BMRB Entry 15465
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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/BMR15465
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Title: SOLUTION STRUCTURE OF THE N-TERMINAL DOMAIN OF PH1500
Deposition date: 2007-09-11 Original release date: 2009-10-12
Authors: Varnay, I.; Truffault, V.; Coles, M.
Citation: Varnay, I.; Djuranovic, S.; Truffault, V.; Lupas, A.; Kessler, H.; Coles, M.. "The Solution Structure of Ph1500-N" . ., .-..
Assembly members:
HYPOTHETICAL_PROTEIN_PH1500, polymer, 83 residues, 9456.377 Da.
Natural source: Common Name: Pyrococcus horikoshii Taxonomy ID: 53953 Superkingdom: Archaea Kingdom: not available Genus/species: PYROCOCCUS HORIKOSHII
Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI
Entity Sequences (FASTA):
HYPOTHETICAL_PROTEIN_PH1500: HHHHHHMEGVIMSELKLKPL
PKVELPPDFVDVIRIKLQGK
TVRTGDVIGISILGKEVKFK
VVQAYPSPLRVEDRTKITLV
THP
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 345 |
| 15N chemical shifts | 70 |
| 1H chemical shifts | 589 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HYPOTHETICAL PROTEIN PH1500 | 1 |
Entities:
Entity 1, HYPOTHETICAL PROTEIN PH1500 83 residues - 9456.377 Da.
| 1 | HIS | HIS | HIS | HIS | HIS | HIS | MET | GLU | GLY | VAL | ||||
| 2 | ILE | MET | SER | GLU | LEU | LYS | LEU | LYS | PRO | LEU | ||||
| 3 | PRO | LYS | VAL | GLU | LEU | PRO | PRO | ASP | PHE | VAL | ||||
| 4 | ASP | VAL | ILE | ARG | ILE | LYS | LEU | GLN | GLY | LYS | ||||
| 5 | THR | VAL | ARG | THR | GLY | ASP | VAL | ILE | GLY | ILE | ||||
| 6 | SER | ILE | LEU | GLY | LYS | GLU | VAL | LYS | PHE | LYS | ||||
| 7 | VAL | VAL | GLN | ALA | TYR | PRO | SER | PRO | LEU | ARG | ||||
| 8 | VAL | GLU | ASP | ARG | THR | LYS | ILE | THR | LEU | VAL | ||||
| 9 | THR | HIS | PRO |
Samples:
sample_1: HYPOTHETICAL PROTEIN PH1500 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_2: HYPOTHETICAL PROTEIN PH1500, [U-100% 15N], 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_3: HYPOTHETICAL PROTEIN PH1500, [U-100% 13C; U-100% 15N], 1 mM; PHOSPHATE BUFFER 50 mM; sodium chloride 50 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 300 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D_15N-SEPARATED_ NOESY | sample_2 | isotropic | sample_conditions_1 |
| HNHA | sample_2 | isotropic | sample_conditions_1 |
| HNHB | sample_2 | isotropic | sample_conditions_1 |
| CNH-NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D_13C-SEPARATED_NOESY | sample_3 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_3 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_3 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_3 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH vNIH-2.9.4A, BRUNGER, A - refinement, structure solution
xwinnmr v3.6, Bruker Biospin - collection, processing
SPARKY v3.110, Goddard - data analysis
NMR spectrometers:
- BRUKER DMX 600 MHz
- BRUKER DMX 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts