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- PDB-4xnz: Crystal structure of broadly and potently neutralizing antibody V... -

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Basic information

Entry
Database: PDB / ID: 4xnz
TitleCrystal structure of broadly and potently neutralizing antibody VRC06B in complex with HIV-1 clade A/E strain 93TH057 gp120
Components
  • Envelope glycoprotein gp160,Envelope glycoprotein gp160
  • HEAVY CHAIN OF ANTIBODY VRC06B
  • LIGHT CHAIN OF ANTIBODY VRC06B
KeywordsIMMUNE SYSTEM / Antibody / HIV-1
Function / homology
Function and homology information


IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / CD22 mediated BCR regulation / complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc epsilon receptor (FCERI) signaling / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation ...IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / CD22 mediated BCR regulation / complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc epsilon receptor (FCERI) signaling / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / Initial triggering of complement / immunoglobulin complex, circulating / IgG immunoglobulin complex / immunoglobulin receptor binding / immunoglobulin mediated immune response / FCGR activation / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / complement activation, classical pathway / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / antigen binding / positive regulation of establishment of T cell polarity / virus-mediated perturbation of host defense response / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / host cell endosome membrane / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Regulation of Complement cascade / Cell surface interactions at the vascular wall / FCGR3A-mediated phagocytosis / FCERI mediated MAPK activation / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / antibacterial humoral response / clathrin-dependent endocytosis of virus by host cell / blood microparticle / Interleukin-4 and Interleukin-13 signaling / Potential therapeutics for SARS / adaptive immune response / viral protein processing / immune response / 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 / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Beta Complex / Immunoglobulin/major histocompatibility complex, conserved site ...HIV Envelope Protein Gp120; Chain G / Human immunodeficiency virus 1, Gp160, envelope glycoprotein / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Beta Complex / 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 / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Immunoglobulin kappa constant / Immunoglobulin heavy constant gamma 1 / Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHuman immunodeficiency virus 1
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.389 Å
AuthorsZhou, T. / Srivatsan, S. / Kwong, P.D.
CitationJournal: Cell / Year: 2015
Title: Maturation and Diversity of the VRC01-Antibody Lineage over 15 Years of Chronic HIV-1 Infection.
Authors: Wu, X. / Zhang, Z. / Schramm, C.A. / Joyce, M.G. / Do Kwon, Y. / Zhou, T. / Sheng, Z. / Zhang, B. / O'Dell, S. / McKee, K. / Georgiev, I.S. / Chuang, G.Y. / Longo, N.S. / Lynch, R.M. / ...Authors: Wu, X. / Zhang, Z. / Schramm, C.A. / Joyce, M.G. / Do Kwon, Y. / Zhou, T. / Sheng, Z. / Zhang, B. / O'Dell, S. / McKee, K. / Georgiev, I.S. / Chuang, G.Y. / Longo, N.S. / Lynch, R.M. / Saunders, K.O. / Soto, C. / Srivatsan, S. / Yang, Y. / Bailer, R.T. / Louder, M.K. / Mullikin, J.C. / Connors, M. / Kwong, P.D. / Mascola, J.R. / Shapiro, L.
History
DepositionJan 16, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 29, 2015Provider: repository / Type: Initial release
Revision 1.1May 6, 2015Group: Database references
Revision 1.2Nov 22, 2017Group: Derived calculations / Refinement description / Source and taxonomy
Category: entity_src_gen / pdbx_struct_assembly ...entity_src_gen / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_oper_list / software
Item: _entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details ..._entity_src_gen.pdbx_alt_source_flag / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_oper_list.symmetry_operation / _software.name
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_PDB_caveat / 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_validate_chiral / pdbx_validate_symm_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 / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_symm_contact.auth_asym_id_2 / _pdbx_validate_symm_contact.auth_seq_id_2 / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
G: Envelope glycoprotein gp160,Envelope glycoprotein gp160
H: HEAVY CHAIN OF ANTIBODY VRC06B
L: LIGHT CHAIN OF ANTIBODY VRC06B
A: Envelope glycoprotein gp160,Envelope glycoprotein gp160
B: HEAVY CHAIN OF ANTIBODY VRC06B
C: LIGHT CHAIN OF ANTIBODY VRC06B
D: Envelope glycoprotein gp160,Envelope glycoprotein gp160
E: HEAVY CHAIN OF ANTIBODY VRC06B
F: LIGHT CHAIN OF ANTIBODY VRC06B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)268,18030
Polymers262,4879
Non-polymers5,69321
Water0
1
G: Envelope glycoprotein gp160,Envelope glycoprotein gp160
H: HEAVY CHAIN OF ANTIBODY VRC06B
L: LIGHT CHAIN OF ANTIBODY VRC06B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,39310
Polymers87,4963
Non-polymers1,8987
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Envelope glycoprotein gp160,Envelope glycoprotein gp160
B: HEAVY CHAIN OF ANTIBODY VRC06B
C: LIGHT CHAIN OF ANTIBODY VRC06B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,61511
Polymers87,4963
Non-polymers2,1198
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
D: Envelope glycoprotein gp160,Envelope glycoprotein gp160
E: HEAVY CHAIN OF ANTIBODY VRC06B
F: LIGHT CHAIN OF ANTIBODY VRC06B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)89,1729
Polymers87,4963
Non-polymers1,6776
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)68.314, 189.442, 219.935
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein Envelope glycoprotein gp160,Envelope glycoprotein gp160


Mass: 39211.434 Da / Num. of mol.: 3 / Fragment: UNP RESIDUES 43-122, 201-303, 325-486
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human immunodeficiency virus 1 / Strain: 93TH057 / Gene: env / Plasmid: pVRC8400 / Cell line (production host): HEK 293 GNTI- / Production host: Homo sapiens (human) / References: UniProt: Q0ED31
#2: Antibody HEAVY CHAIN OF ANTIBODY VRC06B


Mass: 25268.527 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pVRC8400 / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: P01857*PLUS
#3: Antibody LIGHT CHAIN OF ANTIBODY VRC06B


Mass: 23015.602 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pVRC8400 / Cell line (production host): HEK293F / Production host: Homo sapiens (human) / References: UniProt: P01834*PLUS
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 3 / Source method: obtained synthetically
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#5: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 18 / Source method: obtained synthetically / 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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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.71 Å3/Da / Density % sol: 54.63 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 7% PEG 3350, 2.5% isopropanol, 0.1M Tris-HCl, pH 8.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Jul 12, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.389→50 Å / Num. obs: 35035 / % possible obs: 87.8 % / Redundancy: 6.2 % / Biso Wilson estimate: 105.94 Å2 / Rmerge(I) obs: 0.099 / Rpim(I) all: 0.042 / Rrim(I) all: 0.108 / Χ2: 1.598 / Net I/av σ(I): 22.551 / Net I/σ(I): 8.2 / Num. measured all: 217360
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.389-3.463.60.5619870.7140.2970.640.92551
3.46-3.524.10.56911070.7260.2840.6391.03856.4
3.52-3.594.60.45912560.8450.2160.510.97563.3
3.59-3.664.80.42413390.8630.1940.4691.04369.6
3.66-3.745.20.42415190.8810.190.4671.06677.1
3.74-3.835.50.39616430.910.1730.4341.05983.9
3.83-3.925.90.32517290.9480.1380.3551.08287.7
3.92-4.036.10.2918030.9560.1230.3161.10890.5
4.03-4.156.30.24817940.9710.1040.271.20192.2
4.15-4.286.40.20318710.980.0850.2211.29293.7
4.28-4.446.50.15918880.9860.0660.1731.3596.2
4.44-4.616.50.13619220.9890.0570.1481.47797
4.61-4.826.70.12619550.990.0530.1371.58598.4
4.82-5.086.80.11819770.9920.0490.1281.66199.3
5.08-5.46.90.11219890.9920.0460.1221.76199.5
5.4-5.817.10.11220170.9940.0460.1211.76100
5.81-6.47.20.09920080.9950.040.1071.773100
6.4-7.327.20.08220270.9960.0330.0891.86799.9
7.32-9.216.90.05920640.9980.0240.0632.28699.7
9.21-5060.05421400.9970.0240.0593.25897.2

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIXrefinement
HKL-2000data reduction
SCALEPACKdata scaling
PHASERphasing
PDB_EXTRACT3.15data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4JB9

4jb9


Resolution: 3.389→39.895 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 33.68 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3011 1735 4.97 %
Rwork0.244 33159 -
obs0.2469 34894 85.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 343.54 Å2 / Biso mean: 144.9489 Å2 / Biso min: 59.95 Å2
Refinement stepCycle: final / Resolution: 3.389→39.895 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17768 0 366 0 18134
Biso mean--143.77 --
Num. residues----2294
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218606
X-RAY DIFFRACTIONf_angle_d0.55825243
X-RAY DIFFRACTIONf_chiral_restr0.0232870
X-RAY DIFFRACTIONf_plane_restr0.0033226
X-RAY DIFFRACTIONf_dihedral_angle_d9.9896713
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 12

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.3889-3.48860.3738860.30831547163349
3.4886-3.60110.4005990.29831938203761
3.6011-3.72970.30981120.29122284239672
3.7297-3.87890.33851440.29732600274483
3.8789-4.05530.36521520.27342836298889
4.0553-4.26890.29751420.2512955309792
4.2689-4.5360.27751520.21212973312594
4.536-4.88560.26341710.19783075324696
4.8856-5.37620.25711570.21143121327898
5.3762-6.15170.27061580.24123237339599
6.1517-7.74130.32611770.2832533430100
7.7413-39.89780.30031850.23433340352597
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)
13.5797-1.1335-0.95444.1975-1.07675.4765-0.01141.2675-0.2316-0.1892-0.4543-0.43770.1690.96440.33180.88870.01920.10452.1596-0.2920.61922.4396224.23588.0057
24.3619-1.0830.65693.4375-0.95328.12990.14941.7234-0.844-0.2695-0.2910.50751.43550.16730.11981.1208-0.05510.06151.9952-0.61560.7894-0.1606221.95617.0099
34.6471-2.9214-0.87836.1150.71288.9608-0.85790.62180.20510.240.2384-0.4775-0.2199-0.25370.45370.8129-0.1093-0.05881.8746-0.15350.4171-5.1603240.696626.6796
47.99852.14081.61558.0965-2.12846.70421.29891.24172.45620.6904-0.40320.3706-1.1799-0.52250.25560.54370.3893-0.4811.7971-0.37580.9749-23.9987258.212353.4846
59.19641.0403-0.70957.88170.36095.9021-0.7834-1.1232-0.31140.11010.2302-0.5865-0.18260.07660.50220.69280.1063-0.14651.1799-0.03190.47073.0251233.394747.1152
68.4457-5.36622.06915.6231-1.7057.72230.00430.1843-1.03210.1020.23651.297-0.20480.819-0.21820.5778-0.1003-0.11421.0269-0.03420.8181-27.5478244.65761.9685
75.7878-1.49981.385.3937-3.29914.2462-0.36131.6219-0.48420.0205-0.0302-0.36160.04050.57910.37971.0168-0.22270.07651.5932-0.4810.780315.4736162.68094.325
85.03450.5061-0.96143.9909-1.62969.0768-0.60251.6421-1.6757-0.66020.54240.30960.5337-0.29860.03180.8478-0.42630.04521.4086-0.54430.9877-7.2032160.41393.265
98.515-1.8544-1.81297.2576-1.54972.6684-0.76970.3153-0.11780.19360.3214-0.3575-0.3860.22270.35910.6579-0.06-0.21991.1895-0.12720.5482-11.6787176.383325.0231
101.91721.3023-0.8369.2402-6.80585.11330.97621.75010.11831.7439-0.88621.4382-2.30080.81450.21690.82020.2214-0.37552.0433-0.52191.6691-23.7755193.097553.1535
118.7838-0.4842.06228.53860.87682.3253-0.0467-1.2572-0.17070.19560.3421-0.71940.6680.9456-0.32160.64630.0826-0.15161.18750.21460.7791-2.7328165.716943.6903
127.7109-6.8012-0.22916.4875-2.71639.14210.57080.129-0.64220.6940.35391.8596-0.8555-0.4902-0.82390.8149-0.13450.33390.9528-0.02471.4723-28.4463181.003362.6304
135.8125-2.00791.22186.3918-2.73464.3515-0.20430.719-0.1726-0.0894-0.2089-0.31450.89250.23640.43110.96110.30820.1151.5882-0.31580.694116.2225285.22469.3542
147.24030.2508-1.21756.6829-2.66684.5824-0.57970.6083-1.2042-0.11570.34271.06130.77480.01570.25890.8850.18630.24771.3751-0.39821.1187-5.9278283.01669.3725
158.0398-1.5324-4.86485.01170.77753.0339-0.32010.2038-0.45370.1097-0.4444-0.1688-0.0812-0.71460.77260.90610.226-0.06811.1744-0.32090.7791-11.5436300.652529.5273
165.07271.20633.8117.9485-1.56993.66180.40170.93230.25880.5979-1.86620.8172-0.8303-0.92351.17520.49590.2671-0.10761.7051-0.57321.0075-28.0142319.20855.5242
179.21513.81843.42383.93462.90389.7215-0.5479-0.9107-0.20650.1297-0.0394-0.2582-0.1310.16320.56351.17570.47550.1191.08770.28570.7487-2.6624293.481349.4798
186.6796-2.06354.66.9155-1.33284.7387-0.2743-0.7314-0.93890.98620.17461.4886-0.3483-0.48030.18940.8936-0.01650.32441.2107-0.18070.9763-30.5317306.129765.7776
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'G' and (resid 44:252 or resid 477:492)G44 - 252
2X-RAY DIFFRACTION1chain 'G' and (resid 44:252 or resid 477:492)G477 - 492
3X-RAY DIFFRACTION2chain 'G' and (resid 253:476 )G253 - 476
4X-RAY DIFFRACTION3chain 'H' and (resid 1:122 )H1 - 122
5X-RAY DIFFRACTION4chain 'H' and (resid 123:230 )H123 - 230
6X-RAY DIFFRACTION5chain 'L' and (resid 1:102)L1 - 102
7X-RAY DIFFRACTION6chain 'L' and (resid 103:230)L103 - 230
8X-RAY DIFFRACTION7chain 'A' and (resid 44:252 or resid 477:492)A44 - 252
9X-RAY DIFFRACTION7chain 'A' and (resid 44:252 or resid 477:492)A477 - 492
10X-RAY DIFFRACTION8chain 'A' and (resid 253:476 )A253 - 476
11X-RAY DIFFRACTION9chain 'B' and (resid 1:122)B1 - 122
12X-RAY DIFFRACTION10chain 'B' and (resid 123:230)B123 - 230
13X-RAY DIFFRACTION11chain 'C' and (resid 1:102)C1 - 102
14X-RAY DIFFRACTION12chain 'C' and (resid 103:231 )C103 - 231
15X-RAY DIFFRACTION13chain 'D' and (resid 44:252 or resid 477:492)D44 - 252
16X-RAY DIFFRACTION13chain 'D' and (resid 44:252 or resid 477:492)D477 - 492
17X-RAY DIFFRACTION14chain 'D' and (resid 253:476 )D253 - 476
18X-RAY DIFFRACTION15chain 'E' and (resid 1:122)E1 - 122
19X-RAY DIFFRACTION16chain 'E' and (resid 123:231)E123 - 231
20X-RAY DIFFRACTION17chain 'F' and (resid 1:102 )F1 - 102
21X-RAY DIFFRACTION18chain 'F' and (resid 103 through 213 )F0

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