BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15218

Title: 1H and 13C Chemical shifts for the ATWLPPR peptide.   PubMed: 17983687

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

Data sets:
Data typeCount
13C chemical shifts27
1H chemical shifts53

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 7 residues - 843.014 Da.

1   ALATHRTRPLEUPROPROARG

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:

NameSampleSample stateSample conditions
2D DQF-COSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H COSYsample_1isotropicsample_conditions_1
1D proton spectrumsample_1isotropicsample_conditions_1
1D proton spectrumsample_2isotropicsample_conditions_1
1D proton spectrumsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_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

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