BMRB Entry 25294
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/BMR25294
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: NMR structure of the protein NP_809137.1 from Bacteroides thetaiotaomicron
Deposition date: 2014-10-27 Original release date: 2014-11-10
Authors: Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale" Not known ., .-..
Assembly members:
entity, polymer, 118 residues, 13189.811 Da.
Natural source: Common Name: CFB group bacteria Taxonomy ID: 818 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides thetaiotaomicron
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GCELSDPDGLADPMKWSKVP
SGLKNGELKVEAEGGSSLFA
CKNYKSFWISSVKEEGKFKE
NTSYKEFDGGWYLVKIEDNE
LKVIINRNETNASRSFTVCV
EAGNAFDEFKFVQDAAKQ
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 762 |
| 13C chemical shifts | 384 |
| 15N chemical shifts | 124 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 118 residues - 13189.811 Da.
| 1 | GLY | CYS | GLU | LEU | SER | ASP | PRO | ASP | GLY | LEU | ||||
| 2 | ALA | ASP | PRO | MET | LYS | TRP | SER | LYS | VAL | PRO | ||||
| 3 | SER | GLY | LEU | LYS | ASN | GLY | GLU | LEU | LYS | VAL | ||||
| 4 | GLU | ALA | GLU | GLY | GLY | SER | SER | LEU | PHE | ALA | ||||
| 5 | CYS | LYS | ASN | TYR | LYS | SER | PHE | TRP | ILE | SER | ||||
| 6 | SER | VAL | LYS | GLU | GLU | GLY | LYS | PHE | LYS | GLU | ||||
| 7 | ASN | THR | SER | TYR | LYS | GLU | PHE | ASP | GLY | GLY | ||||
| 8 | TRP | TYR | LEU | VAL | LYS | ILE | GLU | ASP | ASN | GLU | ||||
| 9 | LEU | LYS | VAL | ILE | ILE | ASN | ARG | ASN | GLU | THR | ||||
| 10 | ASN | ALA | SER | ARG | SER | PHE | THR | VAL | CYS | VAL | ||||
| 11 | GLU | ALA | GLY | ASN | ALA | PHE | ASP | GLU | PHE | LYS | ||||
| 12 | PHE | VAL | GLN | ASP | ALA | ALA | LYS | GLN |
Samples:
sample_1: entity, [U-98% 13C; U-98% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; DTT, [U-99% 2H], 5 mM; H2O 95%; D2O 5%
sample_conditions_1: temperature: 298 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.220 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G ntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement
TOPSPIN, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment
UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution
MDDNMR, Maxim Mayzel, Vladislav Orekhov - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts