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- PDB-2lbb: Solution structure of acyl CoA binding protein from Babesia bovis T2Bo -

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Basic information

Entry
Database: PDB / ID: 2lbb
TitleSolution structure of acyl CoA binding protein from Babesia bovis T2Bo
ComponentsAcyl CoA binding protein
KeywordsPROTEIN BINDING / acyl CoA binding protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


fatty-acyl-CoA binding
Similarity search - Function
Acyl-CoA-binding protein, ACBP / Acyl-CoA binding protein superfamily / Acyl CoA binding protein / Acyl-CoA-binding (ACB) domain profile. / Acyl-CoA Binding Protein - #10 / Acyl-CoA Binding Protein / FERM/acyl-CoA-binding protein superfamily / Up-down Bundle / Mainly Alpha
Similarity search - Domain/homology
Acyl CoA binding protein
Similarity search - Component
Biological speciesBabesia bovis (eukaryote)
MethodSOLUTION NMR / torsion angle dynamics
Model detailsfewest violations, model 1
AuthorsYang, F. / Barnwal, R.P. / Varani, G. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To be Published
Title: Solution structure of acyl CoA binding protein from Babesia bovis T2Bo
Authors: Yang, F. / Barnwal, R.P. / Varani, G.
History
DepositionMar 29, 2011Deposition site: BMRB / Processing site: RCSB
Revision 1.0Apr 13, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Sep 28, 2011Group: Structure summary
Revision 1.3Apr 17, 2024Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 15, 2024Group: Database references / Category: database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Acyl CoA binding protein


Theoretical massNumber of molelcules
Total (without water)11,1181
Polymers11,1181
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)10 / 100target function
RepresentativeModel #1fewest violations

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Components

#1: Protein Acyl CoA binding protein


Mass: 11117.602 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Babesia bovis (eukaryote) / Gene: BBOV_IV000490 / Production host: Escherichia coli (E. coli) / References: UniProt: A7AV23

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1222D 1H-13C HSQC
1332D 1H-1H NOESY
1423D CBCA(CO)NH
1523D HNCO
1623D HNCA
1723D HN(CA)CB
1823D HBHA(CO)NH
1923D (H)CCH-TOCSY
11013D 1H-15N NOESY
11123D 1H-13C NOESY
11223D HCACO
11323D 1H-13C NOESY aromatic

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Sample preparation

Details
Solution-IDContentsSolvent system
10.8 mM [U-95% 15N] protein, 20 mM BIS-TRIS, 100 mM sodium chloride, 5 mM DTT, 2 mM EDTA, 90% H2O/10% D2O90% H2O/10% D2O
20.8 mM [U-95% 13C; U-95% 15N] protein, 20 mM BIS-TRIS, 100 mM sodium chloride, 5 mM DTT, 2 mM EDTA, 90% H2O/10% D2O90% H2O/10% D2O
31 mM protein, 20 mM BIS-TRIS, 100 mM sodium chloride, 5 mM DTT, 2 mM EDTA, 100% D2O100% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.8 mMprotein-1[U-95% 15N]1
20 mMBIS-TRIS-21
100 mMsodium chloride-31
5 mMDTT-41
2 mMEDTA-51
0.8 mMprotein-6[U-95% 13C; U-95% 15N]2
20 mMBIS-TRIS-72
100 mMsodium chloride-82
5 mMDTT-92
2 mMEDTA-102
1 mMprotein-113
20 mMBIS-TRIS-123
100 mMsodium chloride-133
5 mMDTT-143
2 mMEDTA-153
Sample conditionspH: 6.5 / Pressure: ambient / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX5001
Bruker AvanceBrukerAVANCE6002

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Processing

NMR software
NameDeveloperClassification
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
MOLMOLKoradi, Billeter and Wuthrichstructure display
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
TopSpinBruker Biospincollection
TALOSCornilescu, Delaglio and Baxdata analysis
CcpNMRCCPNchemical shift assignment
CYANAGuntert, Mumenthaler and Wuthrichrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 10

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