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- PDB-1sth: TWO DISTINCTLY DIFFERENT METAL BINDING MODES ARE SEEN IN X-RAY CR... -

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Basic information

Entry
Database: PDB / ID: 1sth
TitleTWO DISTINCTLY DIFFERENT METAL BINDING MODES ARE SEEN IN X-RAY CRYSTAL STRUCTURES OF STAPHYLOCOCCAL NUCLEASE-COBALT(II)-NUCLEOTIDE COMPLEXES
ComponentsSTAPHYLOCOCCAL NUCLEASE
KeywordsHYDROLASE (PHOSPHORIC DIESTER)
Function / homology
Function and homology information


micrococcal nuclease / : / nucleic acid binding / extracellular region / membrane / metal ion binding
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
: / THYMIDINE-3',5'-DIPHOSPHATE / Thermonuclease
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / Resolution: 1.85 Å
AuthorsLoll, P.J. / Quirk, S. / Lattman, E.E.
CitationJournal: Biochemistry / Year: 1995
Title: X-ray crystal structures of staphylococcal nuclease complexed with the competitive inhibitor cobalt(II) and nucleotide.
Authors: Loll, P.J. / Quirk, S. / Lattman, E.E. / Garavito, R.M.
History
DepositionOct 27, 1994Processing site: BNL
Revision 1.0Feb 27, 1995Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 14, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / struct_conn / struct_site
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_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: STAPHYLOCOCCAL NUCLEASE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)17,3043
Polymers16,8431
Non-polymers4612
Water1,04558
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)47.480, 47.480, 63.210
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number76
Space group name H-MP41
Atom site foot note1: CIS PROLINE - PRO 117

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Components

#1: Protein STAPHYLOCOCCAL NUCLEASE


Mass: 16843.330 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / References: UniProt: P00644, micrococcal nuclease
#2: Chemical ChemComp-CO / COBALT (II) ION


Mass: 58.933 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Co
#3: Chemical ChemComp-THP / THYMIDINE-3',5'-DIPHOSPHATE


Type: DNA linking / Mass: 402.188 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H16N2O11P2
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 58 / Source method: isolated from a natural source / Formula: H2O
Nonpolymer detailsCO 142 FORMS A COORDINATE COVALENT LIGAND-METAL BOND WITH ASP 40.

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.11 Å3/Da / Density % sol: 41.82 %
Crystal growDetails: CRYSTAL SOAKED FOR NINE MONTHS AT 277 K IN STABILIZING BUFFER COMPRISING 40% (WW) MPD IN 30 MM TRIS-CL PH 8.15, 50 UM COCL2, 100 UM POTASSIUM CITRATE AND 50 UM PDTP. SOME EVAPORATION ...Details: CRYSTAL SOAKED FOR NINE MONTHS AT 277 K IN STABILIZING BUFFER COMPRISING 40% (WW) MPD IN 30 MM TRIS-CL PH 8.15, 50 UM COCL2, 100 UM POTASSIUM CITRATE AND 50 UM PDTP. SOME EVAPORATION OCCURRED DURING THIS PERIOD, SO MPD CONCENTRATION AT TIME OF DATA COLLECTION, WHILE NOT KNOWN PRECISELY, WAS SUBSTANTIALLY GREATER THAN 40%.
Crystal grow
*PLUS
Temperature: 4 K / pH: 8.15 / Method: vapor diffusion
Details: Loll, P.J., (1989) Proteins Struct. Funct. Genet., 5, 183.
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
120 mg/mlprotein1drop
210.5 mMpotassium phosphate1drop
317 %MPD1drop
42 mg/mlpdTp1drop
510 mM1dropCaCl2
620 mMpotassium citrate1drop
721-23 %(w/w)MPD1reservoir
810.5 mMpotassium phosphate1reservoir

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Data collection

ReflectionNum. obs: 11600 / % possible obs: 99 % / Observed criterion σ(I): 0
Reflection
*PLUS
Highest resolution: 1.85 Å / Lowest resolution: 6 Å / Num. obs: 11570 / Num. measured all: 87667 / Rmerge(I) obs: 0.048

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Processing

Software
NameVersionClassification
X-PLOR3model building
X-PLOR3refinement
X-PLOR3phasing
RefinementResolution: 1.85→6 Å / σ(F): 0
RfactorNum. reflection% reflection
Rwork0.174 --
obs0.174 11570 99 %
Displacement parametersBiso mean: 27 Å2
Refine analyzeLuzzati coordinate error obs: 0.2 Å
Refinement stepCycle: LAST / Resolution: 1.85→6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1087 0 26 58 1171
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.014
X-RAY DIFFRACTIONx_bond_d_na
X-RAY DIFFRACTIONx_bond_d_prot
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_d_na
X-RAY DIFFRACTIONx_angle_d_prot
X-RAY DIFFRACTIONx_angle_deg2.99
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d25.1
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.16
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_scangle_it
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg25.1
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.16

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