BMRB Entry 15218

Name: 1H and 13C Chemical shifts for the ATWLPPR peptide.
Published: 2008-02-20

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PDB ID: 2jp5
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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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

1H and 13C Chemical shifts for the ATWLPPR peptide.

Deposition date:

2007-04-19

Original release date:

2008-02-20

Authors:

Herve du Penhoat, Catherine; Badache, Sabah; Bouchemal, Nadia

Citation:

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).
PubMed: 17983687

Assembly members:

Assembly members:
ATWLPPR, polymer, 7 residues, 843.014 Da.

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available

Experimental source:

Experimental source: Production method: chemical synthesis

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ATWLPPR: ATWLPPR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	27
1H chemical shifts	53

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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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

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