BMRB Entry 16649
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16649
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Title: Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A
Deposition date: 2009-12-22 Original release date: 2010-02-22
Authors: He, Yunfen; Eletsky, Alexander; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas
Citation: He, Yunfen; Eletsky, Alexander; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A" Not known ., .-..
Assembly members:
CtR69A, polymer, 63 residues, 7319.465 Da.
Natural source: Common Name: green sulfur bacteria Taxonomy ID: 1097 Superkingdom: Bacteria Kingdom: not available Genus/species: Chlorobium tepidum
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CtR69A: MGELSWTAEAEKMLGKVPFF
VRKKVRKNTDNYAREIGEPV
VTADVFRKAKEHLGGLEHHH
HHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 255 |
| 15N chemical shifts | 63 |
| 1H chemical shifts | 414 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CtR69A | 1 |
Entities:
Entity 1, CtR69A 63 residues - 7319.465 Da.
Residues 2-55 correspond to residues 484-537 of the native protein. Residues 56-63 represent a non-native affinity tag. Residue 1 corresponds the introduced start-codon.
| 1 | MET | GLY | GLU | LEU | SER | TRP | THR | ALA | GLU | ALA | ||||
| 2 | GLU | LYS | MET | LEU | GLY | LYS | VAL | PRO | PHE | PHE | ||||
| 3 | VAL | ARG | LYS | LYS | VAL | ARG | LYS | ASN | THR | ASP | ||||
| 4 | ASN | TYR | ALA | ARG | GLU | ILE | GLY | GLU | PRO | VAL | ||||
| 5 | VAL | THR | ALA | ASP | VAL | PHE | ARG | LYS | ALA | LYS | ||||
| 6 | GLU | HIS | LEU | GLY | GLY | LEU | GLU | HIS | HIS | HIS | ||||
| 7 | HIS | HIS | HIS |
Samples:
sample_1: entity, [U-100% 13C; U-100% 15N], 1.080 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; NaN3 0.02%
sample_2: entity, [U-5% 13C; U-100% 15N], 0.986 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; NaN3 0.02%
sample_conditions_1: ionic strength: 117.5 mM; 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 CT-HSQC ali | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC (methyl) | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 ali | sample_1 | isotropic | sample_conditions_1 |
| 13C/15N-NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC aro | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY aro | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N LR-HSQC (Histidine) | sample_1 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.4, Guntert - processing
XEASY, Bartels et al. - data analysis
PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution
TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis
CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking
PSVS v1.3, Bhattacharya and Montelione - validation
NMR spectrometers:
- Varian INOVA 500 MHz
- Varian INOVA 750 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts