BMRB Entry 19879
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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/BMR19879
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Title: NMR solution structure of a computational designed protein based on structure template 1cy5
Deposition date: 2014-03-28 Original release date: 2014-10-27
Authors: Xiong, Peng; Wang, Meng; Zhang, Jiahai; Chen, Quan; Liu, Haiyan
Citation: Xiong, Peng; Wang, Meng; Zhou, Xiaoqun; Zhang, Tongchuan; Zhang, Jiahai; Chen, Quan; Liu, Haiyan. "Boost computational protein design with a comprehensive statistical energy function and an in vivo experimental approach" Nat. Struct. Biol. ., .-..
Assembly members:
entity, polymer, 94 residues, 10745.617 Da.
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MTPEQREFLPEILAEIIANL
DPTKILEELLRRGLLTPAEL
QEVLDLKTPEEQAKKLIDFI
LKLSPADVQARINVLRAHGY
QALADKLNKYLTLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 214 |
| 15N chemical shifts | 57 |
| 1H chemical shifts | 442 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 94 residues - 10745.617 Da.
| 1 | MET | THR | PRO | GLU | GLN | ARG | GLU | PHE | LEU | PRO | ||||
| 2 | GLU | ILE | LEU | ALA | GLU | ILE | ILE | ALA | ASN | LEU | ||||
| 3 | ASP | PRO | THR | LYS | ILE | LEU | GLU | GLU | LEU | LEU | ||||
| 4 | ARG | ARG | GLY | LEU | LEU | THR | PRO | ALA | GLU | LEU | ||||
| 5 | GLN | GLU | VAL | LEU | ASP | LEU | LYS | THR | PRO | GLU | ||||
| 6 | GLU | GLN | ALA | LYS | LYS | LEU | ILE | ASP | PHE | ILE | ||||
| 7 | LEU | LYS | LEU | SER | PRO | ALA | ASP | VAL | GLN | ALA | ||||
| 8 | ARG | ILE | ASN | VAL | LEU | ARG | ALA | HIS | GLY | TYR | ||||
| 9 | GLN | ALA | LEU | ALA | ASP | LYS | LEU | ASN | LYS | TYR | ||||
| 10 | LEU | THR | LEU | GLU |
Samples:
sample_1: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM
sample_2: protein, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; phosphate buffer 25 mM; sodium chloride 100 mM; EDTA 2 mM
sample_conditions_1: ionic strength: 125 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 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
| 3D HCCH-COSY | sample_2 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
or all simulated shifts