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- PDB-3zpm: Solution structure of latherin -

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Basic information

Entry
Database: PDB / ID: 3zpm
TitleSolution structure of latherin
ComponentsLATHERIN
KeywordsSURFACTANT PROTEIN / PLUNC / BPI
Function / homology
Function and homology information


surfactant homeostasis / temperature homeostasis / lipid binding / extracellular region
Similarity search - Function
: / Bactericidal permeability-increasing protein; domain 1 / Lipid-binding serum glycoprotein, N-terminal / Bactericidal permeability-increasing protein, alpha/beta domain superfamily / LBP / BPI / CETP family, N-terminal domain / Bactericidal permeability-increasing protein; domain 1 / Super Roll / Alpha Beta
Similarity search - Domain/homology
Biological speciesEQUUS CABALLUS (horse)
MethodSOLUTION NMR / AS PER PUBLICATION
AuthorsVance, S.J. / MacDonald, R.E. / Cooper, A. / Kennedy, M.W. / Smith, B.O.
Citation
Journal: J R Soc Interface / Year: 2013
Title: The structure of latherin, a surfactant allergen protein from horse sweat and saliva.
Authors: Vance, S.J. / McDonald, R.E. / Cooper, A. / Smith, B.O. / Kennedy, M.W.
#1: Journal: Plos One / Year: 2009
Title: Latherin: A Surfactant Protein of Horse Sweat and Saliva.
Authors: McDonald, R.E. / Fleming, R.I. / Beeley, J.G. / Bovell, D.L. / Lu, J.R. / Zhao, X. / Cooper, A. / Kennedy, M.W.
#2: Journal: Ph D Thesis / Year: 2012
Title: The Relationship between Structure and Function in Natural Surfactant Proteins
Authors: Vance, S.J.
History
DepositionFeb 28, 2013Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 26, 2013Provider: repository / Type: Initial release
Revision 1.1Jul 3, 2013Group: Database references
Revision 1.2Jan 15, 2014Group: Database references
Revision 2.0May 2, 2018Group: Atomic model / Data collection / Database references / Category: atom_site / citation / citation_author
Item: _atom_site.Cartn_x / _atom_site.Cartn_y ..._atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _citation.journal_abbrev / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name
Revision 2.1Jun 14, 2023Group: Data collection / Database references / Other
Category: citation / database_2 ...citation / database_2 / pdbx_database_status / pdbx_nmr_software / pdbx_nmr_spectrometer
Item: _citation.country / _database_2.pdbx_DOI ..._citation.country / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_cs / _pdbx_database_status.status_code_mr / _pdbx_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model
Revision 2.2Nov 13, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: LATHERIN


Theoretical massNumber of molelcules
Total (without water)22,9101
Polymers22,9101
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein LATHERIN / DANDER ALLERGEN EQU C 4/EQU C 5 / EQU C 4


Mass: 22910.354 Da / Num. of mol.: 1 / Fragment: RESIDUES 21-228
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) EQUUS CABALLUS (horse) / Plasmid: PET-32 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P82615
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-HSQC
121CBCA(CO)NH
131CC(CO)NH
141HN(CA)CB
151HN(CA)CO
161HNCO
171HBHA(CO)NH
181HBHANH
191(H)CC(CO)NH
1101BMX C NOESY
1111C HSQC B
1121CH3 TOCSY
1131H(CCO)NH B MX N NOESY
1141CHCH3 TOCSY
1151H(CCO)NH
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED LATHERIN.

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Sample preparation

DetailsContents: 95% H2O/5% D2O
Sample conditionsIonic strength: 0.07 / pH: 7.5 / Pressure: 1.0 atm / Temperature: 310.0 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CNSBRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE- KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,READ, RICE,SIMONSON,WARRENrefinement
CcpNmr Analysis2.1structure solution
CcpNmr Analysis2.2structure solution
CcpNmr Analysis2structure solution
DANGLE1.1structure solution
TopSpin1.3structure solution
CNS1.2structure solution
RefinementMethod: AS PER PUBLICATION / Software ordinal: 1
Details: REFINEMENT USING NOE, H-BOND AND RDC RESTRAINTS USING ARIA2 AND CNS. DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 100 / Conformers submitted total number: 20

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