BMRB Entry 25762
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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/BMR25762
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Title: Structure of Pleiotrophin PubMed: 26896299
Deposition date: 2015-08-20 Original release date: 2016-03-29
Authors: Ryan, Eathen; Shen, Di; Wang, Xu
Citation: Ryan, Eathen; Shen, Di; Wang, Xu. "Structural Studies Reveal an Important Role for the Pleiotrophin C Terminus in Mediating Interactions with Chondroitin Sulfate." FEBS J. 283, 1488-1503 (2016).
Assembly members:
PTN, polymer, 136 residues, 15347.028 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PTN: GKKEKPEKKVKKSDCGEWQW
SVCVPTSGDCGLGTREGTRT
GAECKQTMKTQRCKIPCNWK
KQFGAECKYQFQAWGECDLN
TALKTRTGSLKRALHNAECQ
KTVTISKPCGKLTKPKPQAE
SKKKKKEGKKQEKMLD
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 533 |
| 15N chemical shifts | 127 |
| 1H chemical shifts | 620 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Pleiotrophin | 1 |
Entities:
Entity 1, Pleiotrophin 136 residues - 15347.028 Da.
| 1 | GLY | LYS | LYS | GLU | LYS | PRO | GLU | LYS | LYS | VAL | ||||
| 2 | LYS | LYS | SER | ASP | CYS | GLY | GLU | TRP | GLN | TRP | ||||
| 3 | SER | VAL | CYS | VAL | PRO | THR | SER | GLY | ASP | CYS | ||||
| 4 | GLY | LEU | GLY | THR | ARG | GLU | GLY | THR | ARG | THR | ||||
| 5 | GLY | ALA | GLU | CYS | LYS | GLN | THR | MET | LYS | THR | ||||
| 6 | GLN | ARG | CYS | LYS | ILE | PRO | CYS | ASN | TRP | LYS | ||||
| 7 | LYS | GLN | PHE | GLY | ALA | GLU | CYS | LYS | TYR | GLN | ||||
| 8 | PHE | GLN | ALA | TRP | GLY | GLU | CYS | ASP | LEU | ASN | ||||
| 9 | THR | ALA | LEU | LYS | THR | ARG | THR | GLY | SER | LEU | ||||
| 10 | LYS | ARG | ALA | LEU | HIS | ASN | ALA | GLU | CYS | GLN | ||||
| 11 | LYS | THR | VAL | THR | ILE | SER | LYS | PRO | CYS | GLY | ||||
| 12 | LYS | LEU | THR | LYS | PRO | LYS | PRO | GLN | ALA | GLU | ||||
| 13 | SER | LYS | LYS | LYS | LYS | LYS | GLU | GLY | LYS | LYS | ||||
| 14 | GLN | GLU | LYS | MET | LEU | ASP |
Samples:
sample_1: PTN, [U-100% 13C; U-100% 15N], 0.6 ± 0.05 mM; D2O 10%; MES 10 mM; sodium chloride 150 mM; H2O 90%
sample_conditions_1: ionic strength: 0.15 M; pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRView, Johnson, One Moon Scientific - data analysis
CYANA, Guntert, Mumenthaler and Wuthrich - structure solution
X-PLOR_NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian INOVA 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts