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- PDB-1k6y: Crystal Structure of a Two-Domain Fragment of HIV-1 Integrase -

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Basic information

Entry
Database: PDB / ID: 1k6y
TitleCrystal Structure of a Two-Domain Fragment of HIV-1 Integrase
ComponentsIntegrase
KeywordsTRANSFERASE / HIV-1 / integrase / domain organization
Function / homology
Function and homology information


phosphatidylinositol-4,5-bisphosphate binding / induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus ...phosphatidylinositol-4,5-bisphosphate binding / induction by virus of host cysteine-type endopeptidase activity involved in apoptotic process / HIV-1 retropepsin / retroviral ribonuclease H / exoribonuclease H / exoribonuclease H activity / host multivesicular body / DNA integration / RNA-directed DNA polymerase / viral penetration into host nucleus / viral genome integration into host DNA / RNA-directed DNA polymerase activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / establishment of integrated proviral latency / RNA-DNA hybrid ribonuclease activity / suppression by virus of host gene expression / viral entry into host cell / viral nucleocapsid / DNA recombination / lipid binding / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase / aspartic-type endopeptidase activity / DNA-directed DNA polymerase activity / host cell nucleus / host cell plasma membrane / virion membrane / structural molecule activity / RNA binding / DNA binding / zinc ion binding / identical protein binding
Retroviral nucleocapsid protein Gag / Integrase-like, N-terminal / Aspartic peptidase, active site / Zinc finger, CCHC-type / Integrase, catalytic core / Integrase, C-terminal, retroviral / Reverse transcriptase domain / Immunodeficiency lentiviral matrix, N-terminal / Integrase, N-terminal zinc-binding domain / Retrovirus capsid, C-terminal ...Retroviral nucleocapsid protein Gag / Integrase-like, N-terminal / Aspartic peptidase, active site / Zinc finger, CCHC-type / Integrase, catalytic core / Integrase, C-terminal, retroviral / Reverse transcriptase domain / Immunodeficiency lentiviral matrix, N-terminal / Integrase, N-terminal zinc-binding domain / Retrovirus capsid, C-terminal / Retrovirus capsid, N-terminal / Reverse transcriptase connection / Reverse transcriptase thumb / Retroviral matrix protein / Ribonuclease H-like superfamily / Ribonuclease H domain / Matrix protein, lentiviral and alpha-retroviral, N-terminal / Retropepsins / Ribonuclease H superfamily / Integrase Zinc binding domain / Integrase core domain / Aspartic peptidase domain superfamily / Integrase, C-terminal domain superfamily, retroviral / Zinc finger, CCHC-type superfamily / Retropepsin-like catalytic domain / Peptidase A2A, retrovirus, catalytic / Integrase, N-terminal zinc-binding domain / Ribonuclease H-like superfamily/Ribonuclease H / Nucleotidyltransferase; domain 5 / Arc Repressor Mutant, subunit A / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
POL polyprotein / Gag-Pol polyprotein
Biological speciesHuman immunodeficiency virus 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsWang, J. / Ling, H. / Yang, W. / Craigie, R.
CitationJournal: EMBO J. / Year: 2001
Title: Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.
Authors: Wang, J.Y. / Ling, H. / Yang, W. / Craigie, R.
Validation Report
SummaryFull reportAbout validation report
History
DepositionOct 17, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 21, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrase
B: Integrase
C: Integrase
D: Integrase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,07616
Polymers93,2784
Non-polymers79812
Water3,171176
1


TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Integrase
B: Integrase
hetero molecules

C: Integrase
D: Integrase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)94,07616
Polymers93,2784
Non-polymers79812
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation8_675-y+1,-x+2,-z+1/21
Buried area10210 Å2
ΔGint-69 kcal/mol
Surface area35950 Å2
MethodPISA
3
A: Integrase
B: Integrase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,0388
Polymers46,6392
Non-polymers3996
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
4
C: Integrase
D: Integrase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)47,0388
Polymers46,6392
Non-polymers3996
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPQS
Unit cell
γ
α
β
Length a, b, c (Å)102.710, 102.710, 280.560
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein
Integrase /


Mass: 23319.490 Da / Num. of mol.: 4 / Fragment: N-terminal and core domains (Residues 716-927) / Mutation: F185K, W131D, F139D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Production host: Escherichia coli (E. coli)
References: UniProt: Q72498, UniProt: P12497*PLUS, RNA-directed DNA polymerase
#2: Chemical
ChemComp-ZN / ZINC ION / Zinc


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#3: Chemical
ChemComp-K / POTASSIUM ION / Potassium


Mass: 39.098 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: K
#4: Chemical
ChemComp-PO4 / PHOSPHATE ION / Phosphate


Mass: 94.971 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: PO4
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 176 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.97 Å3/Da / Density % sol: 68.99 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 6
Details: 0.7 M NaH2PO4/1.0 K2HPO4, 0.1M Na acetate, pH 6.0, VAPOR DIFFUSION, temperature 277K
Crystal grow
*PLUS
pH: 7.2
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formulaDetails
17 mg/mlprotein1drop
20.5 M1dropNaCl
320 mMHEPES1droppH7.2
40.050 mM1dropZnCl2
55 mMdithiothreitol1drop
60.7 M1reservoirNaH2PO4
71.0 M1reservoirK2HPO4
80.1 Macetate1reservoirpH4.6

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Data collection

DiffractionMean temperature: 173 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X9B / Wavelength: 1.2827 Å
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 8, 2001 / Details: mirrors
RadiationMonochromator: si / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2827 Å / Relative weight: 1
ReflectionResolution: 2.4→30 Å / Num. all: 59673 / Num. obs: 51553 / % possible obs: 86.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -2
Reflection shellResolution: 2.4→2.44 Å / % possible all: 84.4
Reflection
*PLUS
Highest resolution: 2.4 Å / Lowest resolution: 30 Å / Num. obs: 53869 / % possible obs: 90.1 % / Rmerge(I) obs: 0.084
Reflection shell
*PLUS
Highest resolution: 2.4 Å / % possible obs: 84.4 % / Rmerge(I) obs: 0.356

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Processing

Software
NameClassification
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.4→30 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.26 2597 5.037 %RANDOM
Rwork0.233 ---
All0.233 59673 --
Obs0.233 51553 --
Refinement stepCycle: LAST / Resolution: 2.4→30 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5924 0 28 176 6128
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.4 Å / Lowest resolution: 30 Å / σ(F): 0 / Rfactor Rfree: 0.26
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 32.8 Å2
Refine LS restraints
*PLUS
Refinement-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.006
X-RAY DIFFRACTIONc_angle_d
X-RAY DIFFRACTIONc_angle_deg1.34
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_mcbond_it
X-RAY DIFFRACTIONc_scbond_it
X-RAY DIFFRACTIONc_mcangle_it
X-RAY DIFFRACTIONc_scangle_it

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