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- PDB-7a3o: Crystal structure of dengue 1 virus envelope glycoprotein in comp... -

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Basic information

Entry
Database: PDB / ID: 7a3o
TitleCrystal structure of dengue 1 virus envelope glycoprotein in complex with the scFv fragment of the broadly neutralizing human antibody EDE1 C10
Components
  • (Single chain variable fragment (scFv) from antibody EDE1 ...) x 2
  • Core proteinCapsid
KeywordsVIRAL PROTEIN / FLAVIVIRUS / CLASS 2 FUSION PROTEIN / DENGUE / Antibody
Function / homology
Function and homology information


: / flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / membrane => GO:0016020 ...: / flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / membrane => GO:0016020 / host cell endoplasmic reticulum membrane / protein dimerization activity / RNA helicase / induction by virus of host autophagy / viral RNA genome replication / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / virion attachment to host cell / virion membrane / structural molecule activity / extracellular region / ATP binding / metal ion binding
Similarity search - Function
Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B ...Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M superfamily, flavivirus / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / DEAD box, Flavivirus / Flavivirus DEAD domain / helicase superfamily c-terminal domain / Immunoglobulin E-set / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Biological speciesDengue virus 1
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsSharma, A. / Vaney, M.C. / Guardado-Calvo, P. / Duquerroy, S. / Rouvinski, A. / Rey, F.A.
Funding support France, 1items
OrganizationGrant numberCountry
Wellcome Trust France
Citation
Journal: Cell / Year: 2021
Title: The epitope arrangement on flavivirus particles contributes to Mab C10's extraordinary neutralization breadth across Zika and dengue viruses.
Authors: Arvind Sharma / Xiaokang Zhang / Wanwisa Dejnirattisai / Xinghong Dai / Danyang Gong / Wiyada Wongwiwat / Stéphane Duquerroy / Alexander Rouvinski / Marie-Christine Vaney / Pablo Guardado- ...Authors: Arvind Sharma / Xiaokang Zhang / Wanwisa Dejnirattisai / Xinghong Dai / Danyang Gong / Wiyada Wongwiwat / Stéphane Duquerroy / Alexander Rouvinski / Marie-Christine Vaney / Pablo Guardado-Calvo / Ahmed Haouz / Patrick England / Ren Sun / Z Hong Zhou / Juthathip Mongkolsapaya / Gavin R Screaton / Felix A Rey /
Abstract: The human monoclonal antibody C10 exhibits extraordinary cross-reactivity, potently neutralizing Zika virus (ZIKV) and the four serotypes of dengue virus (DENV1-DENV4). Here we describe a comparative ...The human monoclonal antibody C10 exhibits extraordinary cross-reactivity, potently neutralizing Zika virus (ZIKV) and the four serotypes of dengue virus (DENV1-DENV4). Here we describe a comparative structure-function analysis of C10 bound to the envelope (E) protein dimers of the five viruses it neutralizes. We demonstrate that the C10 Fab has high affinity for ZIKV and DENV1 but not for DENV2, DENV3, and DENV4. We further show that the C10 interaction with the latter viruses requires an E protein conformational landscape that limits binding to only one of the three independent epitopes per virion. This limited affinity is nevertheless counterbalanced by the particle's icosahedral organization, which allows two different dimers to be reached by both Fab arms of a C10 immunoglobulin. The epitopes' geometric distribution thus confers C10 its exceptional neutralization breadth. Our results highlight the importance not only of paratope/epitope complementarity but also the topological distribution for epitope-focused vaccine design.
#1: Journal: Nature / Year: 2016
Title: Structural basis of potent Zika-dengue virus antibody cross-neutralization.
Authors: Barba-Spaeth, G. / Dejnirattisai, W. / Rouvinski, A. / Vaney, M.C. / Medits, I. / Sharma, A. / Simon-Loriere, E. / Sakuntabhai, A. / Cao-Lormeau, V.M. / Haouz, A. / England, P. / Stiasny, K. ...Authors: Barba-Spaeth, G. / Dejnirattisai, W. / Rouvinski, A. / Vaney, M.C. / Medits, I. / Sharma, A. / Simon-Loriere, E. / Sakuntabhai, A. / Cao-Lormeau, V.M. / Haouz, A. / England, P. / Stiasny, K. / Mongkolsapaya, J. / Heinz, F.X. / Screaton, G.R. / Rey, F.A.
#2: Journal: Nature / Year: 2015
Title: Recognition determinants of broadly neutralizing human antibodies against dengue viruses.
Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. ...Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. / Petres, S. / Shepard, W.E. / Despres, P. / Arenzana-Seisdedos, F. / Dussart, P. / Mongkolsapaya, J. / Screaton, G.R. / Rey, F.A.
History
DepositionAug 18, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Dec 15, 2021Group: Database references / Derived calculations
Category: citation / pdbx_struct_assembly_gen ...citation / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_oper_list
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title / _pdbx_struct_oper_list.matrix[1][1] / _pdbx_struct_oper_list.matrix[1][2] / _pdbx_struct_oper_list.matrix[1][3] / _pdbx_struct_oper_list.matrix[2][1] / _pdbx_struct_oper_list.matrix[2][2] / _pdbx_struct_oper_list.matrix[2][3] / _pdbx_struct_oper_list.matrix[3][1] / _pdbx_struct_oper_list.matrix[3][2] / _pdbx_struct_oper_list.matrix[3][3] / _pdbx_struct_oper_list.name / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_oper_list.type / _pdbx_struct_oper_list.vector[1] / _pdbx_struct_oper_list.vector[2] / _pdbx_struct_oper_list.vector[3]
Revision 1.2Dec 22, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Core protein
H: Single chain variable fragment (scFv) from antibody EDE1 C10
L: Single chain variable fragment (scFv) from antibody EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)79,42511
Polymers78,3893
Non-polymers1,0368
Water724
1
A: Core protein
H: Single chain variable fragment (scFv) from antibody EDE1 C10
L: Single chain variable fragment (scFv) from antibody EDE1 C10
hetero molecules

A: Core protein
H: Single chain variable fragment (scFv) from antibody EDE1 C10
L: Single chain variable fragment (scFv) from antibody EDE1 C10
hetero molecules


  • defined by author
  • Evidence: gel filtration, Envelope protein (Chain A) are present as homodimers on virion surface and this protein is a crystallographic dimer here. Chain H (antibody heavy chain fragment) forms a ...Evidence: gel filtration, Envelope protein (Chain A) are present as homodimers on virion surface and this protein is a crystallographic dimer here. Chain H (antibody heavy chain fragment) forms a heterodimer with chain L (antibody light chain fragment).
  • 159 kDa, 6 polymers
  • Search similar-shape structures of this assembly by Omokage search (details)
Theoretical massNumber of molelcules
Total (without water)158,85022
Polymers156,7796
Non-polymers2,07216
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_554-y,-x,-z-1/21
Unit cell
Length a, b, c (Å)135.555, 135.555, 160.268
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number182
Space group name H-MP6322
Components on special symmetry positions
IDModelComponents
11A-504-

SO4

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Components

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Antibody , 2 types, 2 molecules HL

#2: Antibody Single chain variable fragment (scFv) from antibody EDE1 C10


Mass: 15679.234 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Variable domain from the heavy chain of broadly neutralising antibody EDE1 C10
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)
#3: Antibody Single chain variable fragment (scFv) from antibody EDE1 C10


Mass: 15632.767 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Variable domain from the light chain of broadly neutralising antibody EDE1 C10
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)

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Protein / Sugars , 2 types, 2 molecules A

#1: Protein Core protein / Capsid / Envelope protein E / Flavivirin protease NS2B regulatory subunit / Flavivirin protease NS3 ...Envelope protein E / Flavivirin protease NS2B regulatory subunit / Flavivirin protease NS3 catalytic subunit / Genome polyprotein / Matrix protein / Non-structural protein 1 / Non-structural protein 2A / Non-structural protein 2B / Non-structural protein 3 / Non-structural protein 4A / Non-structural protein 4B / Peptide 2k / Peptide pr / Protein prM / RNA-directed RNA polymerase NS5 / Serine protease NS3 / Serine protease subunit NS2B / Small envelope protein M


Mass: 47077.293 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Dengue virus serotype 1 envelope protein ectodomain
Source: (gene. exp.) Dengue virus 1 / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)
References: UniProt: Q9II02, flavivirin, nucleoside-triphosphate phosphatase, RNA helicase
#4: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(6+1)][a-L-Fucp]{}}LINUCSPDB-CARE

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Non-polymers , 3 types, 11 molecules

#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 2.69 Å3/Da / Density % sol: 54.33 %
Crystal growTemperature: 291 K / Method: vapor diffusion / pH: 8.5
Details: 50 mM Tris pH 8.5, 25% PEG 3,350, 200 mM (NH4)2SO4, 1.2% myo-inositol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Nov 5, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→50 Å / Num. obs: 21987 / % possible obs: 99.6 % / Redundancy: 8.2 % / CC1/2: 0.999 / Net I/σ(I): 14.5
Reflection shellResolution: 2.8→2.9 Å / Num. unique obs: 3110 / CC1/2: 0.512 / % possible all: 98.8

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.25data extraction
Aimlessdata scaling
PHENIXphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4UT9

4ut9


Resolution: 2.8→19.76 Å / SU ML: 0.41 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 29.06 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2678 1097 5.03 %
Rwork0.2183 20720 -
obs0.2207 21817 99.27 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 189.08 Å2 / Biso mean: 105.4587 Å2 / Biso min: 55.52 Å2
Refinement stepCycle: final / Resolution: 2.8→19.76 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4711 0 60 4 4775
Biso mean--148.57 66.29 -
Num. residues----614
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 8

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.8-2.930.3641470.34342435258296
2.93-3.080.36081560.331825282684100
3.08-3.270.35871320.312925552687100
3.27-3.520.34461280.274125662694100
3.52-3.870.24941250.227726012726100
3.88-4.430.25771420.190225932735100
4.43-5.560.20511280.179426602788100
5.56-19.760.26231390.20142782292199
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.3952-5.428-5.47547.03137.49887.99-0.1749-1.2337-0.41051.89980.18250.98050.0415-0.3752-0.42360.83990.28830.06281.19150.15310.586130.649614.4461-7.1583
28.2723-5.0668-5.52633.18113.32223.56770.4645-1.6923-0.60890.8323-0.47351.35830.0019-2.12620.7990.78780.35860.28961.6832-0.01350.562827.137114.0175-7.0622
33.8174-4.98034.39466.4703-5.7225.0546-0.65631.11630.86131.2927-0.3335-1.7249-0.1796-1.19830.49941.33520.25430.25511.4079-0.39861.099223.721235.39577.4404
48.1099-5.6733-2.19144.35550.44322.44960.6781-0.1157-1.2185-0.9563-0.49140.5683-0.865-0.9096-0.32281.03470.4098-0.12541.18120.08860.643316.06221.5272-24.1147
52.7623-2.4698-2.29884.28752.3391.66460.15510.44390.0768-0.2724-0.3160.1347-1.2151-1.70460.20850.85990.51980.10851.54250.16230.571126.886618.5205-24.9192
68.7801-3.9582-6.83043.33415.40629.7630.64170.34660.12810.0344-0.22210.2137-0.4506-2.5390.05990.69580.23730.03891.50770.21540.68624.0399.6638-18.3248
79.1526-3.1184-5.72837.35472.17445.12260.16191.9976-0.8785-0.5978-0.5810.7919-0.6147-2.50850.10870.77830.4157-0.10051.5656-0.01460.707917.971413.1597-23.8782
87.36120.56952.34315.18710.67380.27440.3276-0.18670.2569-0.4363-0.1554-0.4675-0.4869-0.5563-0.05810.76750.36430.1971.13510.2220.500331.807716.2695-19.8499
92.76812.9952.94924.42254.12443.86-0.0995-0.0801-0.1543-0.84220.1691-0.5333-0.6913-0.0017-0.03350.82370.12210.29020.6220.15370.732440.0775-10.173-47.6751
106.02284.78791.6376.78380.28696.19480.39980.26990.651-0.59960.2265-0.7741-0.9828-0.5725-0.74550.76890.1580.42430.68910.20011.211855.46115.905-34.9984
113.99823.70983.44764.70414.15784.5583-0.1715-0.0537-0.5444-0.93770.3843-0.9602-0.85490.328-0.20661.13320.00550.31520.68150.12190.804337.1648-16.7725-51.9158
124.87125.17671.77686.19030.8751.84930.9034-0.78780.68330.7374-0.81010.41180.1269-0.0718-0.05670.8967-0.02260.39620.8487-0.10951.011254.71026.4486-34.0437
132.6965-1.0469-0.15625.2563-0.02115.7920.5694-0.88371.29860.7577-0.2169-1.1612-1.31340.6085-0.37960.949-0.22750.19330.8988-0.22771.405161.311920.0849-5.2995
147.83150.27582.59448.18044.98743.7838-0.7765-2.36870.374-0.1121-0.75472.623-1.77250.23461.25391.32470.16360.18011.74250.02050.744826.198522.42734.2915
155.20424.62526.54638.43292.4262.007-0.0314-1.97010.10510.1262-2.45410.7293-0.41720.24032.3251.23810.39360.19251.7232-0.11210.797432.307123.98725.7047
164.67112.0832-1.2747.22134.57788.4427-0.3964-1.204-1.22550.80470.0586-0.58610.1644-0.370.30540.56520.27280.10371.36690.3140.699436.10529.0071-4.7291
174.68245.97740.29647.80910.4240.0197-0.4927-0.28391.2364-0.43680.21571.7501-1.7737-1.08490.18941.00490.92650.02571.55920.00240.683227.197425.4725-7.0736
188.7298-4.60010.30354.7088-0.43082.7676-0.5656-0.85990.65640.24760.4089-0.3523-1.2688-0.55820.02171.2590.67610.1791.4291-0.03770.685832.442224.5773-10.3266
199.6178-0.06791.34766.46362.67918.5266-0.1807-1.9091.08090.12110.068-0.8727-0.3413-0.52080.11690.96530.2531-0.02020.9875-0.1680.649239.077822.8348-2.7711
207.40060.27342.8449.49210.43013.94030.7491-0.23241.0072-0.3817-0.28270.0743-0.6384-1.0867-0.1751.45870.57920.14561.3619-0.1020.677530.619330.72070.7329
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'L' and (resid 86 through 93 )L86 - 93
2X-RAY DIFFRACTION2chain 'L' and (resid 94 through 104 )L94 - 104
3X-RAY DIFFRACTION3chain 'L' and (resid 105 through 112 )L105 - 112
4X-RAY DIFFRACTION4chain 'H' and (resid 1 through 17 )H1 - 17
5X-RAY DIFFRACTION5chain 'H' and (resid 18 through 39 )H18 - 39
6X-RAY DIFFRACTION6chain 'H' and (resid 40 through 64 )H40 - 64
7X-RAY DIFFRACTION7chain 'H' and (resid 65 through 91 )H65 - 91
8X-RAY DIFFRACTION8chain 'H' and (resid 92 through 127 )H92 - 127
9X-RAY DIFFRACTION9chain 'A' and (resid 1 through 129 )A1 - 129
10X-RAY DIFFRACTION10chain 'A' and (resid 130 through 192 )A130 - 192
11X-RAY DIFFRACTION11chain 'A' and (resid 193 through 256 )A193 - 256
12X-RAY DIFFRACTION12chain 'A' and (resid 257 through 298 )A257 - 298
13X-RAY DIFFRACTION13chain 'A' and (resid 299 through 395 )A299 - 395
14X-RAY DIFFRACTION14chain 'L' and (resid 3 through 16 )L3 - 16
15X-RAY DIFFRACTION15chain 'L' and (resid 17 through 23 )L17 - 23
16X-RAY DIFFRACTION16chain 'L' and (resid 24 through 34 )L24 - 34
17X-RAY DIFFRACTION17chain 'L' and (resid 35 through 40 )L35 - 40
18X-RAY DIFFRACTION18chain 'L' and (resid 41 through 50 )L41 - 50
19X-RAY DIFFRACTION19chain 'L' and (resid 51 through 71 )L51 - 71
20X-RAY DIFFRACTION20chain 'L' and (resid 72 through 85 )L72 - 85

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