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- PDB-1bhu: THE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR,... -

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Basic information

Entry
Database: PDB / ID: 1bhu
TitleTHE 3D STRUCTURE OF THE STREPTOMYCES METALLOPROTEINASE INHIBITOR, SMPI, ISOLATED FROM STREPTOMYCES NIGRESCENS TK-23, NMR, MINIMIZED AVERAGE STRUCTURE
ComponentsMETALLOPROTEINASE INHIBITOR
KeywordsMETALLOPROTEINASE INHIBITOR
Function / homologyPeptidase inhibitor family I36 / Antimicrobial/protein inhibitor, gamma-crystallin-like / Gamma-B Crystallin; domain 1 - #30 / Gamma-B Crystallin; domain 1 / Gamma-crystallin-like / peptidase inhibitor activity / Sandwich / Mainly Beta / Metalloproteinase inhibitor
Function and homology information
Biological speciesStreptomyces nigrescens (bacteria)
MethodSOLUTION NMR / simulated annealing
AuthorsTate, S. / Ohno, A. / Seeram, S.S. / Hiraga, K. / Oda, K. / Kainosho, M.
Citation
Journal: J.Mol.Biol. / Year: 1998
Title: NMR structure of the Streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure.
Authors: Ohno, A. / Tate, S. / Seeram, S.S. / Hiraga, K. / Swindells, M.B. / Oda, K. / Kainosho, M.
#1: Journal: J.Mol.Biol. / Year: 1998
Title: Elucidation of the Mode of Interaction of Thermolysin with a Proteinaceous Metalloproteinase Inhibitor, Smpi, Based on a Model Complex Structure and a Structural Dynamics Analysis
Authors: Tate, S. / Ohno, A. / Seeram, S.S. / Hiraga, K. / Oda, K. / Kainosho, M.
History
DepositionJun 10, 1998Processing site: BNL
Revision 1.0Jan 6, 1999Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Oct 23, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: METALLOPROTEINASE INHIBITOR


Theoretical massNumber of molelcules
Total (without water)10,3751
Polymers10,3751
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)1 / 60LEAST VIOLATION
RepresentativeModel #1

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Components

#1: Protein METALLOPROTEINASE INHIBITOR / SMPI


Mass: 10374.746 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptomyces nigrescens (bacteria) / Strain: TK-23 / Production host: Escherichia coli (E. coli) / References: UniProt: P01077
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: HETERONUCLEAR MULTI-DIMENSIONAL EXPERIMENT
NMR detailsText: THE STRUCTURE WAS DETEMINED ON THE BASIS OF THE HETERO-NUCLEAR MUTLIDIMENSIONAL NMR TECHNIQUES USING 13C, 15N ENRICHED PROTEINS.

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Sample preparation

DetailsContents: WATER
Sample conditionsIonic strength: NO SALT / pH: 3.3 / Pressure: 1 atm / Temperature: 310 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Bruker DMX500 / Manufacturer: Bruker / Model: DMX500 / Field strength: 500 MHz

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
X-PLOR3.8phasing
NMR software
NameVersionDeveloperClassification
X-PLOR3.8BRUNGERrefinement
X-PLOR3.8structure solution
RefinementMethod: simulated annealing / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE.
NMR ensembleConformer selection criteria: LEAST VIOLATION / Conformers calculated total number: 60 / Conformers submitted total number: 1

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