BMRB Entry 15320
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15320
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Wu, Yibing; Parish, David; Singarapu, Kiran kumar; Sukumaran, Dinesh; Eletski, Alex; Shastry, Ritu; Nwosu, Chioma; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas. "Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36" .
Assembly members:
UPF0350 protein VC_2471, polymer, 94 residues, 10938.577 Da.
Natural source: Common Name: not available Taxonomy ID: 666 Superkingdom: Bacteria Kingdom: not available Genus/species: Vibrio cholerae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: BL21(DE3)+ Magic
Entity Sequences (FASTA):
UPF0350 protein VC_2471: MYTAEQKARIKWACRRGMLE
LDVVIMPFFEECFDSLTESE
QDDFVALLESDDPDLFAWVM
GHGRCENLGLAAMVDKIVAH
NLSKVRLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 324 |
| 15N chemical shifts | 98 |
| 1H chemical shifts | 657 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | UPF0350 protein VC_2471 | 1 |
Entities:
Entity 1, UPF0350 protein VC_2471 94 residues - 10938.577 Da.
| 1 | MET | TYR | THR | ALA | GLU | GLN | LYS | ALA | ARG | ILE | ||||
| 2 | LYS | TRP | ALA | CYS | ARG | ARG | GLY | MET | LEU | GLU | ||||
| 3 | LEU | ASP | VAL | VAL | ILE | MET | PRO | PHE | PHE | GLU | ||||
| 4 | GLU | CYS | PHE | ASP | SER | LEU | THR | GLU | SER | GLU | ||||
| 5 | GLN | ASP | ASP | PHE | VAL | ALA | LEU | LEU | GLU | SER | ||||
| 6 | ASP | ASP | PRO | ASP | LEU | PHE | ALA | TRP | VAL | MET | ||||
| 7 | GLY | HIS | GLY | ARG | CYS | GLU | ASN | LEU | GLY | LEU | ||||
| 8 | ALA | ALA | MET | VAL | ASP | LYS | ILE | VAL | ALA | HIS | ||||
| 9 | ASN | LEU | SER | LYS | VAL | ARG | LEU | GLU | HIS | HIS | ||||
| 10 | HIS | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.2 mM
sample_2: entity, [U-5% 13C; U-100% 15N], 1.1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 4,3D, GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 4,3D, GFT CABCACONNH | sample_1 | isotropic | sample_conditions_1 |
| 4,3D, GFT HCCH COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D, 15N-13C RESOLVEDSIMULTANIOUS NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
Software:
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
AutoStruct, Huang, Tejero, Powers and Montelione - structure solution
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
XEASY, Bartels et al. - peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks