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- PDB-5fo8: Crystal Structure of Human Complement C3b in Complex with MCP (CCP1-4) -

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Basic information

Entry
Database: PDB / ID: 5fo8
TitleCrystal Structure of Human Complement C3b in Complex with MCP (CCP1-4)
Components
  • (COMPLEMENT C3) x 2
  • MEMBRANE COFACTOR PROTEIN
KeywordsLIPID BINDING / LIPID BIANDING / COMPLEMENT SYSTEM / IMMUNE SYSTEM / PLASMA PROTEIN / COFA ACTIVITY / REGULATORS OF COMPLEMENT ACTIVITY
Function / homology
Function and homology information


sequestering of extracellular ligand from receptor / inner acrosomal membrane / negative regulation of complement activation, classical pathway / positive regulation of transforming growth factor beta production / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / T cell mediated immunity / vertebrate eye-specific patterning ...sequestering of extracellular ligand from receptor / inner acrosomal membrane / negative regulation of complement activation, classical pathway / positive regulation of transforming growth factor beta production / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / T cell mediated immunity / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / regulation of Notch signaling pathway / complement-mediated synapse pruning / Alternative complement activation / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / positive regulation of type IIa hypersensitivity / positive regulation of memory T cell differentiation / complement receptor mediated signaling pathway / complement-dependent cytotoxicity / positive regulation of D-glucose transmembrane transport / complement activation / complement activation, alternative pathway / positive regulation of regulatory T cell differentiation / endopeptidase inhibitor activity / neuron remodeling / amyloid-beta clearance / B cell activation / positive regulation of vascular endothelial growth factor production / positive regulation of interleukin-10 production / complement activation, classical pathway / single fertilization / Purinergic signaling in leishmaniasis infection / positive regulation of T cell proliferation / Peptide ligand-binding receptors / Regulation of Complement cascade / response to bacterium / Post-translational protein phosphorylation / fatty acid metabolic process / positive regulation of receptor-mediated endocytosis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of protein phosphorylation / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / signaling receptor activity / virus receptor activity / secretory granule lumen / G alpha (i) signalling events / blood microparticle / adaptive immune response / immune response / cadherin binding / G protein-coupled receptor signaling pathway / receptor ligand activity / endoplasmic reticulum lumen / inflammatory response / signaling receptor binding / negative regulation of gene expression / innate immune response / focal adhesion / Neutrophil degranulation / positive regulation of gene expression / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Membrane cofactor protein CD46 / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / : / S-adenosyl-L-methionine-dependent methyltransferases / Macroglobulin (MG2) domain / Immunoglobulin-like - #1940 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 ...Membrane cofactor protein CD46 / Jelly Rolls - #1540 / N-terminal domain of TfIIb - #160 / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Alpha-macroglobulin, receptor-binding domain / : / S-adenosyl-L-methionine-dependent methyltransferases / Macroglobulin (MG2) domain / Immunoglobulin-like - #1940 / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / Complement C3-like, NTR domain / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / Anaphylatoxin, complement system domain / Complement Module, domain 1 / : / Anaphylatoxin domain signature. / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Complement Module; domain 1 / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Macroglobulin domain MG4 / Macroglobulin domain MG4 / Glycosyltransferase - #20 / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Alpha-2-macroglobulin / Macroglobulin domain / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Other non-globular / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / Single Sheet / Special / Ribbon / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Jelly Rolls / Immunoglobulin-like fold / Immunoglobulins / Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Complement C3 / Membrane cofactor protein
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å
AuthorsForneris, F. / Wu, J. / Xue, X. / Gros, P.
CitationJournal: Embo J. / Year: 2016
Title: Regulators of Complement Activity Mediate Inhibitory Mechanisms Through a Common C3B-Binding Mode.
Authors: Forneris, F. / Wu, J. / Xue, X. / Ricklin, D. / Lin, Z. / Sfyroera, G. / Tzekou, A. / Volokhina, E. / Granneman, J.C. / Hauhart, R. / Bertram, P. / Liszewski, M.K. / Atkinson, J.P. / Lambris, J.D. / Gros, P.
History
DepositionNov 18, 2015Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 6, 2016Provider: repository / Type: Initial release
Revision 1.1Jun 1, 2016Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Other / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_database_status / 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.src_method / _entity.type / _pdbx_database_status.status_code_sf / _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_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_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 20, 2024Group: Structure summary / Category: 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
A: COMPLEMENT C3
B: COMPLEMENT C3
C: MEMBRANE COFACTOR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,92837
Polymers203,9313
Non-polymers2,99734
Water8,863492
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area18170 Å2
ΔGint16.1 kcal/mol
Surface area76110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)82.830, 130.630, 233.830
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21221

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Components

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Protein , 3 types, 3 molecules ABC

#1: Protein COMPLEMENT C3 / C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 1 / C3ADESARG / COMPLEMENT C3B


Mass: 71393.320 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 23-667 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human)
References: UniProt: P01024, alternative-complement-pathway C3/C5 convertase
#2: Protein COMPLEMENT C3 / C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING PROTEIN 1 / C3ADESARG / COMPLEMENT C3B


Mass: 104074.148 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 749-1663 / Source method: isolated from a natural source / Details: PURIFIED FROM HUMAN PLASMA / Source: (natural) HOMO SAPIENS (human)
References: UniProt: P01024, alternative-complement-pathway C3/C5 convertase
#3: Protein MEMBRANE COFACTOR PROTEIN / TLX / TROPHOBLAST LEUKOCYTE COMMON ANTIGEN / MEMBRANE COFACTOR PROTEIN MCP / CD46


Mass: 28463.486 Da / Num. of mol.: 1 / Fragment: CCP DOMAINS 1-4, UNP RESIDUES 35-286
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: P15529

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Sugars , 2 types, 2 molecules

#4: 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
#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

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Non-polymers , 2 types, 524 molecules

#6: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 32 / Source method: obtained synthetically / Formula: C2H6O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 492 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsRESIDUE 1013 HAS BEEN CONVERTED FROM GLN TO GLU IN CONVERSION OF C3 PROTEIN TO C3B

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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: 3.4 Å3/Da / Density % sol: 63.9 % / Description: NONE
Crystal growDetails: 100MM AMMONIUM CITRATE 7% PEG 3350 5MM GLUTATHIONE 50MM BIS-TRIS PROPANE, PH 6.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.933
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.933 Å / Relative weight: 1
ReflectionResolution: 2.4→69.95 Å / Num. obs: 98854 / % possible obs: 99 % / Observed criterion σ(I): 1.5 / Redundancy: 3.8 % / Biso Wilson estimate: 42.69 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 6.8
Reflection shellResolution: 2.4→2.44 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.41 / Mean I/σ(I) obs: 2 / % possible all: 96.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
iMOSFLMdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2I07, PDB ENTRY 3O8E

2i07

3o8e


Resolution: 2.4→57.02 Å / SU ML: 0.24 / σ(F): 1.34 / Phase error: 22.76 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2188 4925 5 %
Rwork0.1879 --
obs0.1895 98766 98.81 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 67 Å2
Refinement stepCycle: LAST / Resolution: 2.4→57.02 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13118 0 195 492 13805
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00513578
X-RAY DIFFRACTIONf_angle_d0.85118342
X-RAY DIFFRACTIONf_dihedral_angle_d15.8535104
X-RAY DIFFRACTIONf_chiral_restr0.0572079
X-RAY DIFFRACTIONf_plane_restr0.0042352
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.42730.30431490.26353007X-RAY DIFFRACTION96
2.4273-2.45580.31051790.25263049X-RAY DIFFRACTION98
2.4558-2.48580.27251620.2413069X-RAY DIFFRACTION98
2.4858-2.51720.30021550.22693038X-RAY DIFFRACTION97
2.5172-2.55040.2771540.2213067X-RAY DIFFRACTION99
2.5504-2.58530.31081570.22383083X-RAY DIFFRACTION97
2.5853-2.62220.27431490.21623109X-RAY DIFFRACTION99
2.6222-2.66140.27641440.21673072X-RAY DIFFRACTION98
2.6614-2.7030.25941520.22133090X-RAY DIFFRACTION99
2.703-2.74730.27481590.22563098X-RAY DIFFRACTION99
2.7473-2.79470.28651650.21573078X-RAY DIFFRACTION99
2.7947-2.84550.25781590.21653110X-RAY DIFFRACTION99
2.8455-2.90020.25051510.21113121X-RAY DIFFRACTION99
2.9002-2.95940.24881690.21133126X-RAY DIFFRACTION99
2.9594-3.02370.25521550.20853123X-RAY DIFFRACTION100
3.0237-3.09410.27451910.20763118X-RAY DIFFRACTION99
3.0941-3.17140.24881900.2073083X-RAY DIFFRACTION99
3.1714-3.25720.23881490.21493168X-RAY DIFFRACTION100
3.2572-3.3530.28241780.20913142X-RAY DIFFRACTION100
3.353-3.46120.23051710.19883153X-RAY DIFFRACTION100
3.4612-3.58490.22921660.20143139X-RAY DIFFRACTION100
3.5849-3.72840.23771580.1953032X-RAY DIFFRACTION96
3.7284-3.89810.21491660.17783185X-RAY DIFFRACTION100
3.8981-4.10350.20671530.17223195X-RAY DIFFRACTION100
4.1035-4.36050.1821760.15093172X-RAY DIFFRACTION100
4.3605-4.69710.17041930.14073178X-RAY DIFFRACTION100
4.6971-5.16950.15661700.1443219X-RAY DIFFRACTION100
5.1695-5.91690.20491570.16883229X-RAY DIFFRACTION100
5.9169-7.4520.20751590.18253256X-RAY DIFFRACTION99
7.452-57.03650.141890.1723332X-RAY DIFFRACTION98
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)
10.01430.00650.0060.006-0.00080.00340.00340.203-0.0546-0.00820.01610.0554-0.0089-0.0791-00.3721-0.00430.1110.66820.01370.36489.931110.008411.8608
20.00610.0018-0.00560.001-0.00410.0118-0.03690.0196-0.07030.0193-0.01610.0214-0.0903-0.1307-0.00020.4156-0.01350.12070.467-0.00880.327710.663718.516623.3981
30.08140.03990.05810.02690.02510.0158-0.03960.0657-0.0264-0.02050.0445-0.0627-0.21690.016800.68970.07830.12810.38740.00010.400333.499648.700427.8136
40.032-0.0103-0.0040.01080.0030.02540.0151-0.0443-0.17090.01680.0582-0.001-0.0916-0.05890.00010.43810.01980.11840.5835-0.00870.382748.77821.436215.9283
50.03730.0110.03890.00570.01330.0494-0.0120.0736-0.0938-0.0581-0.0935-0.057-0.0621-0.0274-0.01110.41490.05510.1870.52290.02320.365529.56813.5663.4808
60.01740.00120.00880.00220.00510.0103-0.03820.0802-0.0887-0.0283-0.0039-0.0036-0.17560.06160.00010.6685-0.02310.15350.38980.08420.393526.939936.71536.4248
70.0765-0.0249-0.00430.01680.0190.0208-0.0355-0.0068-0.1391-0.0464-0.0361-0.0164-0.2085-0.06390.01310.52030.00980.1170.42990.01210.30124.065230.323217.8282
80.27840.02070.08840.33520.06630.10220.0156-0.0050.05-0.2476-0.1860.178-0.2438-0.1785-0.19740.6780.14540.0353-0.04450.02760.169218.004360.066428.2928
90.2049-0.03410.02950.1068-0.02230.11430.00820.0471-0.01070.01040.0218-0.0210.0126-0.090600.1303-0.00870.01020.302-0.03040.2753-9.59191.298349.9512
100.2177-0.03730.0840.05670.00330.04320.021-0.01980.1661-0.01-0.04860.0939-0.2069-0.0632-0.02130.54270.03110.0770.0765-0.01140.271926.988566.42142.3006
110.00750.0025-0.00280.01310.00480.014-0.0223-0.0065-0.09890.0149-0.0765-0.00140.1358-0.00620.00010.45540.0556-0.06630.2101-0.02490.49028.279696.109353.3772
120.00520.0008-0.01140.0319-0.01240.0216-0.0311-0.0964-0.05480.10660.02610.01790.15790.017700.3436-0.0235-0.00030.2163-0.02630.515.971296.982557.3938
130.0014-0.0032-0.00340.00370.00290.00210.0022-0.01830.0846-0.0143-0.0360.0125-0.0757-0.012700.73230.2190.08340.54130.13410.5736-9.017740.418930.4738
14-0.00040.00030.00050.0007-0.00190.0003-0.00280.00440.0206-0.03670.0146-0.0121-0.04960.0107-00.57740.26080.0530.63880.16040.5222-9.374637.572422.2321
150.0006-0.0003-00.00220.00210.00050.01370.0091-0.0057-0.00940.01890.01110.0379-0.031300.43840.01170.01540.6692-0.00150.4331-16.03758.292227.546
160.00040.0018-0.00050.00430.00260.00240.00050.01250.0512-0.0173-0.01020.00130.0291-0.0329-0.00010.47010.00070.06520.70050.01880.3511-7.7068.882525.8837
17-0.0004-0.0002-0.00010.00030.00070.0006-0.00530.01-0.0079-0.0093-0.00410.00020.0068-0.01-00.6349-0.0246-0.0120.6227-0.08720.4475-9.7969-0.316315.06
1800.00060.0010.00110.00190.0024-0.0285-0.0130.0442-0.03010.01410.00880.0332-0.063400.5104-0.0296-0.07770.6812-0.02680.5089-15.94928.790319.442
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESID 1 THROUGH 67 )
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESID 68 THROUGH 112 )
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESID 113 THROUGH 347 )
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESID 348 THROUGH 432 )
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESID 433 THROUGH 515 )
6X-RAY DIFFRACTION6CHAIN 'A' AND (RESID 516 THROUGH 560 )
7X-RAY DIFFRACTION7CHAIN 'A' AND (RESID 561 THROUGH 643 )
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESID 731 THROUGH 1011 )
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESID 1012 THROUGH 1237 )
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESID 1238 THROUGH 1496 )
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESID 1497 THROUGH 1543 )
12X-RAY DIFFRACTION12CHAIN 'B' AND (RESID 1544 THROUGH 1641 )
13X-RAY DIFFRACTION13CHAIN 'C' AND (RESID 124 THROUGH 166 )
14X-RAY DIFFRACTION14CHAIN 'C' AND (RESID 167 THROUGH 190 )
15X-RAY DIFFRACTION15CHAIN 'C' AND (RESID 191 THROUGH 201 )
16X-RAY DIFFRACTION16CHAIN 'C' AND (RESID 202 THROUGH 222 )
17X-RAY DIFFRACTION17CHAIN 'C' AND (RESID 223 THROUGH 235 )
18X-RAY DIFFRACTION18CHAIN 'C' AND (RESID 236 THROUGH 252 )

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