BMRB Entry 16072
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16072
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Title: Solution NMR structure of SSP0047 from Staphylococcus saprophyticus. Northeast Structural Genomics Consortium Target SyR6.
Deposition date: 2008-12-19 Original release date: 2009-02-17
Authors: Ramelot, Theresa; Ding, Keyang; Chen, Chen; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Ding, Keyang; Chen, Chen; Jiang, Mei; Ciccosanti, Colleen; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of SSP0047 from Staphylococcus saprophyticus. Northeast Structural Genomics Consortium Target SyR6." Not known ., .-..
Assembly members:
SSP0047, polymer, 120 residues, 13320 Da.
Natural source: Common Name: Staphylococcus saprophyticus Taxonomy ID: 29385 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus saprophyticus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SSP0047: MTLELQLKHYITNLFNLPRD
EKWECESIEEVADDILPDQY
VRLGPLSNKILQTNTYYSDT
LHKSNIYPFILYYQKQLIAI
GFIDENHDMDFLYLHNTVMP
LLDQRYLLTGGQLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 547 |
| 15N chemical shifts | 120 |
| 1H chemical shifts | 858 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SSP0047 | 1 |
Entities:
Entity 1, SSP0047 120 residues - 13320 Da.
| 1 | MET | THR | LEU | GLU | LEU | GLN | LEU | LYS | HIS | TYR | |
| 2 | ILE | THR | ASN | LEU | PHE | ASN | LEU | PRO | ARG | ASP | |
| 3 | GLU | LYS | TRP | GLU | CYS | GLU | SER | ILE | GLU | GLU | |
| 4 | VAL | ALA | ASP | ASP | ILE | LEU | PRO | ASP | GLN | TYR | |
| 5 | VAL | ARG | LEU | GLY | PRO | LEU | SER | ASN | LYS | ILE | |
| 6 | LEU | GLN | THR | ASN | THR | TYR | TYR | SER | ASP | THR | |
| 7 | LEU | HIS | LYS | SER | ASN | ILE | TYR | PRO | PHE | ILE | |
| 8 | LEU | TYR | TYR | GLN | LYS | GLN | LEU | ILE | ALA | ILE | |
| 9 | GLY | PHE | ILE | ASP | GLU | ASN | HIS | ASP | MET | ASP | |
| 10 | PHE | LEU | TYR | LEU | HIS | ASN | THR | VAL | MET | PRO | |
| 11 | LEU | LEU | ASP | GLN | ARG | TYR | LEU | LEU | THR | GLY | |
| 12 | GLY | GLN | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; H2O 95%; D2O 5%
NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-100% 13C; U-100% 15N], 0.3 ± 0.05 mM; D2O 100%
NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; protein, [U-5% 13C; U-100% 15N], 0.3 ± 0.05 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample | isotropic | sample_conditions_1 |
| 4D 1H-13C NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5_sample | isotropic | sample_conditions_1 |
| 3D CBCACOCAHA | NC_sample_in_D2O | isotropic | sample_conditions_1 |
Software:
NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Bruker AvanceIII 850 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts