BMRB Entry 15218
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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/BMR15218
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Title: 1H and 13C Chemical shifts for the ATWLPPR peptide. PubMed: 17983687
Deposition date: 2007-04-19 Original release date: 2008-02-20
Authors: Herve du Penhoat, Catherine; Badache, Sabah; Bouchemal, Nadia
Citation: Starzec, Anna; Vassy, Roger; Badache, Sabah; Bouchemal, Nadia; Herve du Penhoat, Catherine; Perret, Gerard. "Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex." Peptides 28, 2397-2402 (2007).
Assembly members:
ATWLPPR, polymer, 7 residues, 843.014 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: chemical synthesis
Entity Sequences (FASTA):
ATWLPPR: ATWLPPR
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 27 |
| 1H chemical shifts | 53 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 7 residues - 843.014 Da.
| 1 | ALA | THR | TRP | LEU | PRO | PRO | ARG |
Samples:
sample_1: ATWLPPR 6 mM; phosphate buffer 10 mM; NaCl 140 mM; EDTA 5 uM; NaN3 2 uM
sample_2: ATWLPPR 6 mM; phosphate buffer 10 mM; NaCl 140 mM; EDTA 5 uM; NaN3 2 uM
sample_conditions_1: ionic strength: 0.140 M; pH: 7.0; pressure: 1 atm; temperature: 298 K
sample_conditions_2: ionic strength: 0.140 M; pH: 7.0; pressure: 1 atm; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DQF-COSY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_2 | isotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-1H COSY | sample_1 | isotropic | sample_conditions_1 |
| 1D proton spectrum | sample_1 | isotropic | sample_conditions_1 |
| 1D proton spectrum | sample_2 | isotropic | sample_conditions_1 |
| 1D proton spectrum | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-1H TOCSY | sample_1 | isotropic | sample_conditions_2 |
| 2D 1H-1H NOESY | sample_1 | isotropic | sample_conditions_2 |
Software:
XEASY v1.2, Bartels et al. - data analysis
DYANA v1.5, Guntert, Braun and Wuthrich - structure solution
PROSA, Guntert - data analysis
NMR spectrometers:
- Varian UnityPlus 500 MHz