BMRB Entry 16251
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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/BMR16251
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Title: Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus, Northeast Structural Genomics Consortium Target SyR103B
Deposition date: 2009-04-10 Original release date: 2009-06-23
Authors: Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Mills, Jeffrey; Hua, Jia; Belote, Rachel; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, G; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus" Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
syr103b_protein, polymer, 110 residues, 13529.361 Da.
Natural source: Common Name: Staphyloccus 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):
syr103b_protein: MITFADYFYQWYEVNKLPHV
SESTKRHYESAYKHIKDHFR
HKLLKDIKRTEYQKFLNEYG
LTHSYETIRKLNSYIRNAFD
DAIHEGYVIKNPTYKAELHA
SVLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 480 |
| 15N chemical shifts | 118 |
| 1H chemical shifts | 781 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | syr103b | 1 |
Entities:
Entity 1, syr103b 110 residues - 13529.361 Da.
Residues 2-102 correspond to the 59-159 fragment of the native protein. Residues 103-110 represent a non-native affinity tag, and residue 1 is a result of a new transcription initiation site
| 1 | MET | ILE | THR | PHE | ALA | ASP | TYR | PHE | TYR | GLN | |
| 2 | TRP | TYR | GLU | VAL | ASN | LYS | LEU | PRO | HIS | VAL | |
| 3 | SER | GLU | SER | THR | LYS | ARG | HIS | TYR | GLU | SER | |
| 4 | ALA | TYR | LYS | HIS | ILE | LYS | ASP | HIS | PHE | ARG | |
| 5 | HIS | LYS | LEU | LEU | LYS | ASP | ILE | LYS | ARG | THR | |
| 6 | GLU | TYR | GLN | LYS | PHE | LEU | ASN | GLU | TYR | GLY | |
| 7 | LEU | THR | HIS | SER | TYR | GLU | THR | ILE | ARG | LYS | |
| 8 | LEU | ASN | SER | TYR | ILE | ARG | ASN | ALA | PHE | ASP | |
| 9 | ASP | ALA | ILE | HIS | GLU | GLY | TYR | VAL | ILE | LYS | |
| 10 | ASN | PRO | THR | TYR | LYS | ALA | GLU | LEU | HIS | ALA | |
| 11 | SER | VAL | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC: syr103b_protein, [U-100% 13C; U-100% 15N], 0.69 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90.00%; D2O 10.00%
NC5: syr103b_protein, [U-5% 13C; U-100% 15N], 0.6 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90.00%; D2O 10.00%
sample_conditions_1: ionic strength: 0.215 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N,13C NOESY | NC | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aromatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl | NC5 | isotropic | sample_conditions_1 |
| 2D MEXICO | NC | isotropic | sample_conditions_1 |
| 2D CLEANEX | NC | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.0.2, Guntert - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
CSI v2.0, Wishart and Sykes - data analysis
TALOS v2007.068.09.07, Shen, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure validation
CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.3, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts