BMRB Entry 19942
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19942
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution structure of the terminal Ig-like domain from Leptospira interrogans LigB PubMed: 25068811
Deposition date: 2014-04-25 Original release date: 2014-08-26
Authors: Ptak, Christopher; Hsieh, Ching-Lin; Lin, Yi-Pin; Maltsev, Alexander; Raman, Rajeev; Sharma, Yogendra; Oswald, Robert; Chang, Yung-Fu
Citation: Ptak, Christopher; Hsieh, Ching-Lin; Lin, Yi-Pin; Maltsev, Alexander; Raman, Rajeev; Sharma, Yogendra; Oswald, Robert; Chang, Yung-Fu. "The NMR solution structure of the terminal immunoglobulin-like domain from the Leptospira host-interacting outer membrane protein, LigB" Biochemistry 53, 5249-5260 (2014).
Assembly members:
entity, polymer, 95 residues, 9641.579 Da.
Natural source: Common Name: Leptospira Interrogans Taxonomy ID: 173 Superkingdom: Bacteria Kingdom: not available Genus/species: Leptospira Interrogans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28-His-Sumo
Entity Sequences (FASTA):
entity: SAATLSSISISPINTNINTT
VSKQFFAVGTYSDGTKADLT
SSVTWSSSNQSQAKVSNASE
TKGLVTGIASGNPTIIATYG
SVSGNTILTVNKTDT
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 561 |
| 13C chemical shifts | 368 |
| 15N chemical shifts | 91 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 95 residues - 9641.579 Da.
| 1 | SER | ALA | ALA | THR | LEU | SER | SER | ILE | SER | ILE | ||||
| 2 | SER | PRO | ILE | ASN | THR | ASN | ILE | ASN | THR | THR | ||||
| 3 | VAL | SER | LYS | GLN | PHE | PHE | ALA | VAL | GLY | THR | ||||
| 4 | TYR | SER | ASP | GLY | THR | LYS | ALA | ASP | LEU | THR | ||||
| 5 | SER | SER | VAL | THR | TRP | SER | SER | SER | ASN | GLN | ||||
| 6 | SER | GLN | ALA | LYS | VAL | SER | ASN | ALA | SER | GLU | ||||
| 7 | THR | LYS | GLY | LEU | VAL | THR | GLY | ILE | ALA | SER | ||||
| 8 | GLY | ASN | PRO | THR | ILE | ILE | ALA | THR | TYR | GLY | ||||
| 9 | SER | VAL | SER | GLY | ASN | THR | ILE | LEU | THR | VAL | ||||
| 10 | ASN | LYS | THR | ASP | THR |
Samples:
sample_1: Protein, [U-95% 13C; U-95% 15N], 0.5 mM; sodium chloride 137 mM; sodium phosphate 10 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM
sample_2: Protein, [U-95% 15N], 0.5 mM; sodium chloride 137 mM; sodium phosphate 10 mM; potassium chloride 2.7 mM; potassium phosphate 1.8 mM
sample_conditions_1: temperature: 286 K; pH: 7; pressure: 1 atm; ionic strength: 0.15 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCOCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCBCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D CCONH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCONH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMR, Varian - collection
NMR spectrometers:
- Varian INOVA 500 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts