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- PDB-1k33: Crystal structure analysis of the gp41 core mutant -

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Basic information

Entry
Database: PDB / ID: 1k33
TitleCrystal structure analysis of the gp41 core mutant
ComponentsTransmembrane glycoprotein GP41
KeywordsVIRAL PROTEIN / gp41 / six-helix bundle / trimer-of-hairpins / membrane fusion
Function / homology
Function and homology information


Synthesis and processing of ENV and VPU / symbiont-mediated evasion of host immune response / positive regulation of establishment of T cell polarity / Alpha-defensins / Dectin-2 family / Binding and entry of HIV virion / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / actin filament organization ...Synthesis and processing of ENV and VPU / symbiont-mediated evasion of host immune response / positive regulation of establishment of T cell polarity / Alpha-defensins / Dectin-2 family / Binding and entry of HIV virion / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / actin filament organization / Assembly Of The HIV Virion / Budding and maturation of HIV virion / clathrin-dependent endocytosis of virus by host cell / viral protein processing / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / membrane
Similarity search - Function
Helix Hairpins - #210 / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.75 Å
AuthorsShu, W. / Lu, M.
CitationJournal: Biochemistry / Year: 2002
Title: Interhelical interactions in the gp41 core: implications for activation of HIV-1 membrane fusion.
Authors: Wang, S. / York, J. / Shu, W. / Stoller, M.O. / Nunberg, J.H. / Lu, M.
History
DepositionOct 1, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 10, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Aug 9, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 1.4Oct 27, 2021Group: Database references / Refinement description / Category: database_2 / software / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 1.5Feb 7, 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: Transmembrane glycoprotein GP41


Theoretical massNumber of molelcules
Total (without water)7,8381
Polymers7,8381
Non-polymers00
Water1,20767
1
A: Transmembrane glycoprotein GP41

A: Transmembrane glycoprotein GP41

A: Transmembrane glycoprotein GP41


Theoretical massNumber of molelcules
Total (without water)23,5133
Polymers23,5133
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_555-y,x-y,z1
crystal symmetry operation3_555-x+y,-x,z1
Buried area5190 Å2
ΔGint-40 kcal/mol
Surface area8890 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)51.853, 51.853, 60.700
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number146
Space group name H-MH3
Components on special symmetry positions
IDModelComponents
11A-162-

HOH

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Components

#1: Protein Transmembrane glycoprotein GP41


Mass: 7837.673 Da / Num. of mol.: 1 / Fragment: gp41 ectodomain core / Mutation: I48A
Source method: isolated from a genetically manipulated source
Details: RESIDUES 1 - 34 AND 41 - 68 CONNECTED BY A SIX-RESIDUE LINKER (SER-GLY-GLY-ARG-GLY-GLY)
Source: (gene. exp.) Human immunodeficiency virus 1 / Genus: Lentivirus / Production host: Escherichia coli (E. coli) / References: UniProt: P04578
#2: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 67 / 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: 2 Å3/Da / Density % sol: 38.61 %
Crystal growMethod: vapor diffusion, hanging drop / Details: VAPOR DIFFUSION, HANGING DROP
Crystal grow
*PLUS
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 mg/mlprotein1drop
20.174 M1reservoirNH4Cl
32 %PEG MME40001reservoir

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Data collection

DiffractionMean temperature: 95 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: May 27, 2001 / Details: mirrors
RadiationMonochromator: Ni MIRROR + Ni FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.75→50 Å / Num. all: 6132 / Num. obs: 6132 / % possible obs: 99.4 % / Observed criterion σ(I): 0 / Redundancy: 25.4 % / Biso Wilson estimate: 31.6 Å2 / Rmerge(I) obs: 0.039
Reflection shellResolution: 1.75→1.81 Å / Redundancy: 11.3 % / Rsym value: 0.15 / % possible all: 100
Reflection
*PLUS
Lowest resolution: 50 Å / Num. measured all: 36268
Reflection shell
*PLUS
Mean I/σ(I) obs: 5.7

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Processing

Software
NameVersionClassification
AMoREphasing
CNS1refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.75→25.15 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 729505.71 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0
RfactorNum. reflection% reflectionSelection details
Rfree0.226 669 10.9 %RANDOM
Rwork0.206 ---
all-6132 --
obs-6132 99.4 %-
Solvent computationSolvent model: FLAT MODEL / Bsol: 110.551 Å2 / ksol: 0.460379 e/Å3
Displacement parametersBiso mean: 32.7 Å2
Baniso -1Baniso -2Baniso -3
1--1.29 Å20.48 Å20 Å2
2---1.29 Å20 Å2
3---2.58 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.24 Å0.21 Å
Luzzati d res low-5 Å
Luzzati sigma a0.16 Å0.11 Å
Refinement stepCycle: LAST / Resolution: 1.75→25.15 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms487 0 0 67 554
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_bond_d0.004
X-RAY DIFFRACTIONc_angle_deg0.8
X-RAY DIFFRACTIONc_dihedral_angle_d14.2
X-RAY DIFFRACTIONc_improper_angle_d0.54
X-RAY DIFFRACTIONc_mcbond_it1.451.5
X-RAY DIFFRACTIONc_mcangle_it2.232
X-RAY DIFFRACTIONc_scbond_it2.532
X-RAY DIFFRACTIONc_scangle_it3.812.5
LS refinement shellResolution: 1.75→1.86 Å / Rfactor Rfree error: 0.032 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.339 100 9.6 %
Rwork0.316 942 -
obs--99.7 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PROTEIN_REP.PARAMPROTEIN.TOP
X-RAY DIFFRACTION2WATER_REP.PARAMWATER.TOP
Software
*PLUS
Name: CNS / Version: 1 / Classification: refinement
Refinement
*PLUS
σ(F): 0 / % reflection Rfree: 10.9 % / Rfactor obs: 0.206
Solvent computation
*PLUS
Displacement parameters
*PLUS
Biso mean: 32.7 Å2
Refine LS restraints
*PLUS
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONc_angle_deg0.8
X-RAY DIFFRACTIONc_dihedral_angle_d
X-RAY DIFFRACTIONc_dihedral_angle_deg14.2
X-RAY DIFFRACTIONc_improper_angle_d
X-RAY DIFFRACTIONc_improper_angle_deg0.54
X-RAY DIFFRACTIONc_mcbond_it1.451.5
X-RAY DIFFRACTIONc_scbond_it2.532
X-RAY DIFFRACTIONc_mcangle_it2.232
X-RAY DIFFRACTIONc_scangle_it3.812.5
LS refinement shell
*PLUS
Rfactor Rfree: 0.339 / % reflection Rfree: 9.6 % / Rfactor Rwork: 0.316

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