BMRB Entry 18655

Name: Arced helix (ArcH) NMR structure of the reovirus p14 fusion-associated small transmembrane (FAST) protein transmembrane domain (TMD) in dodecyl phosphocholine (DPC) micelles
Published: 2012-09-04

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PDB ID: 2lx0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18655
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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:

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:

Citation: Sarker, Muzaddid; Key, Tim; Rainey, Jan; Duncan, Roy. "A Cell-Cell Membrane Fusion Module Comprising a Transmembrane Arced Helix (ArcH)" .

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source: Production method: chemical synthesis Host organism: Reptilian orthoreovirus Vector: Not applicable

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ArcH: KKHTIWEVIAGLVALLTFLA FGFWLFKYLQKK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	8
1H chemical shifts	279

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Transmembrane Arced Helix (ArcH)	1

Entities:

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

1

LYS

HIS

THR

ILE

TRP

GLU

VAL

ILE

ALA

2

GLY

LEU

VAL

ALA

LEU

THR

PHE

LEU

ALA

3

PHE

GLY

PHE

TRP

LEU

PHE

LYS

TYR

LEU

GLN

4

LYS

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_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