BMRB Entry 25027
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25027
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Title: NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482
Deposition date: 2014-06-18 Original release date: 2014-09-02
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482" Not known ., .-..
Assembly members:
entity, polymer, 105 residues, 11296.354 Da.
Natural source: Common Name: CFB group bacteria Taxonomy ID: 435590 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides vulgatus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GHMGSPVSYYFSYADGGTSH
TEYPDDSSAGSFILDITSYK
KTGNSTKALSWNASGDSWIH
VNGSSVSYDENPAKERRTGL
VTLKQDESGKTLSLKIVQPG
KTSID
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 654 |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 107 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 105 residues - 11296.354 Da.
| 1 | GLY | HIS | MET | GLY | SER | PRO | VAL | SER | TYR | TYR | ||||
| 2 | PHE | SER | TYR | ALA | ASP | GLY | GLY | THR | SER | HIS | ||||
| 3 | THR | GLU | TYR | PRO | ASP | ASP | SER | SER | ALA | GLY | ||||
| 4 | SER | PHE | ILE | LEU | ASP | ILE | THR | SER | TYR | LYS | ||||
| 5 | LYS | THR | GLY | ASN | SER | THR | LYS | ALA | LEU | SER | ||||
| 6 | TRP | ASN | ALA | SER | GLY | ASP | SER | TRP | ILE | HIS | ||||
| 7 | VAL | ASN | GLY | SER | SER | VAL | SER | TYR | ASP | GLU | ||||
| 8 | ASN | PRO | ALA | LYS | GLU | ARG | ARG | THR | GLY | LEU | ||||
| 9 | VAL | THR | LEU | LYS | GLN | ASP | GLU | SER | GLY | LYS | ||||
| 10 | THR | LEU | SER | LEU | LYS | ILE | VAL | GLN | PRO | GLY | ||||
| 11 | LYS | THR | SER | ILE | ASP |
Samples:
sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: temperature: 308 K; pH: 6.0; pressure: 1 atm; ionic strength: 0.0798 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| APSY 4D-HACANH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| APSY 5D-CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | 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 |
Software:
CYANA, G ntert P., Luginbuhl, Guntert, Billeter and Wuthrich - refinement, geometry optimization
TOPSPIN v3.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - data analysis, chemical shift assignment
j-UNIO, Herrmann, Guntert and Wuthrich - peak picking, chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| UNP | A6KYV6_BACV8 |
| PDB | |
| EMBL | CUN71160 CUP76619 |
| GB | ABR38620 EGX27430 |
| REF | WP_008670674 WP_011964947 WP_057249593 WP_057279461 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts