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- PDB-3u4e: Crystal Structure of PG9 Fab in Complex with V1V2 Region from HIV... -

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Basic information

Entry
Database: PDB / ID: 3u4e
TitleCrystal Structure of PG9 Fab in Complex with V1V2 Region from HIV-1 strain CAP45
Components
  • PG9 Heavy Chain
  • PG9 Light Chain
  • V1V2 region of HIV-1 on 1FD6 scaffold
KeywordsIMMUNE SYSTEM / NEUTRALIZING ANTIBODIES / LONG CDRH3 / HIV-1
Function / homology
Function and homology information


virus-mediated perturbation of host defense response => GO:0019049 / : / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / viral protein processing / fusion of virus membrane with host plasma membrane ...virus-mediated perturbation of host defense response => GO:0019049 / : / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / viral protein processing / 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 / plasma membrane
Similarity search - Function
Ubiquitin-like (UB roll) - #10 / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Ubiquitin-like (UB roll) / Immunoglobulins / Roll ...Ubiquitin-like (UB roll) - #10 / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Ubiquitin-like (UB roll) / Immunoglobulins / Roll / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.185 Å
AuthorsGorman, J. / McLellan, J. / Pancera, M. / Kwong, P.D.
CitationJournal: Nature / Year: 2011
Title: Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9.
Authors: McLellan, J.S. / Pancera, M. / Carrico, C. / Gorman, J. / Julien, J.P. / Khayat, R. / Louder, R. / Pejchal, R. / Sastry, M. / Dai, K. / O'Dell, S. / Patel, N. / Shahzad-Ul-Hussan, S. / Yang, ...Authors: McLellan, J.S. / Pancera, M. / Carrico, C. / Gorman, J. / Julien, J.P. / Khayat, R. / Louder, R. / Pejchal, R. / Sastry, M. / Dai, K. / O'Dell, S. / Patel, N. / Shahzad-Ul-Hussan, S. / Yang, Y. / Zhang, B. / Zhou, T. / Zhu, J. / Boyington, J.C. / Chuang, G.Y. / Diwanji, D. / Georgiev, I. / Do Kwon, Y. / Lee, D. / Louder, M.K. / Moquin, S. / Schmidt, S.D. / Yang, Z.Y. / Bonsignori, M. / Crump, J.A. / Kapiga, S.H. / Sam, N.E. / Haynes, B.F. / Burton, D.R. / Koff, W.C. / Walker, L.M. / Phogat, S. / Wyatt, R. / Orwenyo, J. / Wang, L.X. / Arthos, J. / Bewley, C.A. / Mascola, J.R. / Nabel, G.J. / Schief, W.R. / Ward, A.B. / Wilson, I.A. / Kwong, P.D.
History
DepositionOct 7, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 30, 2011Provider: repository / Type: Initial release
Revision 1.1Dec 21, 2011Group: Database references
Revision 2.0Dec 25, 2019Group: Advisory / Derived calculations / Polymer sequence
Category: entity_poly / pdbx_struct_mod_residue ...entity_poly / pdbx_struct_mod_residue / pdbx_unobs_or_zero_occ_atoms / struct_conn
Item: _entity_poly.pdbx_seq_one_letter_code_can / _pdbx_struct_mod_residue.parent_comp_id ..._entity_poly.pdbx_seq_one_letter_code_can / _pdbx_struct_mod_residue.parent_comp_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _struct_conn.pdbx_leaving_atom_flag
Revision 3.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_close_contact / 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 / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_unobs_or_zero_occ_atoms.auth_asym_id / _pdbx_unobs_or_zero_occ_atoms.auth_seq_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.pdbx_ptnr2_PDB_ins_code / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 3.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 3.2Dec 6, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
G: V1V2 region of HIV-1 on 1FD6 scaffold
J: V1V2 region of HIV-1 on 1FD6 scaffold
H: PG9 Heavy Chain
L: PG9 Light Chain
A: PG9 Heavy Chain
B: PG9 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,96823
Polymers127,5056
Non-polymers5,46317
Water8,755486
1
G: V1V2 region of HIV-1 on 1FD6 scaffold
H: PG9 Heavy Chain
L: PG9 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,82913
Polymers63,7533
Non-polymers3,07710
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
J: V1V2 region of HIV-1 on 1FD6 scaffold
A: PG9 Heavy Chain
B: PG9 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)66,13910
Polymers63,7533
Non-polymers2,3867
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)73.026, 103.545, 186.373
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 2 molecules GJ

#1: Protein V1V2 region of HIV-1 on 1FD6 scaffold


Mass: 13722.299 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Plasmid: PVRC8400 / Production host: Homo Sapiens (human) / References: UniProt: Q1PHM9*PLUS

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Antibody , 2 types, 4 molecules HALB

#2: Antibody PG9 Heavy Chain


Mass: 27193.172 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PVRC8400 / Cell line (production host): HEK 293f / Production host: Homo sapiens (human)
#3: Antibody PG9 Light Chain


Mass: 22837.256 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: PVRC8400 / Cell line (production host): HEK 293S GnTI- / Production host: Homo Sapiens (human)

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Sugars , 4 types, 5 molecules

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


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1WURCSPDB2Glycan 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-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#5: Polysaccharide alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1072.964 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1WURCSPDB2Glycan 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-D-Manp]{[(3+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#6: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#7: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose


Type: oligosaccharide / Mass: 342.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a1122h-1b_1-5][a1122h-1a_1-5]/1-2/a3-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-Manp]{[(3+1)][a-D-Manp]{}}LINUCSPDB-CARE

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Non-polymers , 2 types, 498 molecules

#8: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: SO4
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 486 / 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: 2.76 Å3/Da / Density % sol: 55.48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 13% (w/v) PEG 3350, 11% (v/v) 2-methyl-2,4-pentanediol, 0.2 M lithium sulfate, 0.1 M imidazole pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 14, 2011
RadiationMonochromator: double crystal - liquid nitrogen cooled / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.19→50 Å / Num. all: 73822 / Num. obs: 67917 / % possible obs: 92 % / Observed criterion σ(I): -3 / Redundancy: 4.1 %
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsDiffraction-ID% possible all
2.19-2.242.40.3392.4168.7
2.24-2.32.70.342.6173.4
2.3-2.362.90.342.7177.5
2.36-2.4330.3222.4182.1
2.43-2.513.20.3322.4187.1
2.51-2.63.30.3072.1193.1
2.6-2.73.70.3212.3198.1
2.7-2.824.30.2912.3199.9
2.82-2.974.90.2493.91100
2.97-3.1650.1944.51100
3.16-3.450.13710.51100
3.4-3.7450.106121100
3.74-4.2950.09213.81100
4.29-5.450.08214.41100
5.4-504.70.05418.7199

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Processing

Software
NameVersionClassification
SERGUIdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3U2S

3u2s


Resolution: 2.185→27.693 Å / SU ML: 0.71 / σ(F): 1.91 / Phase error: 25.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2336 3442 5.09 %Random
Rwork0.1818 ---
obs0.1845 67657 91.49 %-
all-73950 --
Solvent computationShrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 31.7 Å2 / ksol: 0.304 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.8889 Å2-0 Å20 Å2
2---6.6663 Å2-0 Å2
3---0.7774 Å2
Refinement stepCycle: LAST / Resolution: 2.185→27.693 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8478 0 348 486 9312
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0099040
X-RAY DIFFRACTIONf_angle_d1.09412297
X-RAY DIFFRACTIONf_dihedral_angle_d14.1623254
X-RAY DIFFRACTIONf_chiral_restr0.0761425
X-RAY DIFFRACTIONf_plane_restr0.0051517
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1851-2.2150.3096870.23051655X-RAY DIFFRACTION59
2.215-2.24660.31991020.21451960X-RAY DIFFRACTION71
2.2466-2.28010.2507900.21922048X-RAY DIFFRACTION74
2.2801-2.31570.29711070.21972102X-RAY DIFFRACTION76
2.3157-2.35370.30941070.22512201X-RAY DIFFRACTION78
2.3537-2.39430.33731170.222219X-RAY DIFFRACTION81
2.3943-2.43780.29831220.22632324X-RAY DIFFRACTION83
2.4378-2.48460.32721230.23442427X-RAY DIFFRACTION87
2.4846-2.53530.29481390.24192503X-RAY DIFFRACTION90
2.5353-2.59040.29381430.25452590X-RAY DIFFRACTION94
2.5904-2.65060.26841430.24212683X-RAY DIFFRACTION97
2.6506-2.71680.30341340.23412776X-RAY DIFFRACTION99
2.7168-2.79020.32711480.23312759X-RAY DIFFRACTION99
2.7902-2.87230.28141740.21072755X-RAY DIFFRACTION100
2.8723-2.96490.29261660.20092779X-RAY DIFFRACTION100
2.9649-3.07070.26781540.19612765X-RAY DIFFRACTION99
3.0707-3.19350.26531440.19192801X-RAY DIFFRACTION100
3.1935-3.33860.24471430.1862838X-RAY DIFFRACTION100
3.3386-3.51430.23581560.17872806X-RAY DIFFRACTION100
3.5143-3.7340.19981490.16782813X-RAY DIFFRACTION100
3.734-4.02150.2051550.15362823X-RAY DIFFRACTION100
4.0215-4.42470.17521520.13492831X-RAY DIFFRACTION100
4.4247-5.06160.16351640.12352859X-RAY DIFFRACTION100
5.0616-6.36430.19231500.16012901X-RAY DIFFRACTION100
6.3643-27.69490.21341730.18832997X-RAY DIFFRACTION99
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)
10.98790.6039-0.23021.2306-0.8293.0382-0.2318-0.0773-0.05440.20630.0305-0.30920.1773-0.0491-0.00370.27060.0360.07020.33460.04520.11632.43663.1945-52.0311
22.1511-1.24750.28752.1069-0.7881.3168-0.1039-0.0840.13290.07380.0659-0.08630.0322-0.0480.01280.2435-0.00330.02370.38650.07090.276726.227916.8322-59.3482
31.378-0.27510.27582.0566-0.83772.8649-0.3696-0.24610.1418-0.25560.0716-0.1963-0.16910.0913-0.01010.324-0.0132-0.06650.3237-0.01680.1961-3.934-2.074830.063
42.44061.2938-0.87552.0572-0.81191.6731-0.189-0.3622-0.2734-0.08680.00120.05350.0224-0.07240.01440.36330.00170.02590.48890.03240.354-11.0251-16.64136.8024
50.4329-0.00520.33250.6616-0.08591.6546-0.07810.0330.12330.00120.0231-0.2177-0.1589-0.0790.00820.1857-0.0274-0.04430.1537-0.00320.249434.27975.172-9.7873
61.0296-0.01360.08471.9629-0.93141.73460.03170.1104-0.0104-0.11110.0218-0.03970.0436-0.01790.01050.1594-0.01470.02440.1725-0.00230.110626.8926-9.2622-24.3788
71.4797-0.0265-0.08411.52410.26332.4230.0146-0.2241-0.0240.055-0.0241-0.0316-0.09290.1504-0.00090.1834-0.00080.00420.2292-0.0070.217133.9546-23.10514.6357
80.62030.3721-0.22332.0331-0.55821.5120.1076-0.04280.02390.0624-0.0348-0.1013-0.0641-0.0449-0.02410.1464-0.0014-0.02650.1611-0.00620.2168-9.098511.65653.4673
91.4623-0.06560.06911.50580.26222.31720.25410.3929-0.0302-0.0877-0.17920.3177-0.4051-0.0048-0.0330.48160.14130.0160.43370.02310.3838-0.457728.3794-36.1017
100.60720.2258-0.37570.7278-0.24121.36610.00110.087-0.0764-0.10240.0302-0.17280.1359-0.0525-0.02140.22210.0020.03110.167-0.00340.3288-2.4236-2.2375-12.2117
111.62760.40560.01783.0157-0.31461.4928-0.11270.07570.31830.29060.1223-0.0904-0.21370.0931-0.01210.35570.0255-0.01280.30040.0410.373211.559918.2773-30.2527
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'G' and (resseq 1:180)
2X-RAY DIFFRACTION2chain 'G' and (resseq 190:244)
3X-RAY DIFFRACTION3chain 'J' and (resseq 1:180)
4X-RAY DIFFRACTION4chain 'J' and (resseq 190:245)
5X-RAY DIFFRACTION5chain 'L' and (resseq 1:116)
6X-RAY DIFFRACTION6chain 'H' and (resseq 1:113)
7X-RAY DIFFRACTION7chain 'H' and (resseq 114:216)
8X-RAY DIFFRACTION8chain 'A' and (resseq 1:113)
9X-RAY DIFFRACTION9chain 'A' and (resseq 114:216)
10X-RAY DIFFRACTION10chain 'B' and (resseq 2:116)
11X-RAY DIFFRACTION11chain 'B' and (resseq 117:209)

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