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- PDB-1ah2: SERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1ah2
TitleSERINE PROTEASE PB92 FROM BACILLUS ALCALOPHILUS, NMR, 18 STRUCTURES
ComponentsSERINE PROTEASE PB92
KeywordsSERINE PROTEASE / SUBTILASE / INDUSTRIAL ENZYME / MAXACAL(TM) / APPLICATION IN WASHING POWDERS
Function / homology
Function and homology information


Hydrolases; Acting on peptide bonds (peptidases); Serine endopeptidases / serine-type endopeptidase activity / proteolysis / extracellular region / metal ion binding
Similarity search - Function
Subtilisin Carlsberg-like catalytic domain / Peptidase S8 propeptide/proteinase inhibitor I9 / Peptidase inhibitor I9 / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8, subtilisin, His-active site / : / Serine proteases, subtilase family, histidine active site. / Serine proteases, subtilase family, aspartic acid active site. / Peptidase S8, subtilisin, Asp-active site ...Subtilisin Carlsberg-like catalytic domain / Peptidase S8 propeptide/proteinase inhibitor I9 / Peptidase inhibitor I9 / Peptidase S8 propeptide/proteinase inhibitor I9 superfamily / Peptidase S8/S53 domain / Peptidase S8, subtilisin, His-active site / : / Serine proteases, subtilase family, histidine active site. / Serine proteases, subtilase family, aspartic acid active site. / Peptidase S8, subtilisin, Asp-active site / Serine proteases, subtilase family, serine active site. / Peptidase S8, subtilisin, Ser-active site / Peptidase S8, subtilisin-related / Serine proteases, subtilase domain profile. / Peptidase S8/S53 domain superfamily / Subtilase family / Peptidase S8/S53 domain / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesBacillus alcalophilus (bacteria)
MethodSOLUTION NMR / DGSA
AuthorsBoelens, R. / Schipper, D. / Martin, J.R. / Karimi-Nejad, Y. / Mulder, F. / Zwan, J.V.D. / Mariani, M.
Citation
Journal: Structure / Year: 1997
Title: The solution structure of serine protease PB92 from Bacillus alcalophilus presents a rigid fold with a flexible substrate-binding site.
Authors: Martin, J.R. / Mulder, F.A. / Karimi-Nejad, Y. / van der Zwan, J. / Mariani, M. / Schipper, D. / Boelens, R.
#1: Journal: J.Biomol.NMR / Year: 1995
Title: Complete 1H, 13C and 15N NMR Assignments and Secondary Structure of the 269-Residue Serine Protease Pb92 from Bacillus Alcalophilus
Authors: Fogh, R.H. / Schipper, D. / Boelens, R. / Kaptein, R.
#2: Journal: J.Biomol.NMR / Year: 1994
Title: 1H, 13C and 15N Assignments of Serine Protease Pb92 from Bacillus Alcalophilus
Authors: Fogh, R. / Schipper, D. / Boelens, R. / Kaptein, R.
History
DepositionApr 11, 1997Processing site: BNL
Revision 1.0Apr 15, 1998Provider: 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 1.4May 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: SERINE PROTEASE PB92


Theoretical massNumber of molelcules
Total (without water)26,7451
Polymers26,7451
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)18 / 20NO NOE AND H-BOND VIOLATIONS > 0.5 A
Representative

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Components

#1: Protein SERINE PROTEASE PB92


Mass: 26745.406 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: INHIBITED BY DFP / Source: (gene. exp.) Bacillus alcalophilus (bacteria) / Strain: PB92 / Production host: Bacillus subtilis (bacteria) / References: UniProt: P27693

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N NOESY-HSQC
1213D 13C NOESY-HSQC

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Sample preparation

Sample conditionspH: 5 / Temperature: 315 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometerType: Varian UNITYPLUS 750 / Manufacturer: Varian / Model: UNITYPLUS 750 / Field strength: 750 MHz

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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: DGSA / Software ordinal: 1
Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL REFERENCE.
NMR ensembleConformer selection criteria: NO NOE AND H-BOND VIOLATIONS > 0.5 A
Conformers calculated total number: 20 / Conformers submitted total number: 18

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