR | ILE | PRO | ASP | ||||
| 12 | LEU | GLY |
Samples:
sample_1: hs00059, [U-13C; U-15N], 0.5 mM; TRIS 10 mM; sodium chloride 300 mM; ZnSO4 10 uM; DTT 10 mM; NaN3 0.01%; benzamidine 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 300 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D (H)CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C_arom NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
FMC, Lemak, Steren, Llinas, Arrowsmith - chemical shift assignment
TALOS, Cornilescu, Delaglio and Bax - data analysis
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts