BMRB Entry 17863
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR17863
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Title: Rv0899 from Mycobacterium tuberculosis contains two seperated domains PubMed: 22108166
Deposition date: 2011-08-14 Original release date: 2011-09-02
Authors: Shi, Chaowei; Li, Juan; Gao, Yuan; Wu, Kaiqi; Huang, Hongda; Tian, Changlin
Citation: Li, Juan; Shi, Chaowei; Gao, Yuan; Wu, Kaiqi; Shi, Pan; Lai, Chaohua; Chen, Liu; Wu, Fangming; Tian, Changlin. "Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal a Monomeric Membrane-Anchoring Protein with Two Separate Domains." J. Mol. Biol. 415, 382-392 (2012).
Assembly members:
Rv0899, polymer, 284 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):
Rv0899: MRPQSVTGPTGVLPTLTPTS
TRGASALSLSLLSISRSGNT
VTLIGDFPDEAAKAALMTAL
NGLLAPGVNVIDQIHVDPVV
RSLDFSSAEPVFTASVPIPD
FGLKVERDTVTLTGTAPSSE
HKDAVKRAATSTWPDMKIVN
NIEVTGQAPPGPPASGPCAD
LQSAINAVTGGPIAFGNDGA
SLIPADYEILNRVADKLKAC
PDARVTINGYTDNTGSEGIN
IPLSAQRAKIVADYLVARGV
AGDHIATVGLGSVNPIASNA
TPEGRAKNRRVEIVVNLEHH
HHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 919 |
| 15N chemical shifts | 218 |
| 1H chemical shifts | 1304 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rv0899 | 1 |
Entities:
Entity 1, Rv0899 284 residues - Formula weight is not available
| 1 | MET | ARG | PRO | GLN | SER | VAL | THR | GLY | PRO | THR | ||||
| 2 | GLY | VAL | LEU | PRO | THR | LEU | THR | PRO | THR | SER | ||||
| 3 | THR | ARG | GLY | ALA | SER | ALA | LEU | SER | LEU | SER | ||||
| 4 | LEU | LEU | SER | ILE | SER | ARG | SER | GLY | ASN | THR | ||||
| 5 | VAL | THR | LEU | ILE | GLY | ASP | PHE | PRO | ASP | GLU | ||||
| 6 | ALA | ALA | LYS | ALA | ALA | LEU | MET | THR | ALA | LEU | ||||
| 7 | ASN | GLY | LEU | LEU | ALA | PRO | GLY | VAL | ASN | VAL | ||||
| 8 | ILE | ASP | GLN | ILE | HIS | VAL | ASP | PRO | VAL | VAL | ||||
| 9 | ARG | SER | LEU | ASP | PHE | SER | SER | ALA | GLU | PRO | ||||
| 10 | VAL | PHE | THR | ALA | SER | VAL | PRO | ILE | PRO | ASP | ||||
| 11 | PHE | GLY | LEU | LYS | VAL | GLU | ARG | ASP | THR | VAL | ||||
| 12 | THR | LEU | THR | GLY | THR | ALA | PRO | SER | SER | GLU | ||||
| 13 | HIS | LYS | ASP | ALA | VAL | LYS | ARG | ALA | ALA | THR | ||||
| 14 | SER | THR | TRP | PRO | ASP | MET | LYS | ILE | VAL | ASN | ||||
| 15 | ASN | ILE | GLU | VAL | THR | GLY | GLN | ALA | PRO | PRO | ||||
| 16 | GLY | PRO | PRO | ALA | SER | GLY | PRO | CYS | ALA | ASP | ||||
| 17 | LEU | GLN | SER | ALA | ILE | ASN | ALA | VAL | THR | GLY | ||||
| 18 | GLY | PRO | ILE | ALA | PHE | GLY | ASN | ASP | GLY | ALA | ||||
| 19 | SER | LEU | ILE | PRO | ALA | ASP | TYR | GLU | ILE | LEU | ||||
| 20 | ASN | ARG | VAL | ALA | ASP | LYS | LEU | LYS | ALA | CYS | ||||
| 21 | PRO | ASP | ALA | ARG | VAL | THR | ILE | ASN | GLY | TYR | ||||
| 22 | THR | ASP | ASN | THR | GLY | SER | GLU | GLY | ILE | ASN | ||||
| 23 | ILE | PRO | LEU | SER | ALA | GLN | ARG | ALA | LYS | ILE | ||||
| 24 | VAL | ALA | ASP | TYR | LEU | VAL | ALA | ARG | GLY | VAL | ||||
| 25 | ALA | GLY | ASP | HIS | ILE | ALA | THR | VAL | GLY | LEU | ||||
| 26 | GLY | SER | VAL | ASN | PRO | ILE | ALA | SER | ASN | ALA | ||||
| 27 | THR | PRO | GLU | GLY | ARG | ALA | LYS | ASN | ARG | ARG | ||||
| 28 | VAL | GLU | ILE | VAL | VAL | ASN | LEU | GLU | HIS | HIS | ||||
| 29 | HIS | HIS | HIS | HIS |
Samples:
sample_1: Rv0899, [U-99% 13C; U-99% 15N], 0.5 – 1 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.05 M; pH: 6.5; pressure: 1 atm; temperature: 303 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HCACO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
NMRView, Johnson, One Moon Scientific - chemical shift assignment
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 500 MHz
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16237 |
| PDB | |
| DBJ | BAH25212 BAL64801 BAQ04819 GAA44658 |
| EMBL | CAL70937 CCC25980 CCC43237 CCC63509 CCE36433 |
| GB | AAK45169 ABI54278 ABQ72638 ABR05261 ACT26182 |
| REF | NP_215414 NP_854580 WP_003404684 WP_003915129 WP_014000491 |
| SP | A1KH31 P65594 P9WIU4 P9WIU5 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts