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- PDB-1k19: NMR Solution Structure of the Chemosensory Protein CSP2 from Moth... -

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Basic information

Entry
Database: PDB / ID: 1k19
TitleNMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae
ComponentsChemosensory Protein CSP2
KeywordsLIPID TRANSPORT / Chemosensory / Pheromone
Function / homologyAntennal chemosensory protein a6 / Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3 / Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3 / Insect odorant-binding protein A10/Ejaculatory bulb-specific protein 3 superfamily / Insect pheromone-binding family, A10/OS-D / Orthogonal Bundle / Mainly Alpha / Chemosensory protein
Function and homology information
Biological speciesMamestra brassicae (cabbage moth)
MethodSOLUTION NMR
AuthorsMosbah, A. / Campanacci, V. / Lartigue, A. / Tegoni, M. / Cambillau, C. / Darbon, H.
Citation
Journal: BIOCHEM.J. / Year: 2003
Title: Solution structure of a chemosensory protein from the moth Mamestra brassicae
Authors: Mosbah, A. / Campanacci, V. / Lartigue, A. / Tegoni, M. / Cambillau, C. / Darbon, H.
#1: Journal: Eur.J.Biochem. / Year: 2001
Title: Chemosensory Protein from the moth Mamestra brassicae. Expression and secondary structure from 1H and 15N NMR
Authors: Campanacci, V. / Mosbah, A. / Bornet, O. / Wechselberger, R. / Jacquin-Joly, E. / Cambillau, C. / Darbon, H. / Tegoni, M.
History
DepositionSep 24, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 4, 2002Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 23, 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 1.4Nov 13, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Chemosensory Protein CSP2


Theoretical massNumber of molelcules
Total (without water)13,0951
Polymers13,0951
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)20 / 50structures with acceptable covalent geometry, structures with favorable non-bond energy, structures with the least restraint violations, structures with the lowest energy, target function
RepresentativeModel #1fewest violations,lowest energy

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Components

#1: Protein Chemosensory Protein CSP2


Mass: 13094.840 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mamestra brassicae (cabbage moth) / Production host: Escherichia coli (E. coli) / References: UniProt: Q9NG96
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D NOESY
2213D 15N-separated NOESY
2323D 15N-separated NOESY
141DQF-COSY
NMR detailsText: This structure was determined using standard 2D homonuclear techniques combined with 3D Heteronuclear techniques.

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Sample preparation

Details
Solution-IDContents
12 mM of unlabeled protein, in 90% H2O and 10% D2O containing 10mM of sodium phosphate buffer, 25 mM NaCl at pH 6.9
21 mM of uniformly labeled protein, in 90% H2O and 10% D2O containing 10mM of sodium phosphate buffer, 25 mM NaCl at pH 6.9
Sample conditionspH: 6.9 / Pressure: ambient / Temperature: 296 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX5001
Varian INOVAVarianINOVA7502

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Processing

NMR software
NameVersionClassification
XwinNMR2.1collection
XEASY1.3.13data analysis
NMRPipe1.8processing
DIANA2.8structure solution
DYANA1.5data analysis
MOLMOL2.6processing
CNS1refinement
Turbo-FrodoMarch 2001 release adata analysis
NMR representativeSelection criteria: fewest violations,lowest energy
NMR ensembleConformer selection criteria: structures with acceptable covalent geometry, structures with favorable non-bond energy, structures with the least restraint violations, structures with the lowest energy, target function
Conformers calculated total number: 50 / Conformers submitted total number: 20

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