BMRB Entry 17298
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17298
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Title: Resonance assignments of protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2 PubMed: 21229398
Deposition date: 2010-11-15 Original release date: 2011-01-18
Authors: Feng, Yingang
Citation: Xuan, Jinsong; Song, Xiaxia; Wang, Jinfeng; Feng, Yingang. "Resonance assignments of a putative PilT N-terminus domain protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2." Biomol. NMR Assignments 5, 161-164 (2011).
Assembly members:
sso1118, polymer, 119 residues, Formula weight is not available
Natural source: Common Name: crenarchaeotes Taxonomy ID: 273057 Superkingdom: Archaea Kingdom: not available Genus/species: Sulfolobus Sulfolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
sso1118: MFAVISPSAFGKLKEILGSN
KNYKFVITTLGVSFAIKSGI
DIDSALDRGVIVRAFSHKPP
KVGNLPQYESEAIMVAFELN
ALLIAEDKDVINKAKELGVN
AIPIEELLASSLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 510 |
| 15N chemical shifts | 113 |
| 1H chemical shifts | 826 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | sso1118 | 1 |
Entities:
Entity 1, sso1118 119 residues - Formula weight is not available
| 1 | MET | PHE | ALA | VAL | ILE | SER | PRO | SER | ALA | PHE | ||||
| 2 | GLY | LYS | LEU | LYS | GLU | ILE | LEU | GLY | SER | ASN | ||||
| 3 | LYS | ASN | TYR | LYS | PHE | VAL | ILE | THR | THR | LEU | ||||
| 4 | GLY | VAL | SER | PHE | ALA | ILE | LYS | SER | GLY | ILE | ||||
| 5 | ASP | ILE | ASP | SER | ALA | LEU | ASP | ARG | GLY | VAL | ||||
| 6 | ILE | VAL | ARG | ALA | PHE | SER | HIS | LYS | PRO | PRO | ||||
| 7 | LYS | VAL | GLY | ASN | LEU | PRO | GLN | TYR | GLU | SER | ||||
| 8 | GLU | ALA | ILE | MET | VAL | ALA | PHE | GLU | LEU | ASN | ||||
| 9 | ALA | LEU | LEU | ILE | ALA | GLU | ASP | LYS | ASP | VAL | ||||
| 10 | ILE | ASN | LYS | ALA | LYS | GLU | LEU | GLY | VAL | ASN | ||||
| 11 | ALA | ILE | PRO | ILE | GLU | GLU | LEU | LEU | ALA | SER | ||||
| 12 | SER | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: sso1118 0.8 ± 0.1 mM; potassium phosphate 50 mM; DSS 0.02%; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CBCA)(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CBCA)NH | 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-15N NOESY-HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY-HSQC for aliphatic region | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY-HSQC for aromatic region | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
FELIX, Accelrys Software Inc. - chemical shift assignment, processing
NMR spectrometers:
- Bruker DMX 600 MHz
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