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- PDB-2lc1: Rv0020c_FHA Structure -

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Basic information

Entry
Database: PDB / ID: 2lc1
TitleRv0020c_FHA Structure
ComponentsPutative uncharacterized protein TB39.8
KeywordsPROTEIN BINDING / FhaA / KINASE SUBSTRATE
Function / homology
Function and homology information


peptidoglycan-based cell wall / mRNA binding / cytosol
Similarity search - Function
FhaA, N-terminal domain / FhaA, N-terminal domain superfamily / FhaA, N-terminal domain / : / Tumour Suppressor Smad4 - #20 / Tumour Suppressor Smad4 / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Forkhead-associated (FHA) domain ...FhaA, N-terminal domain / FhaA, N-terminal domain superfamily / FhaA, N-terminal domain / : / Tumour Suppressor Smad4 - #20 / Tumour Suppressor Smad4 / Forkhead associated domain / Forkhead-associated (FHA) domain profile. / FHA domain / Forkhead-associated (FHA) domain / SMAD/FHA domain superfamily / Sandwich / Mainly Beta
Similarity search - Domain/homology
FHA domain-containing protein FhaA
Similarity search - Component
Biological speciesMycobacterium tuberculosis (bacteria)
MethodSOLUTION NMR / simulated annealing
Model detailslowest energy, model 1
AuthorsBarthe, P.P. / Cohen-Gonsaud, M.M. / Roumestand, C.C.
CitationJournal: Structure / Year: 2011
Title: Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase
Authors: Roumestand, C. / Leiba, J. / Galophe, N. / Margeat, E. / Padilla, A. / Bessin, Y. / Barthe, P. / Molle, V. / Cohen-Gonsaud, M.
History
DepositionApr 11, 2011Deposition site: BMRB / Processing site: PDBJ
Revision 1.0Nov 2, 2011Provider: repository / Type: Initial release
Revision 1.1Jun 14, 2023Group: Data collection / Database references / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / 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_database_status.status_code_nmr_data / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.2May 29, 2024Group: 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: Putative uncharacterized protein TB39.8


Theoretical massNumber of molelcules
Total (without water)10,8881
Polymers10,8881
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)30 / 200structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Putative uncharacterized protein TB39.8 / FhaA


Mass: 10887.962 Da / Num. of mol.: 1 / Fragment: UNP residues 430-527
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Strain: H37rv / Gene: Rv0020c, TB39.8 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P71590

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 1H-15N NOESY
1213D 1H-15N TOCSY
1323D HNCA
1423D CBCA(CO)NH
1523D HN(CA)CB
1623D HNCO
1723D HCACO

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Sample preparation

Details
Solution-IDContentsSolvent system
10.5 mM [U-15N] Rv0020c_FHA-1, 95% H2O/5% D2O95% H2O/5% D2O
20.5 mM [U-13C; U-15N] Rv0020c_FHA-2, 95% H2O/5% D2O95% H2O/5% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
0.5 mMRv0020c_FHA-1[U-15N]1
0.5 mMRv0020c_FHA-2[U-13C; U-15N]2
Sample conditionsIonic strength: 100 / pH: 6.8 / Pressure: ambient / Temperature: 293 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AvanceBrukerAVANCE7001
Bruker AvanceBrukerAVANCE5002

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Processing

NMR software
NameVersionDeveloperClassification
Gifa4.44Delsucprocessing
CYANA2.1Guntert, Mumenthaler and Wuthrichstructure solution
CNS1.2Brunger, Adams, Clore, Gros, Nilges and Readrefinement
TALOS+1.2009.0721.18Cornilescu, Delaglio and Baxangle prediction
RefinementMethod: simulated annealing / Software ordinal: 1 / Details: Water refinement with RECOORD scripts
NMR constraintsNOE constraints total: 1296 / NOE intraresidue total count: 327 / NOE long range total count: 416 / NOE medium range total count: 137 / NOE sequential total count: 416 / Hydrogen bond constraints total count: 64 / Protein phi angle constraints total count: 76 / Protein psi angle constraints total count: 76
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 200 / Conformers submitted total number: 30 / Representative conformer: 1

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