BMRB Entry 18655
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PDB ID:
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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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
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 8 |
| 1H chemical shifts | 279 |
Additional metadata:
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 | LYS | HIS | THR | ILE | TRP | GLU | VAL | ILE | ALA | ||||
| 2 | GLY | LEU | VAL | ALA | LEU | LEU | THR | PHE | LEU | ALA | ||||
| 3 | PHE | GLY | PHE | TRP | LEU | PHE | LYS | TYR | LEU | GLN | ||||
| 4 | LYS | 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
Related Database Links:
| PDB |
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