BMRB Entry 15317
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15317
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Title: NMR Solution Structure of Colwellia psychrerythraea protein CPS_2611. Northeast Structural Genomics target CsR4.
Deposition date: 2007-06-19 Original release date: 2007-08-15
Authors: Ramelot, Theresa; Cort, John; Wang, Huang; Nwosu, Chioma; Cunningham, Kellie; Owens, Leah; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T.; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael
Citation: Ramelot, Theresa; Cort, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of Colwellia psychrerythraea protein CPS_2611. Northeast Structural Genomics target CsR4." Not known ., .-..
Assembly members:
protein, polymer, 76 residues, 17170 Da.
Natural source: Common Name: not available Taxonomy ID: 28229 Superkingdom: Bacteria Kingdom: not available Genus/species: Colwellia psychrerythraea
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
protein: MPIVSKYSNERVEKIIQDLL
DVLVKEEVTPDLALMCLGNA
VTNIIAQVPESKRVAVVDNF
TKALKQSVLEHHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 336 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 556 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
| 2 | subunit 2 | 1 |
Entities:
Entity 1, subunit 1 76 residues - 17170 Da.
8 non-native residues C-terminal His tag (LEHHHHHH)
| 1 | MET | PRO | ILE | VAL | SER | LYS | TYR | SER | ASN | GLU | ||||
| 2 | ARG | VAL | GLU | LYS | ILE | ILE | GLN | ASP | LEU | LEU | ||||
| 3 | ASP | VAL | LEU | VAL | LYS | GLU | GLU | VAL | THR | PRO | ||||
| 4 | ASP | LEU | ALA | LEU | MET | CYS | LEU | GLY | ASN | ALA | ||||
| 5 | VAL | THR | ASN | ILE | ILE | ALA | GLN | VAL | PRO | GLU | ||||
| 6 | SER | LYS | ARG | VAL | ALA | VAL | VAL | ASP | ASN | PHE | ||||
| 7 | THR | LYS | ALA | LEU | LYS | GLN | SER | VAL | LEU | GLU | ||||
| 8 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC_sample: protein, [U-13C; U-15N], 1 ± 0.1 mM; sodium chloride 100 ± 5 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; calcium chloride 5 ± 0.25 mM
NC5_sample: protein, [U-5% 13C; U-100% 15N], 1.1 ± 0.1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %
NC_in_D2O: protein, [U-13C; U-15N], 1.0 ± 0.1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %
NC50_sample_in_D2O: protein, [U-13C; U-15N], 0.5 ± 0.05 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.25 mM; ammonium acetate 20 ± 1 mM; DTT 5 ± 0.25 mM; sodium azide 0.02 ± 0.001 %; protein 0.5 ± 0.05 mM
sample_conditions_1: ionic strength: 0.1 M; pH: 5.5; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (aliph) | 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 HNCACB | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC5_sample | isotropic | sample_conditions_1 |
| 4D 1H-13C NOESY | NC_in_D2O | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HNHA | NC_sample | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 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 HNCO | NC_sample | isotropic | sample_conditions_1 |
| 3D C(CO)NH | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | NC_sample | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | NC_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (15 min) | NC_in_D2O | isotropic | sample_conditions_1 |
| 3D edited filtered 1H-13C NOESY | NC50_sample_in_D2O | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY arom | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom ct) | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC (arom no ct) | NC_sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (30 min) | NC_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (1 hr) | NC_in_D2O | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC (6 days) | NC_in_D2O | isotropic | sample_conditions_1 |
Software:
NMRPipe vlinux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
VNMR v6.1C, Varian - collection
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - data analysis
X-PLOR NIH v2.15.0, Schwieters, Kuszewski, Tjandra and Clore - structure solution
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
SPARKY v3.1, Goddard - data analysis
PSVS v1.3, Bhattacharya and Montelione - structure validation
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
NMR spectrometers:
- 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