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 18655

Title: Arced helix (ArcH) NMR structure of the reovirus p14 fusion-associated small transmembrane (FAST) protein transmembrane domain (TMD) in dodecyl phosphocholine (DPC) micelles

Deposition date: 2012-08-10 Original release date: 2012-09-04

Authors: Sarker, Muzaddid; Key, Tim; Duncan, Roy; Rainey, Jan

Citation: Sarker, Muzaddid; Key, Tim; Rainey, Jan; Duncan, Roy. "A Cell-Cell Membrane Fusion Module Comprising a Transmembrane Arced Helix (ArcH)"  Not known ., .-..

Assembly members:
ArcH, polymer, 32 residues, 3816.708 Da.

Natural source:   Common Name: Reptilian orthoreovirus   Taxonomy ID: 226613   Superkingdom: Viruses   Kingdom: not available   Genus/species: Reptilian orthoreovirus

Experimental source:   Production method: chemical synthesis   Host organism: Reptilian orthoreovirus

Entity Sequences (FASTA):
ArcH: KKHTIWEVIAGLVALLTFLA FGFWLFKYLQKK

Data sets:
Data typeCount
15N chemical shifts8
1H chemical shifts279

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Transmembrane Arced Helix (ArcH)1

Entities:

Entity 1, Transmembrane Arced Helix (ArcH) 32 residues - 3816.708 Da.

1   LYSLYSHISTHRILETRPGLUVALILEALA
2   GLYLEUVALALALEULEUTHRPHELEUALA
3   PHEGLYPHETRPLEUPHELYSTYRLEUGLN
4   LYSLYS

Samples:

sample_1: p14 TMD peptide, Partial 15N (8 of 32 amino acids), 0.75 mM; DPC, [U-2H], 150 mM; DSS 0.5 mM; sodium azide 0.2 mM; sodium acetate, [U-2H], 20 mM; H2O 95%; D2O 5%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.18, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure solution

TOPSPIN v2.1, Bruker Biospin - collection, processing

SPARKY v3.110, Goddard - chemical shift assignment, peak picking

Molmol v2k.2, Koradi, Billeter and Wuthrich - ensemble superposition, RMSD calculation, visualization

Chimera v1.6.2, Pettersen, Goddard, Huang, Couch, Greenblatt, Meng, Ferrin - Distance measurement, visualization

ProcheckNMR v3.5.4, Laskowski and MacArthur - Ramachandran plot statistics, structure validation

DSSP, Kabsch, Sander; Joosten, Te Beek, Krieger, Hekkelman, Hooft, Schneider, Sander, Vriend - secondary structure analysis

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

PDB

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