BMRB Entry 16806
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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/BMR16806
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Title: Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803. Northeast Structural Genomics Consortium Target Target SgR145.
Deposition date: 2010-03-31 Original release date: 2010-04-28
Authors: Rossi, Paolo; Forouhar, F.; Lange, O.; Lee, H.; Lemak, A; Belote, R.; Ciccosanti, C.; Foote, Erica; Sahdev, Seema; Acton, T.; Xiao, R.; Everett, J.; Montelione, Gaetano
Citation: Rossi, Paolo; Forouhar, Farhad; Lange, Oliver; Lee, Hsiau; Acton, Thomas; Xiao, Rong; Montelione, Gaetano. "Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803. Northeast Structural Genomics Consortium Target Target SgR145." To be published ., .-..
Assembly members:
SgR145, polymer, 202 residues, 22403.449 Da.
Natural source: Common Name: Synechocystis sp. PCC 6803 Taxonomy ID: 1148 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SgR145: MWDERFSQSEYVYGTEPNDF
LVSVANQIPQGKILCLAEGE
GRNACFLASLGYEVTAVDQS
SVGLAKAKQLAQEKGVKITT
VQSNLADFDIVADAWEGIVS
IFCHLPSSLRQQLYPKVYQG
LKPGGVFILEGFAPEQLQYN
TGGPKDLDLLPKLETLQSEL
PSLNWLIANNLERNLDEGAY
HQGKAALIQLLGQKLEHHHH
HH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 567 |
| 15N chemical shifts | 159 |
| 1H chemical shifts | 423 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SgR145 | 1 |
Entities:
Entity 1, SgR145 202 residues - 22403.449 Da.
| 1 | MET | TRP | ASP | GLU | ARG | PHE | SER | GLN | SER | GLU | ||||
| 2 | TYR | VAL | TYR | GLY | THR | GLU | PRO | ASN | ASP | PHE | ||||
| 3 | LEU | VAL | SER | VAL | ALA | ASN | GLN | ILE | PRO | GLN | ||||
| 4 | GLY | LYS | ILE | LEU | CYS | LEU | ALA | GLU | GLY | GLU | ||||
| 5 | GLY | ARG | ASN | ALA | CYS | PHE | LEU | ALA | SER | LEU | ||||
| 6 | GLY | TYR | GLU | VAL | THR | ALA | VAL | ASP | GLN | SER | ||||
| 7 | SER | VAL | GLY | LEU | ALA | LYS | ALA | LYS | GLN | LEU | ||||
| 8 | ALA | GLN | GLU | LYS | GLY | VAL | LYS | ILE | THR | THR | ||||
| 9 | VAL | GLN | SER | ASN | LEU | ALA | ASP | PHE | ASP | ILE | ||||
| 10 | VAL | ALA | ASP | ALA | TRP | GLU | GLY | ILE | VAL | SER | ||||
| 11 | ILE | PHE | CYS | HIS | LEU | PRO | SER | SER | LEU | ARG | ||||
| 12 | GLN | GLN | LEU | TYR | PRO | LYS | VAL | TYR | GLN | GLY | ||||
| 13 | LEU | LYS | PRO | GLY | GLY | VAL | PHE | ILE | LEU | GLU | ||||
| 14 | GLY | PHE | ALA | PRO | GLU | GLN | LEU | GLN | TYR | ASN | ||||
| 15 | THR | GLY | GLY | PRO | LYS | ASP | LEU | ASP | LEU | LEU | ||||
| 16 | PRO | LYS | LEU | GLU | THR | LEU | GLN | SER | GLU | LEU | ||||
| 17 | PRO | SER | LEU | ASN | TRP | LEU | ILE | ALA | ASN | ASN | ||||
| 18 | LEU | GLU | ARG | ASN | LEU | ASP | GLU | GLY | ALA | TYR | ||||
| 19 | HIS | GLN | GLY | LYS | ALA | ALA | LEU | ILE | GLN | LEU | ||||
| 20 | LEU | GLY | GLN | LYS | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 21 | HIS | HIS |
Samples:
sample: SgR145, [U-100% 13C; U-100% 15N], 1.1 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HNCACB | sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample | anisotropic | sample_conditions_1 |
| 3D HNCA(CO) | sample | isotropic | sample_conditions_1 |
| 3D HNCA | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C HSQC_NOESY_HSQC | sample | isotropic | sample_conditions_1 |
| 3D 1H-15N HSQC_NOESY_HSQC | sample | isotropic | sample_conditions_1 |
| 3D 1H-13C-15N HSQC_NOESY_HSQC | sample | isotropic | sample_conditions_1 |
| 3D 1H-15N-13C HSQC_NOESY_HSQC | sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample | isotropic | sample_conditions_1 |
| 1D 15N T1 | sample | isotropic | sample_conditions_1 |
| 1D 15N T2 CPMG | sample | isotropic | sample_conditions_1 |
| 2D- HET NOE | sample | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinemen, structure solution
AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement
AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
XEASY, Bartels et al. - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinemen, structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA18831 BAK51873 BAL30871 BAL34040 BAL37209 |
| GB | AGF53380 ALJ69250 |
| REF | WP_010874311 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts
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or all simulated shifts