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- PDB-2sob: SN-OB, OB-FOLD SUB-DOMAIN OF STAPHYLOCOCCAL NUCLEASE, NMR, 10 STR... -

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Entry
Database: PDB / ID: 2sob
TitleSN-OB, OB-FOLD SUB-DOMAIN OF STAPHYLOCOCCAL NUCLEASE, NMR, 10 STRUCTURES
ComponentsSTAPHYLOCOCCAL NUCLEASE
KeywordsHYDROLASE (PHOSPHORIC DIESTER)
Function / homology
Function and homology information


micrococcal nuclease / : / nucleic acid binding / extracellular region / metal ion binding / membrane
Similarity search - Function
OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #90 / Thermonuclease family signature 1. / Thermonuclease active site / Thermonuclease family signature 2. / Staphylococcal nuclease (SNase-like), OB-fold / Staphylococcal nuclease homologue / Thermonuclease domain profile. / Staphylococcal nuclease homologues / SNase-like, OB-fold superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) ...OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #90 / Thermonuclease family signature 1. / Thermonuclease active site / Thermonuclease family signature 2. / Staphylococcal nuclease (SNase-like), OB-fold / Staphylococcal nuclease homologue / Thermonuclease domain profile. / Staphylococcal nuclease homologues / SNase-like, OB-fold superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
Biological speciesStaphylococcus aureus (bacteria)
MethodSOLUTION NMR
AuthorsAlexandrescu, A.T. / Gittis, A.G. / Abeygunawardana, C. / Shortle, D.
Citation
Journal: J.Mol.Biol. / Year: 1995
Title: NMR structure of a stable "OB-fold" sub-domain isolated from staphylococcal nuclease.
Authors: Alexandrescu, A.T. / Gittis, A.G. / Abeygunawardana, C. / Shortle, D.
#1: Journal: Structure / Year: 1993
Title: NMR Analysis of the Residual Structure in the Denatured State of an Unusual Mutant of Staphylococcal Nuclease
Authors: Shortle, D. / Abeygunawardana, C.
#2: Journal: Biochemistry / Year: 1989
Title: Residual Structure in Large Fragments of Staphylococcal Nuclease: Effects of Amino Acid Substitution
Authors: Shortle, D. / Meeker, A.K.
History
DepositionSep 15, 1995Processing site: BNL
SupersessionDec 7, 1995ID: 1SOB
Revision 1.0Dec 7, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 25, 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: STAPHYLOCOCCAL NUCLEASE


Theoretical massNumber of molelcules
Total (without water)11,6271
Polymers11,6271
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / -
Representative

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Components

#1: Protein STAPHYLOCOCCAL NUCLEASE / SN-OB / STAPHYLOCOCCAL NUCLEASE OB-SUBDOMAIN


Mass: 11626.583 Da / Num. of mol.: 1 / Mutation: V66L, G88V, DEL(104-109)
Source method: isolated from a genetically manipulated source
Details: 1 - 103 FRAGMENT OF THE 149 AMINO ACID STAPHYLOCOCCAL NUCLEASE CONTAINING THE "GLOBAL SUPPRESSOR" MUTATIONS V66L AND G88V
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Strain: FOGGI / Gene: STAPHYLOCOCCAL NUCLEASE / Plasmid: PET11A T7
Gene (production host): STAPHYLOCOCCAL NUCLEASE MUTANT/FRAGMENT
Production host: Escherichia coli (E. coli) / References: UniProt: P00644, micrococcal nuclease

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR

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Sample preparation

Crystal grow
*PLUS
Method: other

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Processing

Software
NameVersionClassification
X-PLOR3.1model building
X-PLOR3.1refinement
X-PLOR3.1phasing
NMR softwareName: X-PLOR / Version: 3.1 / Developer: BRUNGER / Classification: refinement
NMR ensembleConformers submitted total number: 10

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