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- PDB-1xxc: C-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR -

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Basic information

Entry
Database: PDB / ID: 1xxc
TitleC-TERMINAL DOMAIN OF ESCHERICHIA COLI ARGININE REPRESSOR
ComponentsARGININE REPRESSOR
KeywordsDNA BINDING REGULATORY PROTEIN
Function / homology
Function and homology information


regulation of arginine catabolic process / plasmid recombination / regulation of arginine biosynthetic process / negative regulation of DNA-templated transcription initiation / : / positive regulation of DNA-templated transcription initiation / L-arginine biosynthetic process / arginine binding / protein complex oligomerization / cis-regulatory region sequence-specific DNA binding ...regulation of arginine catabolic process / plasmid recombination / regulation of arginine biosynthetic process / negative regulation of DNA-templated transcription initiation / : / positive regulation of DNA-templated transcription initiation / L-arginine biosynthetic process / arginine binding / protein complex oligomerization / cis-regulatory region sequence-specific DNA binding / transcription regulator complex / DNA-binding transcription factor activity / identical protein binding / cytoplasm
Similarity search - Function
Arginine repressor / Arginine repressor, C-terminal / Arginine repressor, DNA-binding domain / Arginine repressor, C-terminal domain superfamily / Arginine repressor, DNA binding domain / Arginine repressor, C-terminal domain / Gyrase A; domain 2 - #40 / Gyrase A; domain 2 / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily ...Arginine repressor / Arginine repressor, C-terminal / Arginine repressor, DNA-binding domain / Arginine repressor, C-terminal domain superfamily / Arginine repressor, DNA binding domain / Arginine repressor, C-terminal domain / Gyrase A; domain 2 - #40 / Gyrase A; domain 2 / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Biological speciesEscherichia coli K12 (bacteria)
MethodX-RAY DIFFRACTION / Resolution: 2.8 Å
AuthorsVan Duyne, G.D. / Ghosh, G. / Maas, W.K. / Sigler, P.B.
Citation
Journal: J.Mol.Biol. / Year: 1996
Title: Structure of the oligomerization and L-arginine binding domain of the arginine repressor of Escherichia coli.
Authors: Van Duyne, G.D. / Ghosh, G. / Maas, W.K. / Sigler, P.B.
#1: Journal: Mol.Microbiol. / Year: 1994
Title: The Arginine Repressor of Escherichia Coli
Authors: Maas, W.K.
#2: Journal: J.Mol.Biol. / Year: 1987
Title: Nucleotide Sequence of the Argr Gene of Escherichia Coli K-12 and Isolation of its Product, the Arginine Repressor
Authors: Lim, D.B. / Oppenheim, J.D. / Eckhardt, T. / Maas, W.K.
History
DepositionNov 3, 1995Processing site: BNL
Revision 1.0Mar 8, 1996Provider: 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 / Other
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ARGININE REPRESSOR
B: ARGININE REPRESSOR
C: ARGININE REPRESSOR
D: ARGININE REPRESSOR
E: ARGININE REPRESSOR
F: ARGININE REPRESSOR


Theoretical massNumber of molelcules
Total (without water)50,1096
Polymers50,1096
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8310 Å2
ΔGint-49 kcal/mol
Surface area17430 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.300, 86.700, 213.700
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein
ARGININE REPRESSOR / ARGR


Mass: 8351.467 Da / Num. of mol.: 6 / Fragment: INITIATOR MET PLUS C-TERMINAL RESIDUES 80 - 156
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli K12 (bacteria) / Species: Escherichia coli / Strain: K-12 / Description: T7 PROMOTER SYSTEM (NOVAGEN) / Gene: T7 / Plasmid: PET3A / Gene (production host): T7 / Production host: Escherichia coli (E. coli) / References: UniProt: P0A6D0

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 50.97 %
Crystal grow
*PLUS
Temperature: 18 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
120 mg/mlprotein1drop
210 mML-arginine1drop
350 mMNaHepes1drop
4100 mM1dropNaCl
520 mM1dropCaCl2
620-25 %MPD1drop

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Data collection

Diffraction sourceWavelength: 1.54
DetectorType: RIGAKU / Detector: IMAGE PLATE
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.54 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 10181 / % possible obs: 90 % / Observed criterion σ(I): -3 / Redundancy: 4.6 % / Rmerge(I) obs: 0.056
Reflection
*PLUS
Rmerge(I) obs: 0.056

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Processing

Software
NameVersionClassification
X-PLOR3.8model building
X-PLOR3.8refinement
DENZOdata reduction
SCALEPACKdata scaling
X-PLOR3.8phasing
RefinementResolution: 2.8→8 Å / σ(F): 3
RfactorNum. reflection
Rfree0.37 -
Rwork0.21 -
obs0.21 8942
Displacement parametersBiso mean: 67 Å2
Refine analyzeLuzzati coordinate error obs: 0.45 Å
Refinement stepCycle: LAST / Resolution: 2.8→8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3234 0 0 0 3234
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.02
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_deg2.2
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.4
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
Software
*PLUS
Name: X-PLOR / Classification: refinement
Refinement
*PLUS
Num. reflection all: 10181 / Rfactor all: 0.233
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.4

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