BMRB Entry 16084
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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/BMR16084
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Title: SOLUTION STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SrR115C
Deposition date: 2008-12-22 Original release date: 2009-01-09
Authors: Liu, Gaohua; Rossi, Paolo; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano
Citation: Liu, Gaohua; Rossi, Paolo; Wang, Dongyan; Nwosu, Chioma; Owens, Leah; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano. "SOLUTION STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SrR115C" Not known ., .-..
Assembly members:
SRU_0103, polymer, 99 residues, 11487.540 Da.
Natural source: Common Name: Salinibacter ruber Taxonomy ID: 146919 Superkingdom: Bacteria Kingdom: not available Genus/species: Salinibacter ruber
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
SRU_0103: EDPEDPFTRYALAQEHLKHD
NASRALALFEELVETDPDYV
GTYYHLGKLYERLDRTDDAI
DTYAQGIEVAREEGTQKDLS
ELQDAKLKAEGLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 310 |
| 15N chemical shifts | 99 |
| 1H chemical shifts | 655 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SRU_0103 | 1 |
Entities:
Entity 1, SRU_0103 99 residues - 11487.540 Da.
| 1 | GLU | ASP | PRO | GLU | ASP | PRO | PHE | THR | ARG | TYR | ||||
| 2 | ALA | LEU | ALA | GLN | GLU | HIS | LEU | LYS | HIS | ASP | ||||
| 3 | ASN | ALA | SER | ARG | ALA | LEU | ALA | LEU | PHE | GLU | ||||
| 4 | GLU | LEU | VAL | GLU | THR | ASP | PRO | ASP | TYR | VAL | ||||
| 5 | GLY | THR | TYR | TYR | HIS | LEU | GLY | LYS | LEU | TYR | ||||
| 6 | GLU | ARG | LEU | ASP | ARG | THR | ASP | ASP | ALA | ILE | ||||
| 7 | ASP | THR | TYR | ALA | GLN | GLY | ILE | GLU | VAL | ALA | ||||
| 8 | ARG | GLU | GLU | GLY | THR | GLN | LYS | ASP | LEU | SER | ||||
| 9 | GLU | LEU | GLN | ASP | ALA | LYS | LEU | LYS | ALA | GLU | ||||
| 10 | GLY | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: SRU_0103, [U-100% 13C; U-100% 15N], 1.37 mM
sample_2: SRU_0103, [U-10% 13C; U-100% 15N], 1.05 mM
sample_conditions_1: ionic strength: . M; 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-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (aliph) | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT CABCACONHN | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HNNCABCA | sample_1 | isotropic | sample_conditions_1 |
| 4,3D GFT HABCABCONHN | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY (arom) | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
CYANA, Guntert, Mumenthaler and Wuthrich - geometry optimization, refinement, structure solution
AutoStruct, Huang, Tejero, Powers and Montelione - data analysis, refinement, structure solution
PSVS, Bhattacharya and Montelione - data analysis, refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment, data analysis
XEASY, Bartels et al. - chemical shift assignment, data analysis, refinement
TOPSPIN, Bruker Biospin - collection
VNMRJ, Varian - collection
NMR spectrometers:
- Bruker Avance 800 MHz
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 16821 |
| PDB | |
| EMBL | CBH23027 |
| GB | ABC44923 |
| REF | WP_011402889 WP_043551686 YP_444256 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts