BMRB Entry 5548
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5548
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Citation: Lerch, Mirjam; Gafner, Verena; Bader, Reto; Christen, Barbara; Folkers, G.; Zerbe, Oliver. "Bovine Pancreatic Polypeptide (bPP) Undergoes Significant Changes in
Conformation and Dynamics upon Binding to DPC Micelles " J. Mol. Biol. 322, 1117-1133 (2002).
PubMed: 12367532
Assembly members:
Pancreatic polypeptide, polymer, 37 residues, Formula weight is not available
Natural source: Common Name: Bovine Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Pancreatic polypeptide: APLEPEYPGDNATPEQMAQY
AAELRRYINMLTRPRYX
- assigned_chemical_shifts
- order_parameters
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- heteronucl_NOEs
| Data type | Count |
| 1H chemical shifts | 30 |
| 15N chemical shifts | 30 |
| T1 relaxation values | 112 |
| T2 relaxation values | 112 |
| heteronuclear NOE values | 84 |
| order parameters | 56 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pancreatic polypeptide | 1 |
Entities:
Entity 1, pancreatic polypeptide 37 residues - Formula weight is not available
| 1 | ALA | PRO | LEU | GLU | PRO | GLU | TYR | PRO | GLY | ASP | ||||
| 2 | ASN | ALA | THR | PRO | GLU | GLN | MET | ALA | GLN | TYR | ||||
| 3 | ALA | ALA | GLU | LEU | ARG | ARG | TYR | ILE | ASN | MET | ||||
| 4 | LEU | THR | ARG | PRO | ARG | TYR | NH2 |
Samples:
sample_1: Pancreatic polypeptide, [U-95% 15N], 3 mM; DPC-d38 300 mM
sample_2: Pancreatic polypeptide, [U-95% 15N], mM
sample_cond_1: pH*: 5.5 na; temperature: 310 K; ionic strength: 0 M; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D NOESY | not available | not available | sample_cond_1 |
| E-COSY | not available | not available | sample_cond_1 |
Software:
XWINNMR v2.6 - processing
XEASY v1.53 - data analysis
DYANA v1.5 - structure solution
AMBER v6 - refinement
NMR spectrometers:
- Varian UnityPlus 500 MHz
- Bruker AVANCE 600 MHz
Related Database Links:
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks