BMRB Entry 20015

Name: NMR structure of a V3 (SF2 isolate) peptide
Published: 2009-04-03

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR20015

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR structure of a V3 (SF2 isolate) peptide

Deposition date:

2008-04-09

Original release date:

2009-04-03

Authors:

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

Citation:

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 92, 94-109 (2008).
PubMed: 19117029

Assembly members:

Assembly members:
PND_SF2, polymer, 13 residues, 1481.736 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: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PND_SF2: RKSINIGPGRAFY

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	4
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PND SF2	1

Entities:

Entity 1, PND SF2 13 residues - 1481.736 Da.

1

ARG

LYS

SER

ILE

ASN

ILE

GLY

PRO

GLY

ARG

2

ALA

PHE

TYR

Samples:

sample_1: H2O2 – 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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_2
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_2
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_2

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