BMRB Entry 15829
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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/BMR15829
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Title: SOLUTION NMR STRUCTURE OF SAG0934 from Streptococcus agalactiae. NORTHEAST STRUCTURAL GENOMICS TARGET SaR32[1-108].
Deposition date: 2008-06-26 Original release date: 2009-05-07
Authors: Aramini, James; Rossi, Paolo; Zhao, Li; Foote, Erica; Jiang, Mei; Xiao, Rong; Sharma, Seema; Swapna, G; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Aramini, James; Rossi, Paolo; Zhao, Li; Foote, Erica; Jiang, Mei; Xiao, Rong; Sharma, Seema; Swapna, G; Nair, Rajesh; Everett, John; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "SOLUTION NMR STRUCTURE OF SAG0934 from Streptococcus agalactiae. NORTHEAST STRUCTURAL GENOMICS TARGET SaR32[1-108]." Not known ., .-..
Assembly members:
SaR32, polymer, 116 residues, 13226.012 Da.
Natural source: Common Name: Streptococcus agalactiae Taxonomy ID: 1311 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus agalactiae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SaR32: MMRLANGIVLDKDTTFGELK
FSALRREVRIQNEDGSVSDE
IKERTYDLKSKGQGRMIQVS
IPASVPLKEFDYNARVELIN
PIADTVATATYQGADVDWYI
KADDIVLTLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 502 |
| 15N chemical shifts | 117 |
| 1H chemical shifts | 792 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SaR32 | 1 |
Entities:
Entity 1, SaR32 116 residues - 13226.012 Da.
C-terminal LEHHHHHH purification tag starting at residue 109. The construct was optimized by Hydrogen/Deuterium exchange mass spectrometry (DXMS)
| 1 | MET | MET | ARG | LEU | ALA | ASN | GLY | ILE | VAL | LEU | ||||
| 2 | ASP | LYS | ASP | THR | THR | PHE | GLY | GLU | LEU | LYS | ||||
| 3 | PHE | SER | ALA | LEU | ARG | ARG | GLU | VAL | ARG | ILE | ||||
| 4 | GLN | ASN | GLU | ASP | GLY | SER | VAL | SER | ASP | GLU | ||||
| 5 | ILE | LYS | GLU | ARG | THR | TYR | ASP | LEU | LYS | SER | ||||
| 6 | LYS | GLY | GLN | GLY | ARG | MET | ILE | GLN | VAL | SER | ||||
| 7 | ILE | PRO | ALA | SER | VAL | PRO | LEU | LYS | GLU | PHE | ||||
| 8 | ASP | TYR | ASN | ALA | ARG | VAL | GLU | LEU | ILE | ASN | ||||
| 9 | PRO | ILE | ALA | ASP | THR | VAL | ALA | THR | ALA | THR | ||||
| 10 | TYR | GLN | GLY | ALA | ASP | VAL | ASP | TRP | TYR | ILE | ||||
| 11 | LYS | ALA | ASP | ASP | ILE | VAL | LEU | THR | LEU | GLU | ||||
| 12 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SaR32, [U-100% 13C; U-100% 15N], 0.46 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; H2O 95%; D2O, [U-100% 2H], 5%
sample_2: SaR32, [U-100% 13C; U-100% 15N], 0.46 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; D2O, [U-100% 2H], 100%
sample_3: SaR32, [U-5% 13C; U-100% 15N], 0.57 mM; MES 20 mM; sodium chloride 100 mM; DTT 10 mM; calcium chloride 5 mM; sodium azide 0.02%; D2O, [U-100% 2H], 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| CCH-TOCSY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D simultaneous CN NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| simultaneous CN NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high res. (L/V stereoassignment) | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_3 | isotropic | sample_conditions_1 |
| 1D 1H-15N T1 | sample_3 | isotropic | sample_conditions_1 |
| 1D 1H-15N T2 | sample_3 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom) | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.0, Bruker Biospin - collection
AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.113, Goddard - data analysis, peak picking
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF validation
PSVS v1.3, Bhattacharya and Montelione - structure validation
PDBStat v5.0, Tejero and Montelione - PDB analysis
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAG12480 BAG80618 BAK28458 GAD37696 |
| EMBL | CAQ49394 CAR69097 CAV31171 CAZ51616 CAZ55327 |
| GB | AAB60011 AAM99819 AAY63928 ABP89898 ABP92096 |
| PRF | 2114402C |
| REF | NP_687947 WP_000985015 WP_001234286 WP_002843320 WP_016397616 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts