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- PDB-1c3z: THP12-CARRIER PROTEIN FROM YELLOW MEAL WORM -

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Basic information

Entry
Database: PDB / ID: 1c3z
TitleTHP12-CARRIER PROTEIN FROM YELLOW MEAL WORM
ComponentsTHP12 CARRIER PROTEIN
KeywordsANTIFREEZE PROTEIN / EF-HAND / ALL-ALPHA
Function / homology
Function and homology information


Pheromone/general odorant binding protein domain / Insect pheromone/odorant binding protein domains. / Pheromone/general odorant binding protein / PBP/GOBP family / Pheromone/general odorant binding protein superfamily / Recoverin; domain 1 / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
12 kDa hemolymph protein
Similarity search - Component
Biological speciesTenebrio molitor (yellow mealworm)
MethodSOLUTION NMR / MINIMIZED AVERAGE STRUCTURE OF ENSEMBLE OF 23 STRUCTURES
AuthorsSoennichsen, F.D.
Citation
Journal: Structure Fold.Des. / Year: 1999
Title: A new class of hexahelical insect proteins revealed as putative carriers of small hydrophobic ligands.
Authors: Rothemund, S. / Liou, Y.C. / Davies, P.L. / Krause, E. / Sonnichsen, F.D.
#1: Journal: Biochemistry / Year: 1997
Title: Backbone Structure and Dynamics of a Hemolymph Protein from the Mealworm Beetle Tenebrio molitor
Authors: Rothemund, S / Liou, Y.-C. / Davies, P.L. / Soennichsen, F.D.
History
DepositionJul 10, 1999Deposition site: RCSB / Processing site: NDB
Revision 1.0Nov 10, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name
Revision 1.4Dec 27, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: THP12 CARRIER PROTEIN


Theoretical massNumber of molelcules
Total (without water)12,3351
Polymers12,3351
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)1 / -
Representative

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Components

#1: Protein THP12 CARRIER PROTEIN


Mass: 12334.801 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Tenebrio molitor (yellow mealworm)
Description: THIS SEQUENCE OCCURS NATURALLY IN YELLOW MEAL WORM
Plasmid: PET20B / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q27011

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-SEPARATED NOESY
1213D 13C-SEPARATED NOESY
1314D 13C-SEPARATED NOESY
141CBCACONNH
151HN(CA)CB
161HNHA

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Sample preparation

Details
Solution-IDContents
11MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED
21MM PROTEIN, N15- OR N15/C13-DOUBLE LABELED
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1NO SALT 6.9 AMBIENT 25 K
2NO SALT 6.9 AMBIENT 25 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA5002

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Processing

NMR software
NameVersionDeveloperClassification
NMRPipeSGI6X.M4DELAGLIO, F. ET AL.processing
PIPP3.6.8GARRET, D. ET AL.data analysis
X-PLOR3.81BRUENGERstructure solution
X-PLOR3.81BRUENGERrefinement
RefinementMethod: MINIMIZED AVERAGE STRUCTURE OF ENSEMBLE OF 23 STRUCTURES
Software ordinal: 1
NMR ensembleConformers submitted total number: 1

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