BMRB Entry 25032
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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/BMR25032
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Title: Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira
Deposition date: 2014-06-19 Original release date: 2014-07-14
Authors: Mei, Song
Citation: Mei, Song. "Solution structure of a bacterial immunoglobulin-like domain form a surface protein of Leptospira" Not known ., .-..
Assembly members:
entity, polymer, 102 residues, 10426.439 Da.
Natural source: Common Name: spirochetes Taxonomy ID: 44276 Superkingdom: Bacteria Kingdom: not available Genus/species: Leptospira interrogans
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: ENIDITVSAATLSSISISPI
NTNINTTVSKQFFAVGTYSD
GTKADLTSSVTWSSSNQSQA
KVSNASETKGLVTGIASGNP
TIIATYGSVSGNTILTVNKT
DT
- assigned_chemical_shifts
Data type | Count |
1H chemical shifts | 487 |
13C chemical shifts | 193 |
15N chemical shifts | 108 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | surface protein of Leptospira | 1 |
Entities:
Entity 1, surface protein of Leptospira 102 residues - 10426.439 Da.
1 | GLU | ASN | ILE | ASP | ILE | THR | VAL | SER | ALA | ALA | ||||
2 | THR | LEU | SER | SER | ILE | SER | ILE | SER | PRO | ILE | ||||
3 | ASN | THR | ASN | ILE | ASN | THR | THR | VAL | SER | LYS | ||||
4 | GLN | PHE | PHE | ALA | VAL | GLY | THR | TYR | SER | ASP | ||||
5 | GLY | THR | LYS | ALA | ASP | LEU | THR | SER | SER | VAL | ||||
6 | THR | TRP | SER | SER | SER | ASN | GLN | SER | GLN | ALA | ||||
7 | LYS | VAL | SER | ASN | ALA | SER | GLU | THR | LYS | GLY | ||||
8 | LEU | VAL | THR | GLY | ILE | ALA | SER | GLY | ASN | PRO | ||||
9 | THR | ILE | ILE | ALA | THR | TYR | GLY | SER | VAL | SER | ||||
10 | GLY | ASN | THR | ILE | LEU | THR | VAL | ASN | LYS | THR | ||||
11 | ASP | THR |
Samples:
sample_1: H2O 90%; D2O 10%
sample_conditions_1: temperature: 293 K; pH: 6.5; pressure: 1 atm; ionic strength: 100 mM
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker AMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts