BMRB Entry 16238
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/BMR16238
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 NMR structure of VC_A0919 from Vibrio cholerae. Northeast Structural Genomics Consortium Target VcR52.
Deposition date: 2009-04-02 Original release date: 2009-05-07
Authors: Ramelot, Theresa; Cort, John; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Liu, Jinfeng; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Cort, John; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Liu, Jinfeng; Rost, Burkhard; Swapna, G.V.T.; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of VC_A0919 from Vibrio cholerae. Northeast Structural Genomics Consortium Target VcR52." Not known ., .-..
Assembly members:
VC_A0919, polymer, 108 residues, 12000 Da.
Natural source: Common Name: Vibrio cholerae Taxonomy ID: 666 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio cholerae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
VC_A0919: MSNQTCVENEVCEACGCAGE
IGFIIREGDDVAEVSLFGSD
KAHLEGKLAEYISLAKQVYA
NVEYEVAPVADNATELHARF
KFEVSAEKLIFELKTRALAR
LEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 437 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 692 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | VC_A0919 | 1 |
Entities:
Entity 1, VC_A0919 108 residues - 12000 Da.
8 non-native residues at C-teriminus (LEHHHHHH)
| 1 | MET | SER | ASN | GLN | THR | CYS | VAL | GLU | ASN | GLU | ||||
| 2 | VAL | CYS | GLU | ALA | CYS | GLY | CYS | ALA | GLY | GLU | ||||
| 3 | ILE | GLY | PHE | ILE | ILE | ARG | GLU | GLY | ASP | ASP | ||||
| 4 | VAL | ALA | GLU | VAL | SER | LEU | PHE | GLY | SER | ASP | ||||
| 5 | LYS | ALA | HIS | LEU | GLU | GLY | LYS | LEU | ALA | GLU | ||||
| 6 | TYR | ILE | SER | LEU | ALA | LYS | GLN | VAL | TYR | ALA | ||||
| 7 | ASN | VAL | GLU | TYR | GLU | VAL | ALA | PRO | VAL | ALA | ||||
| 8 | ASP | ASN | ALA | THR | GLU | LEU | HIS | ALA | ARG | PHE | ||||
| 9 | LYS | PHE | GLU | VAL | SER | ALA | GLU | LYS | LEU | ILE | ||||
| 10 | PHE | GLU | LEU | LYS | THR | ARG | ALA | LEU | ALA | ARG | ||||
| 11 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 mM; protein, [U-100% 13C; U-100% 15N], 0.5 ± 0.05 mM
NC5_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± 0.25 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 mM; protein, [U-5% 13C; U-100% 15N], 0.5 ± 0.05 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | NC_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliph) | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCA | NC_sample | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | NC5_sample | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (arom) | NC_sample | isotropic | sample_conditions_1 |
Software:
NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
TOPSPIN v2.1.3, Bruker Biospin - collection
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution
SPARKY v3.113, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis
NMR spectrometers:
- Varian INOVA 600 MHz
- Varian INOVA 750 MHz
- Bruker AvanceIII 850 MHz
Related Database Links:
| PDB | |
| DBJ | BAP05215 |
| EMBL | CFW12101 CPR24259 CPR24260 CQB51070 CRZ40211 |
| GB | AAF96816 ABQ19183 ACP07838 ACP11775 ACQ62378 |
| REF | NP_233304 WP_000070924 WP_000070925 WP_000070926 WP_000070927 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts