BMRB Entry 18215
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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/BMR18215
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Title: Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50.
Deposition date: 2012-01-24 Original release date: 2012-02-03
Authors: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Rossi, Paolo; Lange, Oliver; Lee, Hsiau-Wei; Hamilton, Keith; Ciccosanti, Colleen; Buchwald, William; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus VNG_0733H of Halobacterium salinarium, Northeast Structural Genomics Consortium Target HsR50." To be published ., .-..
Assembly members:
HsR50, polymer, 191 residues, 20753.697 Da.
Natural source: Common Name: Halobacterium salinarium Taxonomy ID: 2242 Superkingdom: Archaea Kingdom: not available Genus/species: Halobacterium salinarium
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HsR50: MSPIPLPVTDTDDAWRARIA
AHRADKDEFLATHDQSPIPP
ADRGAFDGLRYFDIDASFRV
AARYQPARDPEAVELETTRG
PPAEYTRAAVLGFDLGDSHH
TLTAFRVEGESSLFVPFTDE
TTDDGRTYEHGRYLDVDPAG
ADGGDEVALDFNLAYNPFCA
YGGSFSCALPPADNHVPAAI
TAGERVDADLE
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 704 |
15N chemical shifts | 169 |
1H chemical shifts | 1023 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HsR50 | 1 |
Entities:
Entity 1, HsR50 191 residues - 20753.697 Da.
1 | MET | SER | PRO | ILE | PRO | LEU | PRO | VAL | THR | ASP | ||||
2 | THR | ASP | ASP | ALA | TRP | ARG | ALA | ARG | ILE | ALA | ||||
3 | ALA | HIS | ARG | ALA | ASP | LYS | ASP | GLU | PHE | LEU | ||||
4 | ALA | THR | HIS | ASP | GLN | SER | PRO | ILE | PRO | PRO | ||||
5 | ALA | ASP | ARG | GLY | ALA | PHE | ASP | GLY | LEU | ARG | ||||
6 | TYR | PHE | ASP | ILE | ASP | ALA | SER | PHE | ARG | VAL | ||||
7 | ALA | ALA | ARG | TYR | GLN | PRO | ALA | ARG | ASP | PRO | ||||
8 | GLU | ALA | VAL | GLU | LEU | GLU | THR | THR | ARG | GLY | ||||
9 | PRO | PRO | ALA | GLU | TYR | THR | ARG | ALA | ALA | VAL | ||||
10 | LEU | GLY | PHE | ASP | LEU | GLY | ASP | SER | HIS | HIS | ||||
11 | THR | LEU | THR | ALA | PHE | ARG | VAL | GLU | GLY | GLU | ||||
12 | SER | SER | LEU | PHE | VAL | PRO | PHE | THR | ASP | GLU | ||||
13 | THR | THR | ASP | ASP | GLY | ARG | THR | TYR | GLU | HIS | ||||
14 | GLY | ARG | TYR | LEU | ASP | VAL | ASP | PRO | ALA | GLY | ||||
15 | ALA | ASP | GLY | GLY | ASP | GLU | VAL | ALA | LEU | ASP | ||||
16 | PHE | ASN | LEU | ALA | TYR | ASN | PRO | PHE | CYS | ALA | ||||
17 | TYR | GLY | GLY | SER | PHE | SER | CYS | ALA | LEU | PRO | ||||
18 | PRO | ALA | ASP | ASN | HIS | VAL | PRO | ALA | ALA | ILE | ||||
19 | THR | ALA | GLY | GLU | ARG | VAL | ASP | ALA | ASP | LEU | ||||
20 | GLU |
Samples:
sample_1: hsr50.005, [U-100% 13C; U-100% 15N], 0.726 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
sample_2: hsr50.009, [U-100% 13C; U-100% 15N; U-2H], 0.800 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
sample_3: hsr50.007, [U-100% 13C; U-100% 15N], 0.674 mM; Proteinase Inhibitors 1 x; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 200 mM; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM
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-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | 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 1H-13C arom NOESY | sample_1 | isotropic | sample_conditions_1 |
cCH_NOESY | sample_2 | isotropic | sample_conditions_1 |
nNH_NOESY | sample_2 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_3 | anisotropic | sample_conditions_1 |
3D HA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
TOPSPIN, Bruker Biospin - collection
PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
SPARKY, Goddard - data analysis
TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization
PALES, PALES (Zweckstetter, Bax) - geometry optimization
PSVS, Bhattacharya, Montelione - structure validation
PDBStat v5.5-exp, Tejero; Montelione - structure validation
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 900 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