BMRB Entry 19205
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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/BMR19205
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Title: Solution NMR Structure of Engineered Cystine Knot Protein 2.5D PubMed: 24318984
Deposition date: 2013-04-30 Original release date: 2014-05-05
Authors: Cochran, Frank; Das, Rhiju
Citation: Kryshtafovych, Andriy; Moult, John; Bales, Patrick; Bazan, J. Fernando; Biasini, Marco; Burgin, Alex; Chen, Chen; Cochran, Frank; Craig, Timothy; Das, Rhiju; Fass, Deborah; Garcia-Doval, Carmela; Herzberg, Osnat; Lorimer, Donald; Luecke, Hartmut; Ma, Xiaolei; Nelson, Daniel; van Raaij, Mark; Rohwer, Forest; Segall, Anca; Seguritan, Victor; Zeth, Kornelius; Schwede, Torsten. "Challenging the state of the art in protein structure prediction: Highlights of experimental target structures for the 10th Critical Assessment of Techniques for Protein Structure Prediction Experiment CASP10" Proteins 82, 26-42 (2014).
Assembly members:
entity, polymer, 33 residues, 3250.559 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: GCPQGRGDWAPTSCSQDSDC
LAGCVCGPNGFCG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 114 |
| 15N chemical shifts | 33 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Engineered Cystine Knot Protein 2.5D | 1 |
Entities:
Entity 1, Engineered Cystine Knot Protein 2.5D 33 residues - 3250.559 Da.
| 1 | GLY | CYS | PRO | GLN | GLY | ARG | GLY | ASP | TRP | ALA | ||||
| 2 | PRO | THR | SER | CYS | SER | GLN | ASP | SER | ASP | CYS | ||||
| 3 | LEU | ALA | GLY | CYS | VAL | CYS | GLY | PRO | ASN | GLY | ||||
| 4 | PHE | CYS | GLY |
Samples:
sample_1: 2.5D, [U-13C; U-15N], 300 uM; sodium phosphate 50 mM
sample_conditions_1: ionic strength: 50 mM; pH: 6; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| ghnco_LRA | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Varian VNMRS 800 MHz
- Varian VNS 600 MHz
Related Database Links:
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
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SPARKY: Backbone
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