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- PDB-1ckv: STRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B -

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Basic information

Entry
Database: PDB / ID: 1ckv
TitleSTRUCTURE OF THE SOLUBLE METHANE MONOOXYGENASE REGULATORY PROTEIN B
ComponentsPROTEIN (PROTEIN B)
KeywordsHYDROXYLASE REGULATORY PROTEIN
Function / homology
Function and homology information


cellular aromatic compound metabolic process / monooxygenase activity
Similarity search - Function
Monooxygenase component MmoB/DmpM / Phenol Hydroxylase P2 Protein / Monooxygenase component MmoB/DmpM / Monooxygenase component MmoB/DmpM superfamily / MmoB/DmpM family / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Methane monooxygenase regulatory protein B
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
MethodSOLUTION NMR / simulated annealing
AuthorsWalters, K.J. / Gassner, G.T. / Lippard, S.J. / Wagner, G.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 1999
Title: Structure of the soluble methane monooxygenase regulatory protein B.
Authors: Walters, K.J. / Gassner, G.T. / Lippard, S.J. / Wagner, G.
History
DepositionApr 25, 1999Deposition site: BNL / Processing site: RCSB
Revision 1.0Jul 7, 1999Provider: repository / Type: Initial release
Revision 1.1Apr 26, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 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 1.4Dec 27, 2023Group: 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: PROTEIN (PROTEIN B)


Theoretical massNumber of molelcules
Total (without water)16,0001
Polymers16,0001
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)14 / 20NO NOE VIOLOTION GREATER THAN 0.5 ANGSTROMS AND NO DIHEDRAL ANGLE VIOLATION GREATER THAN 5 DEGREES.
Representative

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Components

#1: Protein PROTEIN (PROTEIN B)


Mass: 15999.864 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) / References: UniProt: P18797

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
111HNCO
121HN(CA)CO
131HNCA
141HN(CO)CA
151HNHA
161(H)CCH-TOCSY
171HC(CO)NH
181H(CCO)NH
191HNHB
1101HNHA
1111NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING 3D HETERONUCLEAR AND 2D HOMONUCLEAR NMR SPECTROSCOPY.

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Sample preparation

DetailsContents: 4 MM PEFAPLOC
Sample conditionsIonic strength: 50 mM PHOSPHATE / pH: 6.5 / Temperature: 298 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian DMX600VarianDMX6007501
Bruker INOVA750BrukerINOVA7506002
Bruker U500BrukerU5005003
Bruker INOVA500BrukerINOVA5005004

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Processing

NMR software
NameVersionDeveloperClassification
X-PLOR3.851BRUNGERrefinement
Felixstructure solution
EASYstructure solution
TALOSstructure solution
XPLORstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE
NMR ensembleConformer selection criteria: NO NOE VIOLOTION GREATER THAN 0.5 ANGSTROMS AND NO DIHEDRAL ANGLE VIOLATION GREATER THAN 5 DEGREES.
Conformers calculated total number: 20 / Conformers submitted total number: 14

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