BMRB Entry 18047
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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/BMR18047
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Title: NMR structure of the protein NP_814968.1 from Enterococcus faecalis
Deposition date: 2011-11-08 Original release date: 2011-11-28
Authors: Susac, Lukas; Serrano, Pedro; Geralt, Michael; Mohanty, Biswarajan; JCSG, JCSG; Wuthrich, Kurt
Citation: Susac, Lukas; Serrano, Pedro; Geralt, Michael; Mohanty, Biswarajan; Wuthrich, Kurt. "NMR structure of the protein NP_814968.1 from Enterococcus faecalis" Not known ., .-..
Assembly members:
NP_814968.1, polymer, 143 residues, 16330.557 Da.
Natural source: Common Name: Enterococcus faecalis Taxonomy ID: 1351 Superkingdom: Bacteria Kingdom: not available Genus/species: Enterococcus faecalis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NP_814968.1: MDEVLATSIGTYENRTLLVP
DGRLALTALHKGKDYQGKPM
FYVLFELTNTTEKTQNIQLM
IQSFMEVSQTVHGKAQNLQY
AVLTDSPFQDKLDRLADEIN
PGETIQGAYPYEFINENKPV
HFKFRDRLLSLDEPIASEEI
TIT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 484 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 986 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NP_814968.1 | 1 |
Entities:
Entity 1, NP_814968.1 143 residues - 16330.557 Da.
| 1 | MET | ASP | GLU | VAL | LEU | ALA | THR | SER | ILE | GLY | ||||
| 2 | THR | TYR | GLU | ASN | ARG | THR | LEU | LEU | VAL | PRO | ||||
| 3 | ASP | GLY | ARG | LEU | ALA | LEU | THR | ALA | LEU | HIS | ||||
| 4 | LYS | GLY | LYS | ASP | TYR | GLN | GLY | LYS | PRO | MET | ||||
| 5 | PHE | TYR | VAL | LEU | PHE | GLU | LEU | THR | ASN | THR | ||||
| 6 | THR | GLU | LYS | THR | GLN | ASN | ILE | GLN | LEU | MET | ||||
| 7 | ILE | GLN | SER | PHE | MET | GLU | VAL | SER | GLN | THR | ||||
| 8 | VAL | HIS | GLY | LYS | ALA | GLN | ASN | LEU | GLN | TYR | ||||
| 9 | ALA | VAL | LEU | THR | ASP | SER | PRO | PHE | GLN | ASP | ||||
| 10 | LYS | LEU | ASP | ARG | LEU | ALA | ASP | GLU | ILE | ASN | ||||
| 11 | PRO | GLY | GLU | THR | ILE | GLN | GLY | ALA | TYR | PRO | ||||
| 12 | TYR | GLU | PHE | ILE | ASN | GLU | ASN | LYS | PRO | VAL | ||||
| 13 | HIS | PHE | LYS | PHE | ARG | ASP | ARG | LEU | LEU | SER | ||||
| 14 | LEU | ASP | GLU | PRO | ILE | ALA | SER | GLU | GLU | ILE | ||||
| 15 | THR | ILE | THR |
Samples:
sample_1: NP_814968.1, [U-95% 13C; U-95% 15N], 1.2 mM; sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 5 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.083 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-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 |
| 4D APSY HACANH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY CBCACONH | sample_1 | isotropic | sample_conditions_1 |
| 5D APSY HACACONH | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, G??ntert P. - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| EMBL | CBL31422 CCO72142 CPW23431 CRH64002 |
| GB | AAO81038 ADX79912 AEA93699 AFO43932 AHI40381 |
| REF | NP_814968 WP_002384665 WP_002395822 WP_002397838 WP_002419155 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts