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- PDB-6e4x: Human antibody S5V2-29 in complex with influenza hemagglutinin A/... -

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Basic information

Entry
Database: PDB / ID: 6e4x
TitleHuman antibody S5V2-29 in complex with influenza hemagglutinin A/Texas/50/2012 (H3N2)
Components
  • Hemagglutinin
  • S5V2-29 heavy chain
  • S5V2-29 light chain
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / influenza antibody / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / apical plasma membrane / 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 / extracellular region
Similarity search - Function
Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type ...Hemagglutinin; Chain A, domain 2 / Hemagglutinin Chain A, Domain 2 / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ribbon / 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 / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Alpha-Beta Complex / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Ig-like domain-containing protein / Hemagglutinin
Similarity search - Component
Biological speciesInfluenza A virus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.25 Å
AuthorsMcCarthy, K.R. / Harrison, S.C.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)P01AI089618 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)1U19AI117892-01 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI128832 United States
CitationJournal: Cell / Year: 2019
Title: Antibodies to a Conserved Influenza Head Interface Epitope Protect by an IgG Subtype-Dependent Mechanism.
Authors: Watanabe, A. / McCarthy, K.R. / Kuraoka, M. / Schmidt, A.G. / Adachi, Y. / Onodera, T. / Tonouchi, K. / Caradonna, T.M. / Bajic, G. / Song, S. / McGee, C.E. / Sempowski, G.D. / Feng, F. / ...Authors: Watanabe, A. / McCarthy, K.R. / Kuraoka, M. / Schmidt, A.G. / Adachi, Y. / Onodera, T. / Tonouchi, K. / Caradonna, T.M. / Bajic, G. / Song, S. / McGee, C.E. / Sempowski, G.D. / Feng, F. / Urick, P. / Kepler, T.B. / Takahashi, Y. / Harrison, S.C. / Kelsoe, G.
History
DepositionJul 18, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 22, 2019Provider: repository / Type: Initial release
Revision 1.1May 29, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Dec 18, 2019Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Hemagglutinin
Y: S5V2-29 light chain
Z: S5V2-29 heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,21011
Polymers81,4063
Non-polymers2,8048
Water2,594144
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8880 Å2
ΔGint6 kcal/mol
Surface area33190 Å2
Unit cell
Length a, b, c (Å)115.740, 163.480, 136.370
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

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Protein , 1 types, 1 molecules B

#1: Protein Hemagglutinin /


Mass: 32618.846 Da / Num. of mol.: 1 / Fragment: head domain (UNP residues 53-335)
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (A/Texas/50/2012(H3N2))
Strain: A/Texas/50/2012(H3N2) / Gene: HA, L998_47834gpHA / Plasmid: pFB / Cell line (production host): Hi5 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: R4L1D1

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Antibody , 2 types, 2 molecules YZ

#2: Antibody S5V2-29 light chain


Mass: 22803.189 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGKV1-39*01 / Plasmid: pVRC / Cell line (production host): 293F / Production host: Homo sapiens (human) / References: UniProt: Q8TCD0
#3: Antibody S5V2-29 heavy chain


Mass: 25984.266 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGHV4-61*01 / Plasmid: pVRC / Cell line (production host): 293F / Production host: Homo sapiens (human)

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Sugars , 4 types, 4 molecules

#4: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 894.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-4/a4-b1_a6-e1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-3]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5][a1122h-1b_1-5]/1-2-1-3/a3-b1_a4-c1_c4-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(3+1)][a-L-Fucp]{}[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#7: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 2 types, 148 molecules

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


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 144 / 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: 3.96 Å3/Da / Density % sol: 68.95 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 100 mM magnesium sulfate, 100 mM PIPES, pH 6.0, 30% PEG400

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 20, 2018
RadiationMonochromator: single crystal Si(220) side bounce / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.25→46.37 Å / Num. obs: 61532 / % possible obs: 97.7 % / Redundancy: 5.2 % / CC1/2: 0.998 / Rmerge(I) obs: 0.073 / Net I/σ(I): 14.81
Reflection shellResolution: 2.25→2.33 Å / Num. unique obs: 31682 / % possible all: 99.05

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Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.25→46.37 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 25.15
RfactorNum. reflection% reflectionSelection details
Rfree0.2251 2961 4.93 %RANDOM SELECTION
Rwork0.2025 ---
obs0.2036 60119 97.72 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.25→46.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5505 0 186 144 5835
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0045838
X-RAY DIFFRACTIONf_angle_d0.7497958
X-RAY DIFFRACTIONf_dihedral_angle_d5.4963475
X-RAY DIFFRACTIONf_chiral_restr0.048918
X-RAY DIFFRACTIONf_plane_restr0.005999
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.25-2.28690.34961420.32552769X-RAY DIFFRACTION99
2.2869-2.32630.32731220.30012720X-RAY DIFFRACTION99
2.3263-2.36860.33821350.28342734X-RAY DIFFRACTION99
2.3686-2.41420.35481260.27322733X-RAY DIFFRACTION99
2.4142-2.46350.28111420.26492707X-RAY DIFFRACTION98
2.4635-2.5170.2851200.26762664X-RAY DIFFRACTION96
2.517-2.57560.25161410.26222717X-RAY DIFFRACTION99
2.5756-2.640.28631340.25262774X-RAY DIFFRACTION99
2.64-2.71130.31231530.2552709X-RAY DIFFRACTION99
2.7113-2.79110.27721530.2492743X-RAY DIFFRACTION99
2.7911-2.88120.26021610.24492722X-RAY DIFFRACTION99
2.8812-2.98420.23981530.23642738X-RAY DIFFRACTION99
2.9842-3.10360.24531400.22692722X-RAY DIFFRACTION99
3.1036-3.24480.24521290.21292775X-RAY DIFFRACTION98
3.2448-3.41590.22871370.21582708X-RAY DIFFRACTION97
3.4159-3.62980.22561260.18942628X-RAY DIFFRACTION95
3.6298-3.90990.18431370.18372691X-RAY DIFFRACTION96
3.9099-4.30320.18751580.1682708X-RAY DIFFRACTION97
4.3032-4.92530.1921440.14792743X-RAY DIFFRACTION97
4.9253-6.20310.21381580.17552722X-RAY DIFFRACTION96
6.2031-47.24170.19621500.19282731X-RAY DIFFRACTION93
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)
12.62322.1418-1.9884.0699-2.58084.072-0.08640.79030.415-0.23790.43370.1889-0.2572-0.5456-0.41370.461-0.0035-0.04160.65010.10260.445817.1388-55.6384-39.9468
21.58940.23970.07772.3063-1.96474.2114-0.06920.2091-0.1975-0.22520.10440.0480.5612-0.253-0.040.4381-0.0522-0.02260.3555-0.02690.371817.3466-74.1604-22.9323
31.1347-0.38080.57042.1439-0.08573.0288-0.0964-0.0652-0.15540.0378-0.0218-0.11530.07970.05880.1670.3899-0.0022-0.01480.27240.01420.384722.3198-72.5033-13.8425
41.93020.03030.08583.9708-3.364.0036-0.07310.65720.241-0.4194-0.0874-0.23470.1154-0.0250.1660.4929-0.0423-0.01340.53570.06180.442721.0089-60.2958-36.0495
55.88612.9744-0.99716.9436-2.9897.2497-0.11820.34520.89160.06810.23560.0529-0.23160.3229-0.18330.5316-0.0993-0.00910.75930.2530.736328.1876-42.3397-43.6935
65.50382.646-5.15665.4382-1.50378.7614-0.06310.58980.5806-0.5161-0.19780.1764-0.8269-0.43140.26290.58980.1478-0.13870.5428-0.04990.4235-1.5667-39.6309-11.6698
74.033-1.34241.68453.7771-0.07992.98170.0698-0.06610.01210.0151-0.19810.19950.09840.03640.11990.45020.0542-0.02980.5528-0.09330.4383.6746-50.0777-7.5001
87.5890.61032.08862.06830.90613.50280.11560.40780.0287-0.3799-0.30650.127-0.2916-0.39090.1850.47530.1166-0.03020.4554-0.07210.41160.3961-45.3728-9.1742
94.68561.31610.87690.49120.14870.28410.35970.8353-0.319-0.1853-0.39990.11270.1151-0.61130.20750.53070.0806-0.04010.6704-0.19690.5938-15.5851-38.59120.0695
103.67682.31834.19654.61732.75834.77460.2076-0.2821-0.29770.33110.0244-0.25180.2039-0.5336-0.36760.4672-0.012-0.04840.5825-0.02310.4518-13.9004-28.907129.2858
112.39940.98531.03575.45435.10768.85730.11670.5765-0.1606-0.2678-0.0549-0.09150.04470.2295-0.10150.28150.0265-0.03840.4811-0.07250.376-16.1578-28.13514.1569
126.3514-4.5841-1.16716.41861.53143.83210.27330.31170.4421-0.333-0.05090.1726-0.36630.2245-0.14420.4714-0.03630.00830.51110.05650.4376-13.1302-19.959317.3772
132.74130.6260.59823.64323.99184.3634-0.38970.7282-0.9401-0.41910.3528-0.5740.47780.562-0.27240.56690.0972-0.14190.8934-0.22950.8165-13.0525-41.49716.6687
142.77270.77350.21831.80472.61675.16440.07990.0692-0.0249-0.05490.0342-0.1751-0.14340.2207-0.10440.44760.0445-0.04310.4387-0.00670.4337-15.5645-20.692724.5189
154.08051.84293.19024.07743.38453.5475-0.20740.20740.1952-0.2535-0.44350.544-0.5066-0.87340.51080.40740.1186-0.06390.5139-0.06280.5428-24.7234-25.788216.7485
161.8581-0.55790.42722.40421.84812.88070.3191-0.5654-0.07640.2369-0.1139-0.46140.15540.0873-0.31570.58-0.0759-0.02110.6863-0.08150.496915.1246-44.153514.473
174.60891.5971-0.97811.20281.48118.6279-0.0117-0.2598-0.12360.210.2753-0.50660.38810.8588-0.24250.42480.0088-0.01030.5757-0.13810.439518.2859-48.82323.2691
185.86970.39340.34110.99791.79656.05760.0630.16720.2151-0.10390.3395-0.7867-0.00280.7551-0.42360.416-0.06380.03440.644-0.20490.564522.4582-42.74258.0069
192.7246-0.9340.2196.52830.58162.05710.26230.7316-0.12080.034-0.2851-0.25850.4785-0.30780.01970.24820.0349-0.01530.5979-0.0970.362614.4134-50.3923-2.3805
208.3822-1.7211-6.20784.75111.25064.58620.50470.94690.3112-0.6171-0.0815-0.20180.1209-0.531-0.24550.51470.0127-0.00860.5183-0.02620.533314.2737-51.8587-10.505
211.5361-0.2396-2.39632.19710.75393.5122-0.03340.0605-0.1541-0.00550.14670.2627-0.0235-0.0854-0.23540.43110.0094-0.09550.39960.00350.511-3.8373-35.722.8725
222.20480.3602-0.23751.68710.64292.94640.10590.1253-0.46110.0239-0.06260.04540.2431-0.207-0.07490.4003-0.0248-0.07420.5529-0.08410.5401-7.4842-38.298522.0725
230.97391.30220.78353.2998-0.54183.62030.276-0.0575-0.30710.2088-0.05420.17790.2122-0.1713-0.03630.44070.0134-0.06090.454-0.04780.5666-6.3301-42.566630.4692
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 37 through 89 )
2X-RAY DIFFRACTION2chain 'B' and (resid 90 through 174 )
3X-RAY DIFFRACTION3chain 'B' and (resid 175 through 247 )
4X-RAY DIFFRACTION4chain 'B' and (resid 248 through 288 )
5X-RAY DIFFRACTION5chain 'B' and (resid 289 through 311 )
6X-RAY DIFFRACTION6chain 'Y' and (resid 1 through 25 )
7X-RAY DIFFRACTION7chain 'Y' and (resid 26 through 61 )
8X-RAY DIFFRACTION8chain 'Y' and (resid 62 through 97 )
9X-RAY DIFFRACTION9chain 'Y' and (resid 98 through 109 )
10X-RAY DIFFRACTION10chain 'Y' and (resid 110 through 124 )
11X-RAY DIFFRACTION11chain 'Y' and (resid 125 through 146 )
12X-RAY DIFFRACTION12chain 'Y' and (resid 147 through 159 )
13X-RAY DIFFRACTION13chain 'Y' and (resid 160 through 170 )
14X-RAY DIFFRACTION14chain 'Y' and (resid 171 through 193 )
15X-RAY DIFFRACTION15chain 'Y' and (resid 194 through 208 )
16X-RAY DIFFRACTION16chain 'Z' and (resid 1 through 17 )
17X-RAY DIFFRACTION17chain 'Z' and (resid 18 through 61 )
18X-RAY DIFFRACTION18chain 'Z' and (resid 62 through 92 )
19X-RAY DIFFRACTION19chain 'Z' and (resid 93 through 106 )
20X-RAY DIFFRACTION20chain 'Z' and (resid 107 through 120 )
21X-RAY DIFFRACTION21chain 'Z' and (resid 121 through 151 )
22X-RAY DIFFRACTION22chain 'Z' and (resid 152 through 206 )
23X-RAY DIFFRACTION23chain 'Z' and (resid 207 through 231 )

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