BMRB Entry 18180
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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/BMR18180
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Title: Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11.
Deposition date: 2012-01-05 Original release date: 2012-01-12
Authors: Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano
Citation: Rossi, Paolo; Liu, Gaohua; Lange, Oliver; Lee, Hsiau-Wei; Janjua, Haleema; Ciccosanti, Colleen; Wang, Huang; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11." To be published ., .-..
Assembly members:
HmR11, polymer, 185 residues, 21399.959 Da.
Natural source: Common Name: Haloarcula marismortui Taxonomy ID: 2238 Superkingdom: Archaea Kingdom: not available Genus/species: Haloarcula marismortui
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HmR11: MDEDTEDWETQLQANRDEKD
RFFSEHRQSPIPPEERDDFD
GLSYFDPDPDYRVEATVTVH
ETPESVDLETSDDRTVRYLH
VATLSFDLDGESRDLHAFRQ
AADESRTLFVPFRDKTTGQQ
SYDGGRYMELEPDRDLSDGD
EITLDFNLAYSPFCAYSDTF
SCPLPPESNWLETAVTAGER
TDLEH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 803 |
| 15N chemical shifts | 197 |
| 1H chemical shifts | 1209 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | HmR11 | 1 |
Entities:
Entity 1, HmR11 185 residues - 21399.959 Da.
| 1 | MET | ASP | GLU | ASP | THR | GLU | ASP | TRP | GLU | THR | ||||
| 2 | GLN | LEU | GLN | ALA | ASN | ARG | ASP | GLU | LYS | ASP | ||||
| 3 | ARG | PHE | PHE | SER | GLU | HIS | ARG | GLN | SER | PRO | ||||
| 4 | ILE | PRO | PRO | GLU | GLU | ARG | ASP | ASP | PHE | ASP | ||||
| 5 | GLY | LEU | SER | TYR | PHE | ASP | PRO | ASP | PRO | ASP | ||||
| 6 | TYR | ARG | VAL | GLU | ALA | THR | VAL | THR | VAL | HIS | ||||
| 7 | GLU | THR | PRO | GLU | SER | VAL | ASP | LEU | GLU | THR | ||||
| 8 | SER | ASP | ASP | ARG | THR | VAL | ARG | TYR | LEU | HIS | ||||
| 9 | VAL | ALA | THR | LEU | SER | PHE | ASP | LEU | ASP | GLY | ||||
| 10 | GLU | SER | ARG | ASP | LEU | HIS | ALA | PHE | ARG | GLN | ||||
| 11 | ALA | ALA | ASP | GLU | SER | ARG | THR | LEU | PHE | VAL | ||||
| 12 | PRO | PHE | ARG | ASP | LYS | THR | THR | GLY | GLN | GLN | ||||
| 13 | SER | TYR | ASP | GLY | GLY | ARG | TYR | MET | GLU | LEU | ||||
| 14 | GLU | PRO | ASP | ARG | ASP | LEU | SER | ASP | GLY | ASP | ||||
| 15 | GLU | ILE | THR | LEU | ASP | PHE | ASN | LEU | ALA | TYR | ||||
| 16 | SER | PRO | PHE | CYS | ALA | TYR | SER | ASP | THR | PHE | ||||
| 17 | SER | CYS | PRO | LEU | PRO | PRO | GLU | SER | ASN | TRP | ||||
| 18 | LEU | GLU | THR | ALA | VAL | THR | ALA | GLY | GLU | ARG | ||||
| 19 | THR | ASP | LEU | GLU | HIS |
Samples:
sample_1: HmR11-1, [U-100% 13C; U-100% 15N], 0.7 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM
sample_2: HmR11-1, [U-5% 13C; U-100% 15N], 1.2 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 50 uM
sample_3: HmR11, [U-5% 13C; U-100% 15N], 0.75 mM; NaN3-2 0.02%; DTT-3 10 mM; CaCL2-4 5 mM; NaCL-5 100 mM; Proteinase Inhibitors-6 1 x; MES pH 6.5-7 20 mM; D2O-8 10%; DSS-9 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 |
| 3D 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D hetnoe | sample_2 | isotropic | sample_conditions_1 |
| 1D T1 inv.rec | sample_2 | isotropic | sample_conditions_1 |
| 1D T2 CPMG | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC highres | sample_2 | isotropic | sample_conditions_1 |
| Jmod 15N TROSY | sample_3 | anisotropic | sample_conditions_1 |
| jmod 15N TROSY | sample_3 | anisotropic | 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
XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - 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
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| GB | AAV45400 EMA13016 EMA22096 |
| REF | WP_004962568 WP_007188424 WP_011222974 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts