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 19902

Title: Solution NMR structure of the reovirus p15 fusion-associated small transmembrane (FAST) protein fusion-inducing lipid packing sensor (FLiPS) motif in dodecyl phosphocholine (DPC) micelles

Deposition date: 2014-04-09 Original release date: 2014-04-22

Authors: Sarker, Muzaddid; Duncan, Roy; Read, Jolene; Rainey, Jan

Citation: Read, Jolene; Clancy, Eileen; Sarker, Muzaddid; Langelaan, David; Rainey, Jan; Duncan, Roy. "Novel helix-loop-helix fusion-inducing lipid packing sensor (FLiPS) for cell-cell fusion"  Not known ., .-..

Assembly members:
entity_1, polymer, 21 residues, 1941.335 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):
entity_1: XLGLLSYGAGVASLPLLNVI A

Data sets:
Data typeCount
13C chemical shifts39
15N chemical shifts20
1H chemical shifts146

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 21 residues - 1941.335 Da.

1   ACELEUGLYLEULEUSERTYRGLYALAGLY
2   VALALASERLEUPROLEULEUASNVALILE
3   ALA

Samples:

sample_1: entity_1 1 mM; DPC 150 mM; DSS 0.5 mM; sodium azide 0.2 mM; sodium acetate, [U-2H], 20 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

X-PLOR_NIH v2.34, Schwieters, Kuszewski, Tjandra and Clore - refinement

TOPSPIN v3.1, Bruker Biospin - processing

SPARKY v3.110, Goddard - chemical shift assignment

ProcheckNMR v3.5.4, Laskowski and MacArthur - validation

UCSF_CHIMERA v1.8, NIH - structure viewing

Molmol v2K.2, Koradi, Billeter and Wuthrich - ensemble viewing

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB
GB AAL01373
REF YP_004769555

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts