BMRB Entry 15678
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15678
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: Chemical Shift assignment of SeR13 from Staphylococcus Epidermidis, North East Structural Genomics Consortium Target SeR13 PubMed: 20589905
Deposition date: 2008-03-05 Original release date: 2008-03-17
Authors: Lee, Hsiau-Wei; Wylie, Greg; Bansal, Sonal; Wang, Xu; Shastry, Ritu; Jiang, Mei; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, GVT; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Prestegard, James
Citation: Lee, Hsiau-Wei; Wylie, Greg; Bansal, Sonal; Wang, Xu; Barb, Adam; Macnaughtan, Megan; Ertekin, Asli; Montelione, Gaetano; Prestegard, James. "Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping." Protein Sci. 19, 1673-1685 (2010).
Assembly members:
SeR13, polymer, 94 residues, 10138.311 Da.
Natural source: Common Name: Staphylococcus epidermidis Taxonomy ID: 1282 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus epidermidis
Experimental source: Production method: recombinant technology Host organism: Staphylococcus epidermidis
Entity Sequences (FASTA):
SeR13: MEIIAISETPNHNTMKVSLS
EPRQDNSFTTYTAAQEGQPE
FINRLFEIEGVKSIFYVLDF
ISIDKEDNANWNELLPQIEN
TFAKSNLEHHHHHH
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 13C chemical shifts | 345 |
| 15N chemical shifts | 85 |
| 1H chemical shifts | 494 |
| residual dipolar couplings | 106 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SeR13 | 1 |
Entities:
Entity 1, SeR13 94 residues - 10138.311 Da.
LEHHHHHH are at the C-terminal as part of His-Tag
| 1 | MET | GLU | ILE | ILE | ALA | ILE | SER | GLU | THR | PRO | ||||
| 2 | ASN | HIS | ASN | THR | MET | LYS | VAL | SER | LEU | SER | ||||
| 3 | GLU | PRO | ARG | GLN | ASP | ASN | SER | PHE | THR | THR | ||||
| 4 | TYR | THR | ALA | ALA | GLN | GLU | GLY | GLN | PRO | GLU | ||||
| 5 | PHE | ILE | ASN | ARG | LEU | PHE | GLU | ILE | GLU | GLY | ||||
| 6 | VAL | LYS | SER | ILE | PHE | TYR | VAL | LEU | ASP | PHE | ||||
| 7 | ILE | SER | ILE | ASP | LYS | GLU | ASP | ASN | ALA | ASN | ||||
| 8 | TRP | ASN | GLU | LEU | LEU | PRO | GLN | ILE | GLU | ASN | ||||
| 9 | THR | PHE | ALA | LYS | SER | ASN | LEU | GLU | HIS | HIS | ||||
| 10 | HIS | HIS | HIS | HIS |
Samples:
sample_1: SeR13, [U-100% 13C; U-100% 15N], 1.07 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM
GEL_s: SeR13, [U-100% 13C; U-100% 15N], 0.86 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM; Negative Charged Poly Acrylamide Compressed Gel 7%
Bicelle_s: SeR13, [U-100% 13C; U-100% 15N], 0.60 mM; sodium azide 0.2%; DTT 100 mM; CaCl2 5 mM; sodium chloride 100 mM; MES 20 mM; DMPS/DHPC Mixture 7.5%
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-TROSY | GEL_s | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC-TROSY | Bicelle_s | anisotropic | sample_conditions_1 |
Software:
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement
SPARKY, Goddard - chemical shift assignment
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| EMBL | CDM13704 |
| GB | AAO04721 AAW54376 AIR82327 AJP24693 EES36166 |
| REF | NP_764679 WP_001831110 WP_002489988 WP_002493609 WP_047500344 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts