BMRB Entry 15106
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15106
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Title: Solution Structure of the second Clip domain in PAP2 (CASP Target) PubMed: 17880110
Deposition date: 2007-01-22 Original release date: 2008-06-25
Authors: Huang, R.; Lv, Z.; Dai, H.; Velde, D.; Prakash, O.; Jiang, H.
Citation: Huang, R.; Lu, Z.; Dai, H.; Velde, D.; Prakash, O.; Jiang, H.. "The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2" Biochemistry 46, 11431-11439 (2007).
Assembly members:
Prophenoloxidase_activating_proteinase-2, polymer, 54 residues, Formula weight is not available
Natural source: Common Name: Tobacco hawkmoth 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):
Prophenoloxidase_activating_proteinase-2: LSCLTPDNKPGKCVNIKKCT
HLAEIEEDPIGEDETTYLKN
SVCAGPEDNSVCCG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 198 |
| 15N chemical shifts | 51 |
| 1H chemical shifts | 291 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | clip domain | 1 |
Entities:
Entity 1, clip domain 54 residues - Formula weight is not available
| 1 | LEU | SER | CYS | LEU | THR | PRO | ASP | ASN | LYS | PRO | ||||
| 2 | GLY | LYS | CYS | VAL | ASN | ILE | LYS | LYS | CYS | THR | ||||
| 3 | HIS | LEU | ALA | GLU | ILE | GLU | GLU | ASP | PRO | ILE | ||||
| 4 | GLY | GLU | ASP | GLU | THR | THR | TYR | LEU | LYS | ASN | ||||
| 5 | SER | VAL | CYS | ALA | GLY | PRO | GLU | ASP | ASN | SER | ||||
| 6 | VAL | CYS | CYS | GLY |
Samples:
sample: Prophenoloxidase activating proteinase-2, [U-100% 13C; U-100% 15N], 1.0 mM; phosphate buffer 100 mM
sample_conditions_1: pH: 8.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D_13C-separated_NOESY | sample | isotropic | sample_conditions_1 |
| 3D_15N-separated_NOESY | sample | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker - collection
SPARKY, Goddard - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution
NMR spectrometers:
- Bruker AVANCE 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts