BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 20019

Title: NMR structure of a V3 (MN isolate) peptide   PubMed: 19117029

Authors: Galanakis, Petros; Kandias, Nikolaos; Rizos, Apostolos; Morikis, Dimitrios; Krambovitis, Elias; Spyroulias, Georgios

Citation: Galanakis, Petros; Kandias, Nikolaos; Rizos, Apostolos; Morikis, Dimitrios; Krambovitis, Elias; Spyroulias, Georgios. "NMR evidence of charge-dependent interaction between various PND V3 and CCR5 N-terminal peptides"  Biopolymers 94, 94-109 (2008).

Assembly members:
PND MN, polymer, 13 residues, 1418.734 Da.
PND, non-polymer, 153.139 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: recombinant technology

Entity Sequences (FASTA):
PND MN: RKRIHIGPGRAFY

Data sets:
Data typeCount
13C chemical shifts4
1H chemical shifts88

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1PND MN1
2PND2

Entities:

Entity 1, PND MN 13 residues - 1418.734 Da.

1   ARGLYSARGILEHISILEGLYPROGLYARG
2   ALAPHETYR

Entity 2, PND - C6 H7 N3 O2 - 153.139 Da.

1   PND

Samples:

sample_1: PND MN2 – 2.5 mM; PND2 – 2.5 mM; D2O 10%; H2O 90%

sample_conditions_1: pH: 7.85; temperature: 278 K

sample_conditions_2: pH: 7.85; temperature: 286 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-13C HSQCsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_2
2D 1H-1H NOESYsample_1isotropicsample_conditions_2
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

AMBER v5.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

DYANA, Guntert, Braun and Wuthrich - structure solution

XEASY, Bartels et al. - chemical shift assignment

xwinnmr, Bruker Biospin - processing

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 700 MHz

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