BMRB Entry 16486
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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/BMR16486
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Title: Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR148A
Deposition date: 2009-09-08 Original release date: 2009-09-29
Authors: Eletsky, Alexander; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Garcia, Erwin; Wang, Huang; Ciccosanti, Colleen; Jiang, Mei; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the ACT domain from GTP pyrophosphokinase of Chlorobium tepidum." Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
CtR148A, polymer, 88 residues, 10050.751 Da.
Natural source: Common Name: Chlorobium tepidum Taxonomy ID: 194439 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CtR148A: MTDFLAGIRIVGEDKNGMTN
QITGVISKFDTNIRTIVLNA
KDGIFTCNLMIFVKNTDKLT
TLMDKLRKVQGVFTVERLSN
LEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 368 |
| 15N chemical shifts | 94 |
| 1H chemical shifts | 630 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
| 2 | entity_2 | 1 |
Entities:
Entity 1, entity_1 88 residues - 10050.751 Da.
Residues 2-80 correspond to the 653-731 fragment of the native protein. Residues 81-88 represent a non-native affinity tag. Residue M1 is a result of a new start codon.
| 1 | MET | THR | ASP | PHE | LEU | ALA | GLY | ILE | ARG | ILE | ||||
| 2 | VAL | GLY | GLU | ASP | LYS | ASN | GLY | MET | THR | ASN | ||||
| 3 | GLN | ILE | THR | GLY | VAL | ILE | SER | LYS | PHE | ASP | ||||
| 4 | THR | ASN | ILE | ARG | THR | ILE | VAL | LEU | ASN | ALA | ||||
| 5 | LYS | ASP | GLY | ILE | PHE | THR | CYS | ASN | LEU | MET | ||||
| 6 | ILE | PHE | VAL | LYS | ASN | THR | ASP | LYS | LEU | THR | ||||
| 7 | THR | LEU | MET | ASP | LYS | LEU | ARG | LYS | VAL | GLN | ||||
| 8 | GLY | VAL | PHE | THR | VAL | GLU | ARG | LEU | SER | ASN | ||||
| 9 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC5_PEG: CtR148A, [U-5% 13C; U-100% 15N], 0.3 mM; MES 18 mM; sodium chloride 180 mM; calcium chloride 4.5 mM; DTT 9 mM; DSS 45 uM; sodium azide 0.045%; polyethylene glycol 4%; D2O 16%; H2O 84%
NC5_PAAG: CtR148A, [U-5% 13C; U-100% 15N], 0.45 mM; MES 18 mM; sodium chloride 180 mM; calcium chloride 4.5 mM; DTT 9 mM; DSS 45 uM; sodium azide 0.045%; polyacrylamide 7%; D2O 14%; H2O 86%
NC: CtR148A, [U-100% 13C; U-100% 15N], 0.3 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; D2O 10%; H2O 90%
NC5: CtR148A, [U-5% 13C; U-100% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; D2O 10%; H2O 90%
MIX: CtR148A, [U-100% 13C; U-100% 15N], 0.5 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.05%; CtR148A 0.5 mM; D2O 10%; H2O 90%
sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 15N T1 | NC | isotropic | sample_conditions_1 |
| 1D 15N T2 | NC | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aromatic | NC | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HNCACB | NC | isotropic | sample_conditions_1 |
| 3D HNCO | NC | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | NC | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N/13C NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC methyl | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-modulated | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-modulated | NC5_PEG | anisotropic | sample_conditions_1 |
| 2D 1H-15N HSQC J-modulated | NC5_PAAG | anisotropic | sample_conditions_1 |
| 3D 1H-13C X-filtered NOESY | MIX | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.4, Guntert - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
TALOS+ v1.2009.0721.18, Yang,Cornilescu, Delaglio and Bax - data analysis
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure validation
PSVS v1.3, Bhattacharya and Montelione - structure validation
NMR spectrometers:
- Varian INOVA 750 MHz
- Varian INOVA 600 MHz
- Varian INOVA 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts