BMRB Entry 5549
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5549
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Title: Neuropeptide Y5-Receptor II: Solution Structure and Dynamics of [31Ala,32Pro]-NPY PubMed: 12069594
Deposition date: 2002-10-07 Original release date: 2008-07-17
Authors: Bader, Reto; Rytz, G.; Lerch, M.; Beck-Sickinger, Annette; Zerbe, Oliver
Citation: Bader, Reto; Rytz, G.; Lerch, M.; Beck-Sickinger, Annette; Zerbe, Oliver. "Key Motif to Gain Selectivity at the Neuropeptide Y5-receptor: Structure and Dynamics of Micelle-bound [Ala31,Pro32]-NPY" Biochemistry 41, 8031-8042 (2002).
Assembly members:
[Ala31, Pro32]-NEUROPEPTIDE Y, polymer, 37 residues, Formula weight is not available
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: chemical synthesis
Entity Sequences (FASTA):
[Ala31, Pro32]-NEUROPEPTIDE Y: YPSKPDNPGEDAPAEDLARY
YSALRHYINLAPRQRYX
- assigned_chemical_shifts
- order_parameters
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- heteronucl_NOEs
Data type | Count |
1H chemical shifts | 222 |
15N chemical shifts | 31 |
T1 relaxation values | 56 |
T2 relaxation values | 54 |
heteronuclear NOE values | 28 |
S2 parameters | 28 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | [Ala31, Pro32]-NPY | 1 |
Entities:
Entity 1, [Ala31, Pro32]-NPY 37 residues - Formula weight is not available
1 | TYR | PRO | SER | LYS | PRO | ASP | ASN | PRO | GLY | GLU | ||||
2 | ASP | ALA | PRO | ALA | GLU | ASP | LEU | ALA | ARG | TYR | ||||
3 | TYR | SER | ALA | LEU | ARG | HIS | TYR | ILE | ASN | LEU | ||||
4 | ALA | PRO | ARG | GLN | ARG | TYR | NH2 |
Samples:
sample_1: [Ala31, Pro32]-NEUROPEPTIDE Y, [U-15N], 2.5 mM; DPC 300 mM; H2O 90%; D2O 90%
sample_cond_1: pH*: 6.0; temperature: 310 K; pressure: 1 atm
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D NOESY | sample_1 | not available | sample_cond_1 |
E-COSY | sample_1 | not available | sample_cond_1 |
Software:
XWINNMR v2.1 - data processing
XEASY v1.53 - data analysis
DYANA v1.5 - structure solution
NMR spectrometers:
- Varian UnityPlus 500 MHz
- Bruker AVANCE 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts