BMRB Entry 15604
Click here to enlarge.
PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15604
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solution NMR structure of Ssl0352 protein from Synechocystis sp. - Northeast Structural Genomics Consortium target SgR42
Deposition date: 2007-12-22 Original release date: 2008-03-07
Authors: Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas
Citation: Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Rost, Burkhard; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of Ssl0352 protein from Synechocystis sp." Proteins: Struct. Funct. Genet. ., .-..
Assembly members:
SgR42_protein, polymer, 66 residues, 7657.740 Da.
Natural source: Common Name: Synechocystis sp. Taxonomy ID: 1143 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis sp.
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SgR42_protein: MIFPGATVRVTNVDDTYYRF
EGLVQRVSDGKAAVLFENGN
WDKLVTFRLSELEAVKPILE
HHHHHH
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 13C chemical shifts | 268 |
| 15N chemical shifts | 66 |
| 1H chemical shifts | 446 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SgR42_protein | 1 |
Entities:
Entity 1, SgR42_protein 66 residues - 7657.740 Da.
C-terminal His-tag LEHHHHHH
| 1 | MET | ILE | PHE | PRO | GLY | ALA | THR | VAL | ARG | VAL | ||||
| 2 | THR | ASN | VAL | ASP | ASP | THR | TYR | TYR | ARG | PHE | ||||
| 3 | GLU | GLY | LEU | VAL | GLN | ARG | VAL | SER | ASP | GLY | ||||
| 4 | LYS | ALA | ALA | VAL | LEU | PHE | GLU | ASN | GLY | ASN | ||||
| 5 | TRP | ASP | LYS | LEU | VAL | THR | PHE | ARG | LEU | SER | ||||
| 6 | GLU | LEU | GLU | ALA | VAL | LYS | PRO | ILE | LEU | GLU | ||||
| 7 | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
NC: SgR42 protein, [U-100% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%
NC5: SgR42 protein, [U-5% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%
sample_conditions_1: ionic strength: 135 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | 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 HNCO | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT CABCA(CO)NHN | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HNNCABCA | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HABCAB(CO)NHN | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY aliphatic | NC | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY aliphatic | NC | isotropic | sample_conditions_1 |
| (4,3)D GFT HCCH-COSY aromatic | NC | isotropic | sample_conditions_1 |
| 3D 1H-15N,13C NOESY | NC | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC 28ms methyl | NC5 | isotropic | sample_conditions_1 |
| 2D 1H-13C CT-HSQC 56ms methyl | NC5 | isotropic | sample_conditions_1 |
Software:
VNMRJ v2.1B, Varian - collection
PROSA v6.0.2, Guntert - processing
CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking
CSI v2.0, Wishart and Sykes - data analysis
TALOS, Cornilescu, Delaglio and Bax - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution
AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
XEASY, Bartels et al. - chemical shift assignment, data analysis
NMR spectrometers:
- Varian INOVA 750 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