BMRB Entry 18364
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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/BMR18364
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Title: NMR structure of the protein YP_001300941.1 from Bacteroides vulgatus
Deposition date: 2012-03-29 Original release date: 2012-04-30
Authors: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt; JCSG, JCSG
Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of the protein YP_001300941.1 from Bacteroides vulgatus" .
Assembly members:
GS13500A, polymer, 126 residues, 13488.005 Da.
Natural source: Common Name: Bacteroides vulgates Taxonomy ID: 821 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacteroides vulgates
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: SpeedET
Entity Sequences (FASTA):
GS13500A: GASDFQTGIHKIVIQQSGDT
DSFEVSVSIGGADKGGPAKL
YNDKGEYIGDSYSAQIRTAT
MSCCTNGNAFFMTCAGSVSS
ISEAGKRLHITVIGYIDDKE
VNRLEKEYITDGNTLIETFS
VSTKEI
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 395 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 790 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | GS13500A | 1 |
Entities:
Entity 1, GS13500A 126 residues - 13488.005 Da.
| 1 | GLY | ALA | SER | ASP | PHE | GLN | THR | GLY | ILE | HIS | ||||
| 2 | LYS | ILE | VAL | ILE | GLN | GLN | SER | GLY | ASP | THR | ||||
| 3 | ASP | SER | PHE | GLU | VAL | SER | VAL | SER | ILE | GLY | ||||
| 4 | GLY | ALA | ASP | LYS | GLY | GLY | PRO | ALA | LYS | LEU | ||||
| 5 | TYR | ASN | ASP | LYS | GLY | GLU | TYR | ILE | GLY | ASP | ||||
| 6 | SER | TYR | SER | ALA | GLN | ILE | ARG | THR | ALA | THR | ||||
| 7 | MET | SER | CYS | CYS | THR | ASN | GLY | ASN | ALA | PHE | ||||
| 8 | PHE | MET | THR | CYS | ALA | GLY | SER | VAL | SER | SER | ||||
| 9 | ILE | SER | GLU | ALA | GLY | LYS | ARG | LEU | HIS | ILE | ||||
| 10 | THR | VAL | ILE | GLY | TYR | ILE | ASP | ASP | LYS | GLU | ||||
| 11 | VAL | ASN | ARG | LEU | GLU | LYS | GLU | TYR | ILE | THR | ||||
| 12 | ASP | GLY | ASN | THR | LEU | ILE | GLU | THR | PHE | SER | ||||
| 13 | VAL | SER | THR | LYS | GLU | ILE |
Samples:
sample_1: GS13500A, [U-98% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; H2O 95 mM; D2O, [U-99% 2H], 5 mM
sample_conditions_1: ionic strength: 0.08 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 4D APSY-HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-HACACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY-CBCACONH | 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:
TOPSPIN v2.1, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
UNIO, (Unio)-Herrmann and Wuthrich - chemical shift assignment, structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CBW24855 CUO17365 CUQ42974 |
| GB | ABR41319 ALK85811 EES67826 EFI05346 EFI12350 |
| REF | WP_005805239 WP_005823213 WP_008640853 WP_008766551 WP_009040585 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts