BMRB Entry 17318
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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/BMR17318
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Title: NMR solution structure of the protein YP_001092504.1
Deposition date: 2010-11-23 Original release date: 2010-12-16
Authors: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt
Citation: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt. "NMR solution structure of the protein YP_001092504.1" Not known ., .-..
Assembly members:
YP_001092504.1, polymer, 132 residues, 14833.001 Da.
Natural source: Common Name: Shewanella loihica PV-4 Taxonomy ID: 323850 Superkingdom: Bacteria Kingdom: not available Genus/species: Shewanella loihica
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
YP_001092504.1: GMTPQSDTPKVTGLKLKRKS
RQLEISFDNGQQFTLSCELL
RVYSPSAEVHGHGNPVLVTH
KKNVNINAITPVGNYAVKLV
FDDGHDTGLYSWKVLYDLAS
NQVDLWENYLARLRAAKASR
EPLIDMAVKYHT
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 933 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | YP_001092504.1 | 1 |
Entities:
Entity 1, YP_001092504.1 132 residues - 14833.001 Da.
| 1 | GLY | MET | THR | PRO | GLN | SER | ASP | THR | PRO | LYS | ||||
| 2 | VAL | THR | GLY | LEU | LYS | LEU | LYS | ARG | LYS | SER | ||||
| 3 | ARG | GLN | LEU | GLU | ILE | SER | PHE | ASP | ASN | GLY | ||||
| 4 | GLN | GLN | PHE | THR | LEU | SER | CYS | GLU | LEU | LEU | ||||
| 5 | ARG | VAL | TYR | SER | PRO | SER | ALA | GLU | VAL | HIS | ||||
| 6 | GLY | HIS | GLY | ASN | PRO | VAL | LEU | VAL | THR | HIS | ||||
| 7 | LYS | LYS | ASN | VAL | ASN | ILE | ASN | ALA | ILE | THR | ||||
| 8 | PRO | VAL | GLY | ASN | TYR | ALA | VAL | LYS | LEU | VAL | ||||
| 9 | PHE | ASP | ASP | GLY | HIS | ASP | THR | GLY | LEU | TYR | ||||
| 10 | SER | TRP | LYS | VAL | LEU | TYR | ASP | LEU | ALA | SER | ||||
| 11 | ASN | GLN | VAL | ASP | LEU | TRP | GLU | ASN | TYR | LEU | ||||
| 12 | ALA | ARG | LEU | ARG | ALA | ALA | LYS | ALA | SER | ARG | ||||
| 13 | GLU | PRO | LEU | ILE | ASP | MET | ALA | VAL | LYS | TYR | ||||
| 14 | HIS | THR |
Samples:
sample_1: sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; Protein-YP_001092504.1, [U-98% 13C; U-98% 15N], 1.2 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 0.113 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 |
| 2D 1H-13C 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 |
| 15N resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13Cali resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 13Caro resolved [1H,1H]-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 15 N {1H} - NOE | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation
UNIO v2.0.1, Herrmann and Wuthrich - structure solution
OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - energy refinement
CARA, Keller and Wuthrich - chemical shift assignment
TOPSPIN v1.3, Bruker Biospin - Acquisition, data analysis, processing
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts