BMRB Entry 16091
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16091
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Title: SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S8E; FROM Methanothermobacter thermautotrophicus, NORTHEASTSTRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET TR71D
Deposition date: 2008-12-24 Original release date: 2009-02-17
Authors: Liu, Gaohua; Rossi, Paolo; Wang, Dongyan; NWOSU, CHIOMA; OWENS, LEAH; Xiao, Rong; Liu, Jinfeng; BARAN, MICHAEL; SWAPNA, G.V.T; ACTON, THOMAS; Rost, BURKHARD; MONTELIONE, GAETANO
Citation: Liu, Gaohua; MONTELIONE, Gaetano. "SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S8E FROM Methanothermobacter thermautotrophicus, NORTHEASTSTRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET" Not known ., .-..
Assembly members:
rps8e, polymer, 294 residues, 33088.738 Da.
Natural source: Common Name: Methanobacterium thermoautotrophicum Taxonomy ID: 145262 Superkingdom: Archaea Kingdom: not available Genus/species: Methanobacterium thermoautotrophicum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 303 |
| 15N chemical shifts | 97 |
| 1H chemical shifts | 662 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rps8e | 1 |
Entities:
Entity 1, rps8e 294 residues - 33088.738 Da.
| 1 | GLY | ASP | ARG | ARG | VAL | ARG | LEU | ILE | ARG | THR | ||||
| 2 | ARG | GLY | GLY | ASN | THR | LYS | VAL | ARG | LEU | ALA | ||||
| 3 | SER | ASP | THR | ARG | ILE | ASN | VAL | VAL | ASP | PRO | ||||
| 4 | GLU | THR | GLY | LYS | VAL | GLU | ILE | ALA | GLU | ILE | ||||
| 5 | ARG | ASN | VAL | VAL | GLU | ASN | THR | ALA | ASN | PRO | ||||
| 6 | HIS | PHE | VAL | ARG | ARG | ASN | ILE | ILE | THR | ARG | ||||
| 7 | GLY | ALA | VAL | VAL | GLU | THR | ASN | LEU | GLY | ASN | ||||
| 8 | VAL | ARG | VAL | THR | SER | ARG | PRO | GLY | GLN | ASP | ||||
| 9 | GLY | VAL | ILE | ASN | GLY | VAL | LEU | ILE | ARG | GLU | ||||
| 10 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS | GLY | ASP | ||||
| 11 | ARG | ARG | VAL | ARG | LEU | ILE | ARG | THR | ARG | GLY | ||||
| 12 | GLY | ASN | THR | LYS | VAL | ARG | LEU | ALA | SER | ASP | ||||
| 13 | THR | ARG | ILE | ASN | VAL | VAL | ASP | PRO | GLU | THR | ||||
| 14 | GLY | LYS | VAL | GLU | ILE | ALA | GLU | ILE | ARG | ASN | ||||
| 15 | VAL | VAL | GLU | ASN | THR | ALA | ASN | PRO | HIS | PHE | ||||
| 16 | VAL | ARG | ARG | ASN | ILE | ILE | THR | ARG | GLY | ALA | ||||
| 17 | VAL | VAL | GLU | THR | ASN | LEU | GLY | ASN | VAL | ARG | ||||
| 18 | VAL | THR | SER | ARG | PRO | GLY | GLN | ASP | GLY | VAL | ||||
| 19 | ILE | ASN | GLY | VAL | LEU | ILE | ARG | GLU | LEU | GLU | ||||
| 20 | HIS | HIS | HIS | HIS | HIS | HIS | GLY | ASP | ARG | ARG | ||||
| 21 | VAL | ARG | LEU | ILE | ARG | THR | ARG | GLY | GLY | ASN | ||||
| 22 | THR | LYS | VAL | ARG | LEU | ALA | SER | ASP | THR | ARG | ||||
| 23 | ILE | ASN | VAL | VAL | ASP | PRO | GLU | THR | GLY | LYS | ||||
| 24 | VAL | GLU | ILE | ALA | GLU | ILE | ARG | ASN | VAL | VAL | ||||
| 25 | GLU | ASN | THR | ALA | ASN | PRO | HIS | PHE | VAL | ARG | ||||
| 26 | ARG | ASN | ILE | ILE | THR | ARG | GLY | ALA | VAL | VAL | ||||
| 27 | GLU | THR | ASN | LEU | GLY | ASN | VAL | ARG | VAL | THR | ||||
| 28 | SER | ARG | PRO | GLY | GLN | ASP | GLY | VAL | ILE | ASN | ||||
| 29 | GLY | VAL | LEU | ILE | ARG | GLU | LEU | GLU | HIS | HIS | ||||
| 30 | HIS | HIS | HIS | HIS |
Samples:
sample_1: rps8e, [U-100% 13C; U-100% 15N], 0.94 mM; H2O 95%; D2O 5%
sample_2: rps8e, [U-10% 13C; U-100% 15N], 1 mM; H2O 95%; D2O 5%
sample_1d20: rps8e, [U-100% 13C; U-100% 15N], 0.94 mM; D2O 100%
sample_conditions_1: pH: 6.5; 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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1d20 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1d20 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct, Huang, Tejero, Powers and Montelione - geometry optimization, peak picking, refinement
PSVS, Bhattacharya and Montelione - geometry optimization
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts