BMRB Entry 19507
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19507
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Title: Backbone assignment and Secondary Structure of Intrinsically Unstructured Culture Filtrate Antigen protein (CFP10) from Mycobacterium Tuberculosis
Deposition date: 2013-09-19 Original release date: 2013-11-11
Authors: Pandey, Himanshu; Guleria, Anupam; Raikwal, Nisha; Arora, Ashish; Kumar, Dinesh
Citation: Guleria, Anupam; Raikwal, Nisha; Shukla, Vaibhav; Pandey, Himanshu; Arora, Ashish; Kumar, Dinesh. "Pseudo 5D HN(C)N Experiment to Facilitate the Assignment of Backbone Resonances in Proteins Exhibiting High Backbone Shift Degeneracy" Not known ., .-..
Assembly members:
CFP10, polymer, 113 residues, Formula weight is not available
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CFP10: MAEMKTDAATLAQEAGNFER
ISGDLKTQIDQVESTAGSLQ
GQWRGAAGTAAQAAVVRFQE
AANKQKQELDEISTNIRQAG
VQYSRADEEQQQALSSQMGF
KLAAALEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 317 |
| 15N chemical shifts | 109 |
| 1H chemical shifts | 109 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CFP10 Monomer | 1 |
Entities:
Entity 1, CFP10 Monomer 113 residues - Formula weight is not available
| 1 | MET | ALA | GLU | MET | LYS | THR | ASP | ALA | ALA | THR | ||||
| 2 | LEU | ALA | GLN | GLU | ALA | GLY | ASN | PHE | GLU | ARG | ||||
| 3 | ILE | SER | GLY | ASP | LEU | LYS | THR | GLN | ILE | ASP | ||||
| 4 | GLN | VAL | GLU | SER | THR | ALA | GLY | SER | LEU | GLN | ||||
| 5 | GLY | GLN | TRP | ARG | GLY | ALA | ALA | GLY | THR | ALA | ||||
| 6 | ALA | GLN | ALA | ALA | VAL | VAL | ARG | PHE | GLN | GLU | ||||
| 7 | ALA | ALA | ASN | LYS | GLN | LYS | GLN | GLU | LEU | ASP | ||||
| 8 | GLU | ILE | SER | THR | ASN | ILE | ARG | GLN | ALA | GLY | ||||
| 9 | VAL | GLN | TYR | SER | ARG | ALA | ASP | GLU | GLU | GLN | ||||
| 10 | GLN | GLN | ALA | LEU | SER | SER | GLN | MET | GLY | PHE | ||||
| 11 | LYS | LEU | ALA | ALA | ALA | LEU | GLU | HIS | HIS | HIS | ||||
| 12 | HIS | HIS | HIS |
Samples:
sample_1: CFP10, [U-13C; U-15N], 0.8 – 1.0 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 290 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D hNCAnH | sample_1 | isotropic | sample_conditions_1 |
| reduced dimensionality (4,3)-hnCOCANH | sample_1 | isotropic | sample_conditions_1 |
| Pseudo 5D HN(C)N | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.0, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAL68012 BAQ08111 GAA43756 |
| EMBL | CCC28957 CCC46227 CCE39297 CCG13791 CCK53890 |
| GB | AAC83445 AAK48356 AAL14999 ABQ75702 ABR08234 |
| REF | NP_218391 NP_857541 WP_003399940 WP_003900771 WP_009937166 |
| SP | P0A567 P9WNK4 P9WNK5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts