BMRB Entry 34016
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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/BMR34016
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Title: NMR structure of peptide 2 targeting CXCR4 PubMed: 27571038
Deposition date: 2016-07-01 Original release date: 2016-09-02
Authors: Di Maro, S.; Trotta, A.; Brancaccio, D.; Di Leva, F.; La Pietra, V.; Ierano, C.; Napolitano, M.; Portella, L.; D'Alterio, C.; Siciliano, R.; Sementa, D.; Tomassi, S.; Carotenuto, A.; Novellino, E.; Scala, S.; Marinelli, L.
Citation: Di Maro, S.; Trotta, A.; Brancaccio, D.; Di Leva, F.; La Pietra, V.; Ierano, C.; Napolitano, M.; Portella, L.; D'Alterio, C.; Siciliano, R.; Sementa, D.; Tomassi, S.; Carotenuto, A.; Novellino, E.; Scala, S.; Marinelli, L.. "Exploring the N-terminal region of C-X-C motif chemokine 12 (CXCL12): Identification of plasma-stable cyclic peptides as novel, potent C-X-C chemokine receptor type 4 (CXCR4) antagonists." J. Med. Chem. 59, 8369-8380 (2016).
Assembly members:
entity_1, polymer, 7 residues, 904.114 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: RACRFFC
- assigned_chemical_shifts
- spectral_peak_list
| Data type | Count |
| 1H chemical shifts | 45 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 7 residues - 904.114 Da.
| 1 | ARG | ALA | CYS | ARG | PHE | PHE | CYS |
Samples:
sample_1: H2O, deuterad, 10%; Peptide 2 2 mM; SDS, deuterated, 200 mM
sample_conditions_1: ionic strength: 0 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 1D 1H | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-1H NOESY | sample_1 | anisotropic | sample_conditions_1 |
| 2D 1H-1H TOCSY | sample_1 | anisotropic | sample_conditions_1 |
| 2D DQF-COSY | sample_1 | anisotropic | sample_conditions_1 |
Software:
DYANA, Guntert, Braun and Wuthrich - structure calculation
XEASY, Bartels et al. - chemical shift assignment
DISCOVER, Accelrys Software Inc. - refinement
NMR spectrometers:
- Varian INOVA 700 MHz