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- PDB-1ab7: NMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL E... -

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Basic information

Entry
Database: PDB / ID: 1ab7
TitleNMR 15N RELAXATION AND STRUCTURAL STUDIES REVEAL CONFORMATIONAL EXCHANGE IN BARSTAR C40/82A, 30 STRUCTURES
ComponentsBARSTAR
KeywordsRIBONUCLEASE INHIBITOR
Function / homologyBarstar-like / Barstar (barnase inhibitor) / Barstar (barnase inhibitor) / Barstar-like superfamily / Barnase; Chain D / 2-Layer Sandwich / cytoplasm / Alpha Beta / Barstar
Function and homology information
Biological speciesBacillus amyloliquefaciens (bacteria)
MethodSOLUTION NMR / DISTANCE GEOMETRY - SIMULATED ANNEALING
AuthorsWong, K.B. / Fersht, A.R. / Freund, S.M.V.
Citation
Journal: J.Mol.Biol. / Year: 1997
Title: NMR 15N relaxation and structural studies reveal slow conformational exchange in barstar C40/82A.
Authors: Wong, K.B. / Fersht, A.R. / Freund, S.M.
#1: Journal: Trends Biochem.Sci. / Year: 1989
Title: Barnase and Barstar: Two Small Proteins to Fold and Fit Together
Authors: Hartley, R.W.
History
DepositionFeb 4, 1997Processing site: BNL
Revision 1.0Sep 4, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 3, 2021Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / 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.process_site / _struct_ref_seq_dif.details
Revision 1.4May 22, 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: BARSTAR


Theoretical massNumber of molelcules
Total (without water)10,1571
Polymers10,1571
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)30 / 150LEAST RESTRAINT VIOLATION
Representative

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Components

#1: Protein BARSTAR


Mass: 10157.412 Da / Num. of mol.: 1 / Mutation: C40A, C82A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Bacillus amyloliquefaciens (bacteria) / Production host: Escherichia coli (E. coli) / References: UniProt: P11540

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: NOESY
NMR detailsText: THE STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON THE 13C, 15N-LABELED BARSTAR MUTANT C40A,C82A

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Sample preparation

Sample conditionspH: 6.7 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMX 500BrukerAMX 5005001
Bruker AMX2 600BrukerAMX2 6006002

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.1BRUNGERrefinement
X-PLOR3.1structure solution
RefinementMethod: DISTANCE GEOMETRY - SIMULATED ANNEALING / Software ordinal: 1
NMR ensembleConformer selection criteria: LEAST RESTRAINT VIOLATION / Conformers calculated total number: 150 / Conformers submitted total number: 30

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