BMRB Entry 19433
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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/BMR19433
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Title: NMR structure of the protein YP_002937094.1 from Eubacterium rectale
Deposition date: 2013-08-19 Original release date: 2013-09-03
Authors: Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Dutta, Samit; 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, 103 residues, 11358.535 Da.
Natural source: Common Name: Eubacterium rectale Taxonomy ID: 39491 Superkingdom: Bacteria Kingdom: not available Genus/species: Eubacterium rectale
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: GAQDGKETTTIRLINQTYFN
VKNIKVTWNDGKEQTVNTLG
SHDSIDFSSDAGSVYKMDVT
GTTQSGEKFTGHFKGLVGKD
TRVFIELDENADVQVFIPQG
EID
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 339 |
| 15N chemical shifts | 112 |
| 1H chemical shifts | 693 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_002937094.1 | 1 |
Entities:
Entity 1, YP_002937094.1 103 residues - 11358.535 Da.
| 1 | GLY | ALA | GLN | ASP | GLY | LYS | GLU | THR | THR | THR | ||||
| 2 | ILE | ARG | LEU | ILE | ASN | GLN | THR | TYR | PHE | ASN | ||||
| 3 | VAL | LYS | ASN | ILE | LYS | VAL | THR | TRP | ASN | ASP | ||||
| 4 | GLY | LYS | GLU | GLN | THR | VAL | ASN | THR | LEU | GLY | ||||
| 5 | SER | HIS | ASP | SER | ILE | ASP | PHE | SER | SER | ASP | ||||
| 6 | ALA | GLY | SER | VAL | TYR | LYS | MET | ASP | VAL | THR | ||||
| 7 | GLY | THR | THR | GLN | SER | GLY | GLU | LYS | PHE | THR | ||||
| 8 | GLY | HIS | PHE | LYS | GLY | LEU | VAL | GLY | LYS | ASP | ||||
| 9 | THR | ARG | VAL | PHE | ILE | GLU | LEU | ASP | GLU | ASN | ||||
| 10 | ALA | ASP | VAL | GLN | VAL | PHE | ILE | PRO | GLN | GLY | ||||
| 11 | GLU | ILE | ASP |
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; H20 95%; D2O 5%
sample_conditions_1: ionic strength: 0.220 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 |
| 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, Guntert, Mumenthaler and Wuthrich - refinement
UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN, Bruker Biospin - collection, processing
Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CBK93813 CDC69040 CUN23035 CUN83241 |
| GB | ACR74960 |
| REF | WP_012742060 WP_055223681 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts