BMRB Entry 17381
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17381
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for a putative surface protein
Deposition date: 2010-12-24 Original release date: 2012-02-29
Authors: Wang, Tao
Citation: Wang, Tao. "1H and 15N Assigned Chemical Shifts for a putative surface protein" Not known ., .-..
Assembly members:
putative_surface_protein, polymer, 97 residues, Formula weight is not available
Natural source: Common Name: Streptococcus pneumoniae Taxonomy ID: 1313 Superkingdom: Bacteria Kingdom: not available Genus/species: Streptococcus pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
putative_surface_protein: SPKTILGIEVSQEPKKDYLV
GDSLDLSEGRFAVAYSNDTM
EEHSFTDEGVEISGYDAQKT
GRQTLTLHYQGHEVSFDVLV
SPKAALNDELEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 228 |
| 15N chemical shifts | 84 |
| 1H chemical shifts | 471 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | putative surface protein | 1 |
Entities:
Entity 1, putative surface protein 97 residues - Formula weight is not available
| 1 | SER | PRO | LYS | THR | ILE | LEU | GLY | ILE | GLU | VAL | ||||
| 2 | SER | GLN | GLU | PRO | LYS | LYS | ASP | TYR | LEU | VAL | ||||
| 3 | GLY | ASP | SER | LEU | ASP | LEU | SER | GLU | GLY | ARG | ||||
| 4 | PHE | ALA | VAL | ALA | TYR | SER | ASN | ASP | THR | MET | ||||
| 5 | GLU | GLU | HIS | SER | PHE | THR | ASP | GLU | GLY | VAL | ||||
| 6 | GLU | ILE | SER | GLY | TYR | ASP | ALA | GLN | LYS | THR | ||||
| 7 | GLY | ARG | GLN | THR | LEU | THR | LEU | HIS | TYR | GLN | ||||
| 8 | GLY | HIS | GLU | VAL | SER | PHE | ASP | VAL | LEU | VAL | ||||
| 9 | SER | PRO | LYS | ALA | ALA | LEU | ASN | ASP | GLU | LEU | ||||
| 10 | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: putative surface protein, [U-99% 13C; U-99% 15N], 0.7 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; 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 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(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 H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DMX 500 MHz
Related Database Links:
| PDB | |
| EMBL | CEX10252 CIR31810 CIV87805 CKF09277 CKH75363 |
| GB | EHD61255 EJG57305 |
| REF | WP_055387523 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts