BMRB Entry 17575
Click here to enlarge.
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/BMR17575
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: solution structure of the C domain of Rv0899 from mycobacterium tuberculosis PubMed: 22206986
Deposition date: 2011-04-06 Original release date: 2012-01-04
Authors: Yao, Yong; Marassi, Francesca
Citation: Yao, Yong; Barghava, Neha; Kim, Johnny; Niederweis, Michael; Marassi, Francesca. "Molecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899)." J. Mol. Biol. 416, 208-220 (2012).
Assembly members:
entity, polymer, 137 residues, 14052.831 Da.
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):
entity: GQAPPGPPASGPCADLQSAI
NAVTGGPIAFGNDGASLIPA
AYEILNRVADKLKACPDARV
TINGYTDNTGSEGINIPLSA
QRAKIVADYLVARGVAGDHI
ATVGLGSVNPIASNATPEGR
AKNRRVEIVVNHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 350 |
| 15N chemical shifts | 129 |
| 1H chemical shifts | 795 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | C domain of Rv0899 | 1 |
Entities:
Entity 1, C domain of Rv0899 137 residues - 14052.831 Da.
| 1 | GLY | GLN | ALA | PRO | PRO | GLY | PRO | PRO | ALA | SER | ||||
| 2 | GLY | PRO | CYS | ALA | ASP | LEU | GLN | SER | ALA | ILE | ||||
| 3 | ASN | ALA | VAL | THR | GLY | GLY | PRO | ILE | ALA | PHE | ||||
| 4 | GLY | ASN | ASP | GLY | ALA | SER | LEU | ILE | PRO | ALA | ||||
| 5 | ALA | TYR | GLU | ILE | LEU | ASN | ARG | VAL | ALA | ASP | ||||
| 6 | LYS | LEU | LYS | ALA | CYS | PRO | ASP | ALA | ARG | VAL | ||||
| 7 | THR | ILE | ASN | GLY | TYR | THR | ASP | ASN | THR | GLY | ||||
| 8 | SER | GLU | GLY | ILE | ASN | ILE | PRO | LEU | SER | ALA | ||||
| 9 | GLN | ARG | ALA | LYS | ILE | VAL | ALA | ASP | TYR | LEU | ||||
| 10 | VAL | ALA | ARG | GLY | VAL | ALA | GLY | ASP | HIS | ILE | ||||
| 11 | ALA | THR | VAL | GLY | LEU | GLY | SER | VAL | ASN | PRO | ||||
| 12 | ILE | ALA | SER | ASN | ALA | THR | PRO | GLU | GLY | ARG | ||||
| 13 | ALA | LYS | ASN | ARG | ARG | VAL | GLU | ILE | VAL | VAL | ||||
| 14 | ASN | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-99% 13C; U-99% 15N], 0.5 mM; D2O 10%; H2O 90%
sample_conditions_1: pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 600 MHz
Related Database Links:
| BMRB | 16237 17863 |
| 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