BMRB Entry 15415
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15415
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Title: Solution structure of Sso6901 from Sulfolobus solfataricus P2 PubMed: 18096617
Deposition date: 2007-08-03 Original release date: 2008-10-29
Authors: Feng, Yingang; Guo, Li; Huang, Li; Wang, Jinfeng
Citation: Guo, Li; Feng, Yingang; Zhang, Zhenfeng; Yao, Hongwei; Luo, Yuanming; Wang, Jinfeng; Huang, Li. "Biochemical and structural characterization of Cren7, a novel chromatin protein conserved among Crenarchaea" Nucleic Acids Res. 36, 1129-1137 (2008).
Assembly members:
Cren7, polymer, 60 residues, 6685.043 Da.
Natural source: Common Name: Sulfolobus solfataricus Taxonomy ID: 2287 Superkingdom: Archaea Kingdom: not available Genus/species: Sulfolobus solfataricus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Cren7: MSSGKKPVKVKTPAGKEAEL
VPEKVWALAPKGRKGVKIGL
FKDPETGKYFRHKLPDDYPI
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 279 |
15N chemical shifts | 51 |
1H chemical shifts | 434 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | Cren7 | 1 |
Entities:
Entity 1, Cren7 60 residues - 6685.043 Da.
1 | MET | SER | SER | GLY | LYS | LYS | PRO | VAL | LYS | VAL | |
2 | LYS | THR | PRO | ALA | GLY | LYS | GLU | ALA | GLU | LEU | |
3 | VAL | PRO | GLU | LYS | VAL | TRP | ALA | LEU | ALA | PRO | |
4 | LYS | GLY | ARG | LYS | GLY | VAL | LYS | ILE | GLY | LEU | |
5 | PHE | LYS | ASP | PRO | GLU | THR | GLY | LYS | TYR | PHE | |
6 | ARG | HIS | LYS | LEU | PRO | ASP | ASP | TYR | PRO | ILE |
Samples:
sample_1H: entity1.0 2.0 mM; DSS 0.01%; potassium phosphate 50 mM
sample_15N13C: entity, [U-13C; U-15N], 1.0 2.0 mM; DSS 0.01%; potassium phosphate 50 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 310 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-1H TOCSY | sample_1H | isotropic | sample_conditions_1 |
2D DQF-COSY | sample_1H | isotropic | sample_conditions_1 |
2D 1H-1H NOESY | sample_1H | isotropic | sample_conditions_1 |
2D 1H-15N HSQC | sample_15N13C | isotropic | sample_conditions_1 |
2D 1H-13C HSQC | sample_15N13C | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_15N13C | isotropic | sample_conditions_1 |
3D HNCACB | sample_15N13C | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_15N13C | isotropic | sample_conditions_1 |
3D HNCO | sample_15N13C | isotropic | sample_conditions_1 |
3D HN(CA)CO | sample_15N13C | isotropic | sample_conditions_1 |
3D 1H-15N TOCSY | sample_15N13C | isotropic | sample_conditions_1 |
3D HCCH-COSY | sample_15N13C | isotropic | sample_conditions_1 |
3D CCH-TOCSY | sample_15N13C | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_15N13C | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_15N13C | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection
FELIX, Accelrys Software Inc. - chemical shift assignment, peak picking, processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
PDB | |
GB | AAK41249 ACP35343 ACP38003 ACP45499 ACP48703 |
REF | WP_009992425 WP_012711256 |
SP | C3MPN0 C3MYM4 C3N5A6 C3NDW0 C3NHU3 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts