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- PDB-1a9v: TERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2,... -

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Basic information

Entry
Database: PDB / ID: 1a9v
TitleTERTIARY STRUCTURE OF THE MAJOR HOUSE DUST MITE ALLERGEN DER P 2, NMR, 10 STRUCTURES
ComponentsMITE ALLERGEN DER P 2
KeywordsALLERGEN / IMMUNOGLOBULIN FOLD
Function / homology
Function and homology information


sterol transport / sterol binding / extracellular region
Similarity search - Function
Sterol transport protein NPC2-like / Immunoglobulin-like - #770 / ML domain / MD-2-related lipid-recognition domain / Domain involved in innate immunity and lipid metabolism. / Immunoglobulin E-set / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Mite group 2 allergen Der p 2
Similarity search - Component
Biological speciesDermatophagoides pteronyssinus (European house dust mite)
MethodSOLUTION NMR / DISTANCE GEOMETRY, SIMULATED ANNEAL
AuthorsMueller, G.A. / Benjamin, D.C. / Rule, G.S.
Citation
Journal: Biochemistry / Year: 1998
Title: Tertiary structure of the major house dust mite allergen Der p 2: sequential and structural homologies.
Authors: Mueller, G.A. / Benjamin, D.C. / Rule, G.S.
#1: Journal: J.Biol.Chem. / Year: 1997
Title: Expression and Secondary Structure Determination by NMR Methods of the Major House Dust Mite Allergen Der P 2
Authors: Mueller, G.A. / Smith, A.M. / Williams Junior, D.C. / Hakkaart, G.A. / Aalberse, R.C. / Chapman, M.D. / Rule, G.S. / Benjamin, D.C.
History
DepositionApr 10, 1998Processing site: BNL
Revision 1.0Oct 14, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site / _pdbx_nmr_software.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: MITE ALLERGEN DER P 2


Theoretical massNumber of molelcules
Total (without water)14,1141
Polymers14,1141
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200LOWEST ENERGY
Representative

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Components

#1: Protein MITE ALLERGEN DER P 2


Mass: 14114.336 Da / Num. of mol.: 1 / Mutation: D1S
Source method: isolated from a genetically manipulated source
Details: D1S MUTANT MADE TO ENHANCE N-TERMINAL MET REMOVAL
Source: (gene. exp.) Dermatophagoides pteronyssinus (European house dust mite)
Cell line: BL21 / Plasmid: PET-21A / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (PLYSE) / References: UniProt: P49278

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCA
121CA(CO)HN
131HN(CA)HA
141HA(CACO)NH
151HN(CA)CB
161CBCA(CO)NH
171HNCO
181CBACOHA
191HBHA(CACO)NH
1101(H)CCH-TOCSY
1111HSQC-NOESY
1121CHH-NOESY
1131HCH-NOESY
1141NHNH-NOESY
1151CN-NOESY
NMR detailsText: STRUCTURE WAS DETERMINED USING DOUBLE LABELED MATERIAL AND TRIPLE RESONANCE METHODS

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Sample preparation

DetailsContents: 90 H2O/10 D2O
Sample conditionsIonic strength: 50 mM NACL 100 mM K2SO4 / pH: 6.0 / Pressure: 1 atm / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS / Manufacturer: Varian / Model: UNITYPLUS / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
X-PLOR3.8phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.821BRUNGERrefinement
Felixstructure solution
X-PLOR3.821structure solution
RefinementMethod: DISTANCE GEOMETRY, SIMULATED ANNEAL / Software ordinal: 1 / Details: CONVENTIONAL
NMR ensembleConformer selection criteria: LOWEST ENERGY / Conformers calculated total number: 200 / Conformers submitted total number: 10

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