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- PDB-3mlz: Crystal structure of anti-HIV-1 V3 Fab 3074 in complex with a VI1... -

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Basic information

Entry
Database: PDB / ID: 3mlz
TitleCrystal structure of anti-HIV-1 V3 Fab 3074 in complex with a VI191 V3 peptide
Components
  • HIV-1 gp120 third variable region (V3) crown
  • Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab heavy chain
  • Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab light chain
KeywordsIMMUNE SYSTEM / human monoclonal antibody / Fab / HIV-1 / gp120 / third variable loop / antibody-antigen interaction
Function / homology
Function and homology information


membrane fusion involved in viral entry into host cell / symbiont entry into host cell / viral envelope / virion attachment to host cell / virion membrane
Similarity search - Function
Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Envelope glycoprotein
Similarity search - Component
Biological speciesHomo sapiens (human)
Human immunodeficiency virus 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.99 Å
AuthorsKong, X.-P.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2010
Title: Conserved structural elements in the V3 crown of HIV-1 gp120.
Authors: Jiang, X. / Burke, V. / Totrov, M. / Williams, C. / Cardozo, T. / Gorny, M.K. / Zolla-Pazner, S. / Kong, X.P.
History
DepositionApr 18, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 14, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software
Item: _software.classification / _software.contact_author ..._software.classification / _software.contact_author / _software.contact_author_email / _software.date / _software.language / _software.location / _software.name / _software.type / _software.version
Revision 1.3Nov 27, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
L: Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab light chain
H: Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab heavy chain
P: HIV-1 gp120 third variable region (V3) crown


Theoretical massNumber of molelcules
Total (without water)49,7663
Polymers49,7663
Non-polymers00
Water3,387188
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5210 Å2
ΔGint-27 kcal/mol
Surface area21270 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.413, 100.413, 177.757
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522

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Components

#1: Antibody Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab light chain


Mass: 22662.156 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#2: Antibody Human monoclonal anti-HIV-1 gp120 V3 antibody 3074 Fab heavy chain


Mass: 24468.215 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human)
#3: Protein/peptide HIV-1 gp120 third variable region (V3) crown


Mass: 2635.891 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Human immunodeficiency virus 1 / References: UniProt: C0SMB0
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 188 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY
Sequence detailsAUTHORS STATE THAT THE FAB WERE MADE BY ENZYME DIGESTION, THEREFORE THE REAL ENDINGS OF THE CHAINS ...AUTHORS STATE THAT THE FAB WERE MADE BY ENZYME DIGESTION, THEREFORE THE REAL ENDINGS OF THE CHAINS ARE UNKNOWN.

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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: 2.6 Å3/Da / Density % sol: 52.68 %
Crystal growTemperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 1.49 M NH4 sulfate, 0.1 M NaCl, 0.1 M Hepes, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 296K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X4A / Wavelength: 0.9791 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 17, 2007
Details: a KOHZU double crystal monochromator with a sagittally focused second crystal. Two spherical mirrors, one will be rhodium coated. User choice of either mirror depending on the desired energy
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9791 Å / Relative weight: 1
ReflectionResolution: 2.99→50 Å / Num. obs: 11328 / % possible obs: 100 % / Rmerge(I) obs: 0.162 / Χ2: 1.302 / Net I/σ(I): 7.4
Reflection shell
Resolution (Å)Rmerge(I) obsNum. unique allΧ2% possible all
2.99-3.110.49410971.401100
3.11-3.230.37810981.416100
3.23-3.380.30910921.474100
3.38-3.560.24411091.47100
3.56-3.780.19911081.483100
3.78-4.070.1711091.396100
4.07-4.480.13811291.265100
4.48-5.130.12311381.214100
5.13-6.460.11411671.114100
6.46-500.06712810.779100

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
REFMAC5.5.0102refinement
PDB_EXTRACT3.1data extraction
ADSCQuantumdata collection
HKL-2000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.99→48.97 Å / Cor.coef. Fo:Fc: 0.933 / Cor.coef. Fo:Fc free: 0.797 / Occupancy max: 1 / Occupancy min: 1 / SU B: 24.304 / SU ML: 0.45 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.587 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.33 538 4.8 %RANDOM
Rwork0.191 ---
obs0.198 11277 99.79 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 100.1 Å2 / Biso mean: 46.504 Å2 / Biso min: 3.21 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å2-0 Å2
2--0 Å2-0 Å2
3----0 Å2
Refinement stepCycle: LAST / Resolution: 2.99→48.97 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3475 0 0 188 3663
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.0223567
X-RAY DIFFRACTIONr_angle_refined_deg1.6461.9574865
X-RAY DIFFRACTIONr_dihedral_angle_1_deg8.0085463
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.58424.063128
X-RAY DIFFRACTIONr_dihedral_angle_3_deg20.49415546
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.7491513
X-RAY DIFFRACTIONr_chiral_restr0.10.2547
X-RAY DIFFRACTIONr_gen_planes_refined0.0080.0212696
X-RAY DIFFRACTIONr_mcbond_it0.6791.52315
X-RAY DIFFRACTIONr_mcangle_it1.25923746
X-RAY DIFFRACTIONr_scbond_it1.39231252
X-RAY DIFFRACTIONr_scangle_it2.5254.51119
LS refinement shellResolution: 2.99→3.069 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.506 41 -
Rwork0.251 741 -
all-782 -
obs--97.14 %

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