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- PDB-1a3r: FAB FRAGMENT (ANTIBODY 8F5) COMPLEXED WITH PEPTIDE FROM HUMAN RHI... -

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Basic information

Entry
Database: PDB / ID: 1a3r
TitleFAB FRAGMENT (ANTIBODY 8F5) COMPLEXED WITH PEPTIDE FROM HUMAN RHINOVIRUS (SEROTYPE 2) VIRAL CAPSID PROTEIN VP2 (RESIDUES 156-170)
Components
  • HUMAN RHINOVIRUS CAPSID PROTEIN VP2
  • IGG2A 8F5 FAB (HEAVY CHAIN)
  • IGG2A 8F5 FAB (LIGHT CHAIN)
KeywordsViral protein/Immune system / IMMUNOGLOBULIN / ANTIBODY / RHINOVIRUS / NEUTRALIZATION / CONTINUOUS EPITOPE / COMPLEX (IMMUNOGLOBULIN-VIRAL PEPTIDE) / Viral protein-Immune system COMPLEX
Function / homology
Function and homology information


symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / channel activity ...symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / ribonucleoside triphosphate phosphatase activity / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / DNA replication / RNA helicase activity / endocytosis involved in viral entry into host cell / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / virion attachment to host cell / host cell nucleus / structural molecule activity / proteolysis / RNA binding / zinc ion binding / ATP binding / metal ion binding / membrane
Similarity search - Function
: / : / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 ...: / : / Poliovirus 3A protein-like / Poliovirus 3A protein like / Picornavirus 2B protein / Poliovirus core protein 3a, soluble domain / Picornavirus 2B protein / Peptidase C3, picornavirus core protein 2A / Picornavirus core protein 2A / Picornavirus coat protein VP4 / Picornavirus coat protein (VP4) / Immunoglobulin V-Type / Peptidase C3A/C3B, picornaviral / 3C cysteine protease (picornain 3C) / Picornavirales 3C/3C-like protease domain / Picornavirales 3C/3C-like protease domain profile. / Immunoglobulin V-set domain / Picornavirus capsid / picornavirus capsid protein / Helicase, superfamily 3, single-stranded RNA virus / Superfamily 3 helicase of positive ssRNA viruses domain profile. / Helicase, superfamily 3, single-stranded DNA/RNA virus / RNA helicase / Immunoglobulin V-set domain / Picornavirus/Calicivirus coat protein / Viral coat protein subunit / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / RNA-directed RNA polymerase, C-terminal domain / Viral RNA-dependent RNA polymerase / Reverse transcriptase/Diguanylate cyclase domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / Immunoglobulin-like fold / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / Immunoglobulins / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
Genome polyprotein / Igh protein / ENSMUSG00000076577 protein
Similarity search - Component
Biological speciesMus musculus (house mouse)
Human rhinovirus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsTormo, J. / Blaas, D. / Fita, I.
Citation
Journal: EMBO J. / Year: 1994
Title: Crystal structure of a human rhinovirus neutralizing antibody complexed with a peptide derived from viral capsid protein VP2.
Authors: Tormo, J. / Blaas, D. / Parry, N.R. / Rowlands, D. / Stuart, D. / Fita, I.
#1: Journal: Protein Sci. / Year: 1992
Title: Three-Dimensional Structure of the Fab Fragment of a Neutralizing Antibody to Human Rhinovirus Serotype 2
Authors: Tormo, J. / Stadler, E. / Skern, T. / Auer, H. / Kanzler, O. / Betzel, C. / Blaas, D. / Fita, I.
#2: Journal: J.Biol.Chem. / Year: 1990
Title: Crystallization and Preliminary X-Ray Diffraction Studies of the Fab Fragment of a Neutralizing Monoclonal Antibody Directed Against Human Rhinovirus Serotype 2
Authors: Tormo, J. / Fita, I. / Kanzler, O. / Blaas, D.
History
DepositionJan 23, 1998Processing site: BNL
Revision 1.0Apr 29, 1998Provider: repository / Type: Initial release
Revision 1.1Mar 25, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Aug 2, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: database_2 / diffrn_source ...database_2 / diffrn_source / pdbx_initial_refinement_model / software / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _diffrn_source.pdbx_synchrotron_site / _software.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_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_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
Revision 1.4Oct 16, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature
Item: _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: IGG2A 8F5 FAB (LIGHT CHAIN)
H: IGG2A 8F5 FAB (HEAVY CHAIN)
P: HUMAN RHINOVIRUS CAPSID PROTEIN VP2


Theoretical massNumber of molelcules
Total (without water)49,7163
Polymers49,7163
Non-polymers00
Water3,837213
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5700 Å2
ΔGint-35 kcal/mol
Surface area19950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.790, 76.320, 92.320
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Antibody IGG2A 8F5 FAB (LIGHT CHAIN) / ANTIBODY 8F5


