BMRB Entry 16691
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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/BMR16691
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Title: Solution NMR Structure of Probable 30S Ribosomal Protein PSRP-3 (Ycf65-like protein) from Synechocystis sp. (strain PCC 6803), Northeast Structural Genomics Consortium Target Target SgR46
Deposition date: 2010-01-22 Original release date: 2010-02-25
Authors: Liu, G.; Janjua, J.; Xiao, R.; Buchwald, W.; Ciccosanti, C.; Belote, R.; Everett, J.; Nair, R.; Acton, T; Rost, B.; Montelione, G.
Citation: Liu, G.; Janjua, J.; Xiao, R.; Buchwald, W.; Ciccosanti, C.; Belote, R.; Everett, J.; Nair, R.; Acton, T; Rost, B.; Montelione, G.. "Solution NMR Structure of Probable 30S ribosomal protein PSRP-3 (Ycf65-like protein) from Synechocystis sp. (PCC 6803), Northeast Structural Genomics Consortium Target Target SgR46" To be published ., .-..
Assembly members:
SgR46, polymer, 116 residues, 13318.086 Da.
Natural source: Common Name: Synechocystis sp. PCC 6803 Taxonomy ID: 1148 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis Synechocystis sp. PCC 6803
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SgR46: MAASTVHTSFILKVLWLDQN
VAIAVDQIVGKGTSPLTSYF
FWPRADAWQQLKDELEAKHW
IAEADRINVLNQATEVINFW
QDLKNQNKQISMAEAQGKFP
EVVFSGSNLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 373 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 783 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SgR46 | 1 |
Entities:
Entity 1, SgR46 116 residues - 13318.086 Da.
| 1 | MET | ALA | ALA | SER | THR | VAL | HIS | THR | SER | PHE | ||||
| 2 | ILE | LEU | LYS | VAL | LEU | TRP | LEU | ASP | GLN | ASN | ||||
| 3 | VAL | ALA | ILE | ALA | VAL | ASP | GLN | ILE | VAL | GLY | ||||
| 4 | LYS | GLY | THR | SER | PRO | LEU | THR | SER | TYR | PHE | ||||
| 5 | PHE | TRP | PRO | ARG | ALA | ASP | ALA | TRP | GLN | GLN | ||||
| 6 | LEU | LYS | ASP | GLU | LEU | GLU | ALA | LYS | HIS | TRP | ||||
| 7 | ILE | ALA | GLU | ALA | ASP | ARG | ILE | ASN | VAL | LEU | ||||
| 8 | ASN | GLN | ALA | THR | GLU | VAL | ILE | ASN | PHE | TRP | ||||
| 9 | GLN | ASP | LEU | LYS | ASN | GLN | ASN | LYS | GLN | ILE | ||||
| 10 | SER | MET | ALA | GLU | ALA | GLN | GLY | LYS | PHE | PRO | ||||
| 11 | GLU | VAL | VAL | PHE | SER | GLY | SER | ASN | LEU | GLU | ||||
| 12 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample: SgR46, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%
sample_1: SgR46, [U-10% 13C; U-100% 15N], 0.8 mM; H2O 95%; D2O 5%
sample_2: SgR46, [U-100% 13C; U-100% 15N], 0.3 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 7.5; pressure: 1.0 atm; temperature: 293 K
sample_conditions_2: pH: 4.5; pressure: 1.0 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic 927 | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_2 |
| 3D CBCA(CO)NH 816 | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-13C arom NOESY | sample | isotropic | sample_conditions_1 |
| 3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESY | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_2 |
| 3D HCCH-TOCSY 829 | sample | isotropic | sample_conditions_1 |
| 3D HNCA | sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH 819 | sample_2 | isotropic | sample_conditions_2 |
| 3D C(CO)NH | sample_2 | isotropic | sample_conditions_2 |
| 3D HNCOCA | sample_2 | isotropic | sample_conditions_2 |
| 3D 1H-15N NOESY 939 | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY 940 | sample_1 | isotropic | sample_conditions_1 |
| 1D T1 | sample_1 | isotropic | sample_conditions_1 |
| 1D T2 | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C arom HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY 830 | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic 928 | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | 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
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment
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
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA10474 BAK51259 BAL30257 BAL33426 BAL36595 |
| GB | AGF52766 AIE74500 ALJ68680 |
| REF | WP_010873701 WP_038531511 |
| SP | Q55385 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts