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- PDB-1qp2: SOLUTION STRUCTURE OF PHOTOSYSTEM I ACCESSORY PROTEIN E FROM THE ... -

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Basic information

Entry
Database: PDB / ID: 1qp2
TitleSOLUTION STRUCTURE OF PHOTOSYSTEM I ACCESSORY PROTEIN E FROM THE CYANOBACTERIUM NOSTOC SP. STRAIN PCC 8009
ComponentsPROTEIN (PSAE PROTEIN)
KeywordsELECTRON TRANSPORT / MAINLY BETA / ROLL / PLECKSTRIN TOPOLOGY / SH3-LIKE
Function / homology
Function and homology information


photosystem I reaction center / plasma membrane-derived thylakoid membrane / photosynthesis
Similarity search - Function
SH3 type barrels. - #50 / Photosystem I PsaE, reaction centre subunit IV / Photosystem I reaction centre subunit IV / PsaE / Electron transport accessory-like domain superfamily / SH3 type barrels. / Roll / Mainly Beta
Similarity search - Domain/homology
Photosystem I reaction center subunit IV
Similarity search - Component
Biological speciesNostoc sp. (bacteria)
MethodSOLUTION NMR / distance geometry simulated annealing, molecular dynamics
Model type detailsminimized average
AuthorsMayer, K.L. / Shen, G. / Bryant, D.A. / Lecomte, J.T.J. / Falzone, C.J.
CitationJournal: Biochemistry / Year: 1999
Title: The solution structure of photosystem I accessory protein E from the cyanobacterium Nostoc sp. strain PCC 8009.
Authors: Mayer, K.L. / Shen, G. / Bryant, D.A. / Lecomte, J.T. / Falzone, C.J.
History
DepositionMay 29, 1999Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 20, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Source and taxonomy / Version format compliance
Revision 1.3May 1, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PROTEIN (PSAE PROTEIN)


Theoretical massNumber of molelcules
Total (without water)7,9691
Polymers7,9691
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)1 / 100structures with the lowest energy
RepresentativeModel #1minimized average structure

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Components

#1: Protein PROTEIN (PSAE PROTEIN)


Mass: 7969.069 Da / Num. of mol.: 1 / Fragment: FULL LENGTH / Mutation: WILD-TYPE
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Nostoc sp. (bacteria) / Strain: PCC 8009 / Plasmid: PET3D / Production host: Escherichia coli (E. coli) / References: UniProt: Q9WWP1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
1213D 15N-separated NOESY
1313D 13C-separated NOESY
141J-MODULATED HSQC
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy.

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Sample preparation

CrystalDescription: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.
DetailsContents: NO BUFFER OR ADDED SALT
Sample conditionsIonic strength: NO BUFFER OR ADDED SALT / pH: 6.1 / Pressure: ambient / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker AMX2 / Manufacturer: Bruker / Model: AMX2 / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.851model building
X-PLOR3.851refinement
X-PLOR3.851phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.85Brungerstructure calculation
XwinNMR2Brukercollection
Felix95MSIprocessing
X-PLOR3.85Brungerrefinement
X-PLOR3.85Brungerstructure solution
RefinementMethod: distance geometry simulated annealing, molecular dynamics
Software ordinal: 1
Details: 966 distance restraints 73 dihedral angle restraints 54 distance retraints from hydrogen bonds
NMR representativeSelection criteria: minimized average structure
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 1

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