Mass: 24416.984 Da / Num. of mol.: 1 / Fragment: FAB FRAGMENT (PAPAIN DIGESTION) / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q52L64*PLUS
#2: Antibody IGG2A 8F5 FAB (HEAVY CHAIN) / ANTIBODY 8F5


Mass: 23588.201 Da / Num. of mol.: 1 / Fragment: FAB FRAGMENT (PAPAIN DIGESTION) / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse) / References: UniProt: Q505N9*PLUS
#3: Protein/peptide HUMAN RHINOVIRUS CAPSID PROTEIN VP2


Mass: 1710.905 Da / Num. of mol.: 1 / Fragment: RESIDUES 156 - 170 / Source method: isolated from a natural source / Details: COMMON COLD VIRUS / Source: (natural) Human rhinovirus 2 / Genus: Rhinovirus / Species: Human rhinovirus A / Strain: SEROTYPE 2 / References: UniProt: P04936
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 213 / Source method: isolated from a natural source / Formula: H2O
Compound detailsNH2: THE SYNTHETIC PEPTIDE HAS ITS C-TERMINAL END BLOCKED WITH AN AMIDE GROUP.
Has protein modificationY
Sequence detailsTHE PEPTIDE IS NUMBERED ACCORDING TO THE VIENNA ISOLATE SEQUENCE (SKERN ET AL., NUCLEIC ACIDS RES., ...THE PEPTIDE IS NUMBERED ACCORDING TO THE VIENNA ISOLATE SEQUENCE (SKERN ET AL., NUCLEIC ACIDS RES., 13:2111- 2126(1985)

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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: 52.9 %
Crystal growpH: 7.5
Details: FAB-PEPTIDE COMPLEX WAS CRYSTALLIZED FROM 0.9 M SODIUM CITRATE, 25 MM SODIUM CHLORIDE, 50 MM TRIS-HCL, PH 7.75, pH 7.5
Crystal grow
*PLUS
Temperature: 4 ℃ / Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
17.0 mg/mlFab1drop
21.1 mg/mloligonucleotide1drop
30.45 Msodium citrate1drop
425 mM1dropNaCl
550 mMTris1drop
60.9 Msodium citrate1reservoir

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Data collection

DiffractionMean temperature: 293 K
Diffraction sourceSource: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: X11
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 20, 1991
RadiationMonochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthRelative weight: 1
ReflectionResolution: 2.1→20 Å / Num. obs: 28392 / % possible obs: 94.6 % / Biso Wilson estimate: 13.6 Å2 / Rsym value: 0.062
Reflection shellResolution: 2.1→2.15 Å / Rsym value: 0.18 / % possible all: 90.2
Reflection
*PLUS
Rmerge(I) obs: 0.07

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Processing

Software
NameVersionClassification
MOSFLMdata reduction
ROTAVATAdata reduction
Agrovatadata reduction
X-PLOR3.851model building
X-PLOR3.851refinement
CCP4(AGROVATAdata scaling
ROTAVATAdata scaling
X-PLOR3.851phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1BBD

1bbd


Resolution: 2.1→20 Å / Data cutoff high absF: 10000000 / Data cutoff low absF: 0.001 / Isotropic thermal model: RESTRAINED / σ(F): 0 / Details: BULK SOLVENT MODEL USED
RfactorNum. reflection% reflection
Rwork0.171 --
obs0.171 28392 93.97 %
Displacement parametersBiso mean: 27.3 Å2
Refine analyzeLuzzati coordinate error obs: 0.21 Å / Luzzati d res low obs: 5 Å / Luzzati sigma a obs: 0.22 Å
Refinement stepCycle: LAST / Resolution: 2.1→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3456 0 0 213 3669
Refine LS restraints
Refine-IDTypeDev idealDev ideal target
X-RAY DIFFRACTIONx_bond_d0.005
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_deg1.3
X-RAY DIFFRACTIONx_angle_deg_na
X-RAY DIFFRACTIONx_angle_deg_prot
X-RAY DIFFRACTIONx_dihedral_angle_d27.9
X-RAY DIFFRACTIONx_dihedral_angle_d_na
X-RAY DIFFRACTIONx_dihedral_angle_d_prot
X-RAY DIFFRACTIONx_improper_angle_d1.11
X-RAY DIFFRACTIONx_improper_angle_d_na
X-RAY DIFFRACTIONx_improper_angle_d_prot
X-RAY DIFFRACTIONx_mcbond_it2.1921.5
X-RAY DIFFRACTIONx_mcangle_it3.4672
X-RAY DIFFRACTIONx_scbond_it3.9822
X-RAY DIFFRACTIONx_scangle_it5.6962.5
LS refinement shellResolution: 2.1→2.23 Å / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rwork0.226 4445 -
obs--90.07 %
Xplor file
Refine-IDSerial noParam fileTopol file
X-RAY DIFFRACTION1PARHCSDX.PROTOPHCSDX.PRO
X-RAY DIFFRACTION2PARAM19.SOLTOPH19.SOL
Software
*PLUS
Name: X-PLOR / Version: 3.851 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_dihedral_angle_deg27.9
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_improper_angle_deg1.11

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