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- PDB-2mrl: Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR stru... -

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Basic information

Entry
Database: PDB / ID: 2mrl
TitleBackbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264
ComponentsUncharacterized protein BTH I2711
KeywordsUNKNOWN FUNCTION / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID
Function / homologyDNA polymerase; domain 1 - #610 / : / Uncharacterized protein BTH_I2711-like / DNA polymerase; domain 1 / Orthogonal Bundle / Mainly Alpha / Uncharacterized protein
Function and homology information
Biological speciesBurkholderia thailandensis E264 (bacteria)
MethodSOLUTION NMR / torsion angle dynamics
Model detailslowest energy, model 1
AuthorsBarnwal, R. / Varani, G. / Seattle Structural Genomics Center for Infectious Disease (SSGCID)
CitationJournal: To be Published
Title: NMR structure for potential drug target from Burkholderia thailandensis E264
Authors: Barnwal, R. / Varani, G.
History
DepositionJul 9, 2014Deposition site: BMRB / Processing site: RCSB
Revision 1.0Jul 30, 2014Provider: 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: Uncharacterized protein BTH I2711


Theoretical massNumber of molelcules
Total (without water)8,1331
Polymers8,1331
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 / 200target function
RepresentativeModel #1lowest energy

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Components

#1: Protein Uncharacterized protein BTH I2711


Mass: 8133.304 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Burkholderia thailandensis E264 (bacteria)
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301 / Gene: BTH_I2711 / Production host: Escherichia coli (E. coli) / References: UniProt: Q2SV23

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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

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Sample preparation

DetailsContents: 7.2 mg/mL [U-95% 13C; U-95% 15N] protein BTH I2711, 95% H2O/5% D2O
Solvent system: 95% H2O/5% D2O
SampleConc.: 7.2 mg/mL / Component: protein BTH_I2711 / Isotopic labeling: [U-95% 13C; U-95% 15N]
Sample conditionspH: 7 / 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 Wuthrichrefinement
CYANAGuntert, Mumenthaler and Wuthrichstructure solution
TALOSCornilescu, Delaglio and Baxdata analysis
CCPNMRCCPNchemical shift assignment
CCPNMRCCPNdata analysis
CCPNMRCCPNpeak picking
TopSpinBruker Biospincollection
TopSpinBruker Biospinprocessing
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: 20

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