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- PDB-2n57: NMR structure of Acyl carrier protein from Brucella melitensis -

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Basic information

Entry
Database: PDB / ID: 2n57
TitleNMR structure of Acyl carrier protein from Brucella melitensis
ComponentsAcyl carrier protein
KeywordsLIPID BINDING PROTEIN / acyl carrier protein / Brucella melitensis / structural genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homology
Function and homology information


phosphopantetheine binding / acyl carrier activity / cytoplasm
Similarity search - Function
Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Acyl carrier protein (ACP) / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain
Similarity search - Domain/homology
Acyl carrier protein / Acyl carrier protein
Similarity search - Component
Biological speciesBrucella melitensis bv. 3 str. Ether (bacteria)
MethodSOLUTION NMR / torsion angle dynamics
Model detailslowest energy, model1
AuthorsBarnwal, R. / Varani, G. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To be Published
Title: NMR structure of Acyl carrier protein from Brucella melitensis.
Authors: Barnwal, R. / Varani, G.
History
DepositionJul 8, 2015Deposition site: BMRB / Processing site: RCSB
SupersessionJul 22, 2015ID: 2L3V
Revision 1.0Jul 22, 2015Provider: repository / Type: Initial release
Revision 1.1May 1, 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
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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Acyl carrier protein


Theoretical massNumber of molelcules
Total (without water)8,3081
Polymers8,3081
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 / 200target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Acyl carrier protein / ACP


Mass: 8308.197 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Brucella melitensis bv. 3 str. Ether (bacteria)
Gene: acpP, BAOG_00187 / Production host: Escherichia coli (E. coli) / References: UniProt: D1F788, UniProt: A0A0J9WZH6*PLUS

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1112D 1H-15N HSQC
1212D 1H-13C HSQC
1313D CBCA(CO)NH
1413D HNCO
1513D HN(CA)CB
1613D HBHA(CO)NH
1713D C(CO)NH
1813D H(CCO)NH
1913D 1H-15N NOESY
11013D 1H-13C NOESY aliphatic

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Sample preparation

DetailsContents: 1.2-1.4 mM [U-95% 13C; U-95% 15N] Acyl carrier protein, 93% H2O/7% D2O
Solvent system: 93% H2O/7% D2O
SampleUnits: mM / Component: Acyl carrier protein-1 / Isotopic labeling: [U-95% 13C; U-95% 15N] / Conc. range: 1.2-1.4
Sample conditionspH: 7 / Pressure: ambient / Temperature: 298 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
NameDeveloperClassification
NMRPipeDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
CCPNMRCCPNchemical shift assignment
CCPNMRCCPNdata analysis
CCPNMRCCPNpeak picking
TopSpinBruker Biospincollection
TopSpinBruker Biospinprocessing
CYANAGuntert, Mumenthaler and Wuthrichgeometry optimization
CYANAGuntert, Mumenthaler and Wuthrichrefinement
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 200 / Conformers submitted total number: 10

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