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- PDB-2mns: Solution NMR structure of the reovirus p15 fusion-associated smal... -

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Basic information

Entry
Database: PDB / ID: 2mns
TitleSolution NMR structure of the reovirus p15 fusion-associated small transmembrane (FAST) protein fusion-inducing lipid packing sensor (FLiPS) motif in dodecyl phosphocholine (DPC) micelles
ComponentsMembrane fusion protein p15
KeywordsMEMBRANE PROTEIN / P15 FLiPS / FAST Protein / Fusion Protein / Reovirus
Function / homologymembrane / Membrane fusion protein p15
Function and homology information
Biological speciesBaboon orthoreovirus
MethodSOLUTION NMR / torsion angle dynamics
Model detailslowest energy, model1
AuthorsSarker, M. / Duncan, R. / Read, J. / Rainey, J.
CitationJournal: To be Published
Title: Novel helix-loop-helix fusion-inducing lipid packing sensor (FLiPS) for cell-cell fusion
Authors: Read, J. / Clancy, E. / Sarker, M. / Langelaan, D. / Rainey, J. / Duncan, R.
History
DepositionApr 9, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Apr 23, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 16, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_conn / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Membrane fusion protein p15


Theoretical massNumber of molelcules
Total (without water)1,9651
Polymers1,9651
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)50 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein/peptide Membrane fusion protein p15


Mass: 1965.363 Da / Num. of mol.: 1 / Fragment: unp residues 68-87
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Baboon orthoreovirus / Production host: Escherichia coli (E. coli) / References: UniProt: Q918V6
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-1H NOESY
1212D 1H-1H TOCSY
1312D 1H-15N HSQC
1412D 1H-13C HSQC

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Sample preparation

DetailsContents: 1 mM protein_1, 150 mM DPC, 0.5 mM DSS, 0.2 mM sodium azide, 20 mM [U-2H] sodium acetate, 90% H2O/10% D2O
Solvent system: 90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMentity_1-11
150 mMDPC-21
0.5 mMDSS-31
0.2 mMsodium azide-41
20 mMsodium acetate-5[U-2H]1
Sample conditionspH: 5 / Pressure: ambient / Temperature: 310 K

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NMR measurement

NMR spectrometerType: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 700 MHz

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR NIH2.34Schwieters, Kuszewski, Tjandra and Clorerefinement
TopSpin3.1Bruker Biospinprocessing
Sparky3.11Goddardchemical shift assignment
ProcheckNMR3.5.4Laskowski and MacArthurvalidation
UCSF Chimera1.8NIHstructure viewing
MOLMOL2K.2Koradi, Billeter and Wuthrichensemble viewing
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 50

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