BMRB Entry 16385
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16385
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Title: Solution NMR structure of the CARDB domain of PF1109 from Pyrococcus furiosus. Northeast Structural Genomics Consortium target PfR193A
Deposition date: 2009-06-30 Original release date: 2009-07-06
Authors: Aramini, James; Lee, Dong-Yup; Ciccosanti, Colleen; Hamilton, Keith; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, Gurla; Everett, John; Montelione, Gaetano
Citation: Aramini, James; Lee, Dong-Yup; Ciccosanti, Colleen; Hamilton, Keith; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Swapna, Gurla; Everett, John; Montelione, Gaetano. "Solution NMR structure of the CARDB domain of PF1109 from Pyrococcus furiosus." Not known ., .-..
Assembly members:
CARDB domain, polymer, 114 residues, 12868.545 Da.
Natural source: Common Name: Pyrococcus furiosus Taxonomy ID: 2261 Superkingdom: Archaea Kingdom: not available Genus/species: Pyrococcus furiosus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CARDB domain: MEFPDLTVEIKGPDVVGVNK
LAEYEVHVKNLGGIGVPSTK
VRVYINGTLYKNWTVSLGPK
EEKVLTFSWTPTQEGMYRIN
ATVDEENTVVELNENNNVAT
FDVSVVLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 498 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 788 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CARDB domain | 1 |
Entities:
Entity 1, CARDB domain 114 residues - 12868.545 Da.
Contains additional N-terminal Met and C-terminal LEHHHHHH affinity tag due to cloning.
| 1 | MET | GLU | PHE | PRO | ASP | LEU | THR | VAL | GLU | ILE | ||||
| 2 | LYS | GLY | PRO | ASP | VAL | VAL | GLY | VAL | ASN | LYS | ||||
| 3 | LEU | ALA | GLU | TYR | GLU | VAL | HIS | VAL | LYS | ASN | ||||
| 4 | LEU | GLY | GLY | ILE | GLY | VAL | PRO | SER | THR | LYS | ||||
| 5 | VAL | ARG | VAL | TYR | ILE | ASN | GLY | THR | LEU | TYR | ||||
| 6 | LYS | ASN | TRP | THR | VAL | SER | LEU | GLY | PRO | LYS | ||||
| 7 | GLU | GLU | LYS | VAL | LEU | THR | PHE | SER | TRP | THR | ||||
| 8 | PRO | THR | GLN | GLU | GLY | MET | TYR | ARG | ILE | ASN | ||||
| 9 | ALA | THR | VAL | ASP | GLU | GLU | ASN | THR | VAL | VAL | ||||
| 10 | GLU | LEU | ASN | GLU | ASN | ASN | ASN | VAL | ALA | THR | ||||
| 11 | PHE | ASP | VAL | SER | VAL | VAL | LEU | GLU | HIS | HIS | ||||
| 12 | HIS | HIS | HIS | HIS |
Samples:
sample_1: PfR193A, [U-100% 13C; U-100% 15N], 0.65 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; D2O 10%; H2O 90%
sample_2: PfR193A, [U-5% 13C; U-100% 15N], 0.43 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | 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 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC high resolution (L/V methyl stereoassignment) | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 3D CCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N hetNOE | sample_1 | isotropic | sample_conditions_1 |
| 1D 15N T1 and T2 | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v2.1, Bruker Biospin - collection, data analysis
NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.112, Goddard - data analysis, peak picking
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis
PSVS v1.3, Bhattacharya and Montelione - structure quality analysis
MolProbity v3.15, Richardson - structure quality analysis
PDBStat v5.1, Tejero and Montelione - PDB coordinate analysis
TALOS vplus, Cornilescu, Delaglio and Bax - dihedral angle constraints
NMR spectrometers:
- Bruker Avance 800 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts