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- PDB-3hrz: Cobra Venom Factor (CVF) in complex with human factor B -

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Basic information

Entry
Database: PDB / ID: 3hrz
TitleCobra Venom Factor (CVF) in complex with human factor B
Components
  • (Cobra venom factor) x 3
  • Complement factor B
KeywordsIMMUNE SYSTEM / serine protease / glycosilated / multi-domain / complement system / convertase / Complement alternate pathway / Complement pathway / Disulfide bond / Glycoprotein / Immune response / Inflammatory response / Innate immunity / Secreted / Thioester bond / Cleavage on pair of basic residues / Glycation / Hydrolase / Protease / Sushi / Zymogen
Function / homology
Function and homology information


alternative-complement-pathway C3/C5 convertase / classical-complement-pathway C3/C5 convertase complex / complement binding / Alternative complement activation / Activation of C3 and C5 / complement activation, alternative pathway / complement activation / endopeptidase inhibitor activity / Regulation of Complement cascade / response to bacterium ...alternative-complement-pathway C3/C5 convertase / classical-complement-pathway C3/C5 convertase complex / complement binding / Alternative complement activation / Activation of C3 and C5 / complement activation, alternative pathway / complement activation / endopeptidase inhibitor activity / Regulation of Complement cascade / response to bacterium / toxin activity / blood microparticle / inflammatory response / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular exosome / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
ubp-family deubiquitinating enzyme fold - #20 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / ubp-family deubiquitinating enzyme fold ...ubp-family deubiquitinating enzyme fold - #20 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / ubp-family deubiquitinating enzyme fold / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Complement C3-like, NTR domain / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / Alpha-2-macroglobulin / Macroglobulin domain / 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 / von Willebrand factor type A domain / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / Single Sheet / von Willebrand factor A-like domain superfamily / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Immunoglobulins / Peptidase S1, PA clan / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
: / PHOSPHATE ION / Complement factor B / Cobra venom factor
Similarity search - Component
Biological speciesHomo sapiens (human)
Naja kaouthia (monocled cobra)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.2 Å
AuthorsJanssen, B.J.C. / Gomes, L. / Koning, R.I. / Svergun, D.I. / Koster, A.J. / Fritzinger, D.C. / Vogel, C.-W. / Gros, P.
CitationJournal: Embo J. / Year: 2009
Title: Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex
Authors: Janssen, B.J. / Gomes, L. / Koning, R.I. / Svergun, D.I. / Koster, A.J. / Fritzinger, D.C. / Vogel, C.W. / Gros, P.
History
DepositionJun 10, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 7, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / 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_struct_conn_angle / struct_asym / struct_conn / struct_ref_seq_dif / 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 / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _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_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 / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Mar 31, 2021Group: Source and taxonomy / Structure summary / Category: chem_comp / entity_src_gen
Item: _chem_comp.pdbx_synonyms / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain
Revision 2.2Oct 13, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 2.3Sep 6, 2023Group: 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: Cobra venom factor
B: Cobra venom factor
C: Cobra venom factor
D: Complement factor B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)227,03718
Polymers224,8224
Non-polymers2,21514
Water13,529751
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24920 Å2
ΔGint-123 kcal/mol
Surface area81780 Å2
MethodPISA
Unit cell
Length a, b, c (Å)128.890, 283.390, 134.400
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number20
Space group name H-MC2221

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Components

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Protein , 4 types, 4 molecules ABCD

#1: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 69581.984 Da / Num. of mol.: 1 / Fragment: residues 23-649 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#2: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 28418.568 Da / Num. of mol.: 1 / Fragment: residues 733-984 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#3: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 43626.547 Da / Num. of mol.: 1 / Fragment: residues 1264-1642 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#4: Protein Complement factor B / C3/C5 convertase / Properdin factor B / Glycine-rich beta glycoprotein / GBG / PBF2 / Complement ...C3/C5 convertase / Properdin factor B / Glycine-rich beta glycoprotein / GBG / PBF2 / Complement factor B Ba fragment / Complement factor B Bb fragment


Mass: 83194.859 Da / Num. of mol.: 1 / Fragment: residues 26-764 / Mutation: D279G,N285D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFB, BF, BFD / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
References: UniProt: P00751, alternative-complement-pathway C3/C5 convertase

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Sugars , 2 types, 4 molecules

#5: 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
#6: 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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
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 , 5 types, 761 molecules

#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#9: Chemical ChemComp-P6G / HEXAETHYLENE GLYCOL / POLYETHYLENE GLYCOL PEG400


Mass: 282.331 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C12H26O7 / Comment: precipitant*YM
#10: Chemical
ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: PO4
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 751 / 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: 2.73 Å3/Da / Density % sol: 54.94 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: PEG 3350, PEG 400, Na/K Phosphate, Bis-Tris propane, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9834 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 15, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9834 Å / Relative weight: 1
ReflectionResolution: 2.2→34 Å / Num. all: 124437 / Num. obs: 123939 / % possible obs: 99.6 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 34.8 Å2 / Rmerge(I) obs: 0.093 / Rsym value: 0.093 / Net I/σ(I): 11.8
Reflection shellResolution: 2.2→2.32 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.602 / Mean I/σ(I) obs: 2.6 / Num. measured all: 67190 / Num. unique all: 17889 / Rsym value: 0.602 / % possible all: 99.3

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
MOSFLMdata reduction
SCALA3.2.25data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
DNAdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2OK5 and 2I07

2ok5

2i07


Resolution: 2.2→33.487 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.846 / SU ML: 0.3 / Isotropic thermal model: Isotropic / σ(F): 1.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.226 2486 2.01 %random
Rwork0.18 ---
all0.181 124437 --
obs0.181 123930 99.51 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 36.48 Å2 / ksol: 0.333 e/Å3
Displacement parametersBiso max: 142.3 Å2 / Biso mean: 44.995 Å2 / Biso min: 13.73 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 2.2→33.487 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15051 0 136 751 15938
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00715538
X-RAY DIFFRACTIONf_angle_d1.11321037
X-RAY DIFFRACTIONf_chiral_restr0.0692366
X-RAY DIFFRACTIONf_plane_restr0.0042684
X-RAY DIFFRACTIONf_dihedral_angle_d16.7035703
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 18

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.2410.351400.2746625676598
2.241-2.2870.3091330.2526697683099
2.287-2.3370.2861560.2326646680299
2.337-2.3910.2691260.2216714684099
2.391-2.4510.2871450.2166640678599
2.451-2.5170.2431460.19967116857100
2.517-2.5910.2541250.1976708683399
2.591-2.6750.2661350.267156850100
2.675-2.770.2911280.20467266854100
2.77-2.8810.2541440.20267196863100
2.881-3.0120.2661300.19767516881100
3.012-3.1710.221410.20167716912100
3.171-3.370.2621430.18467506893100
3.37-3.6290.2231380.17467806918100
3.629-3.9940.1831330.15868226955100
3.994-4.5710.1671470.13668446991100
4.571-5.7540.1721300.13168737003100
5.754-33.4910.1841460.1556952709898
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)
11.43380.9274-0.28363.0338-0.85883.8302-0.04890.3093-0.0864-0.4918-0.1546-0.08790.0434-0.302-0.00040.47380.05270.01810.2443-0.02930.1975-21.846818.64819.2512
22.9157-0.7388-0.41123.0368-0.432.22960.09790.12310.0614-0.2304-0.0735-0.1358-0.12780.0643-0.00020.37340.00190.01560.1411-0.03440.1744-24.4273-16.812618.9354
32.64941.60381.58063.9761.87362.6039-0.14610.00360.0706-0.05580.0398-0.103-0.1879-0.00950.00020.32610.01680.01860.12130.01160.1625-25.7249-21.607751.9437
41.6922-0.1680.21072.5491-0.9993.35280.0301-0.11990.05330.3701-0.03170.067-0.1551-0.0249-0.00030.5680.0667-0.010.1641-0.02050.2121-25.179412.847149.6955
51.85960.8230.47282.89090.07732.02460.0242-0.00660.13520.1437-0.04240.2633-0.4233-0.1824-0.00020.5050.12340.00830.1489-0.03530.2018-31.345724.284430.0326
61.65950.7805-0.5782.74450.33471.50830.0133-0.010.2511-0.1637-0.05390.5638-0.3285-0.267-0.00020.36570.0797-0.03750.1867-0.05060.3084-46.8226-15.62424.1985
70.07660.48770.30641.49910.0848-0.0131-0.0282-0.0311-0.20490.0677-0.1325-0.3660.0266-0.00080.00060.48770.04450.0310.2066-0.00210.3088-22.22076.19427.7886
80.4898-0.52630.17550.07390.1943-0.0117-0.51470.3663-0.2351-0.16660.52450.68150.3645-0.73830.00120.4636-0.06740.04010.3550.01910.4903-52.3286-46.456229.0398
92.4108-0.5323-0.34211.97440.27381.85390.00910.0257-0.06960.15760.01030.16940.1392-0.2246-00.3747-0.02620.03960.184-0.02080.2337-41.1186-47.733734.3573
102.47790.1339-0.86281.3304-0.54853.5375-0.1527-0.0546-0.3207-0.1819-0.0153-0.10050.2219-0.0926-0.00070.375-0.00270.01450.25750.01590.4366-6.5894-33.2468.8212
112.73660.629-0.44833.22790.5862.40240.0036-0.1967-0.19120.2594-0.045-0.27560.45130.0641-0.00020.44880.0212-0.01450.1394-0.01250.212-28.5076-50.331652.5063
120.6325-1.14240.21220.65390.33720.6314-0.05710.4585-0.4911-0.2821-0.0234-0.0040.3432-0.1081-0.00090.6985-0.0340.02350.2038-0.09240.4004-27.7391-63.250531.1007
133.46680.07191.71794.299-0.1813.9797-0.0455-0.17180.03360.66150.1281-0.14120.17720.1618-0.00010.69870.046-0.0140.1451-0.04060.2228-34.4289-81.13718.3684
141.38930.1954-0.67511.8627-0.951.0893-0.0021-0.2272-0.8710.3336-0.2330.03480.69370.0443-0.00070.8768-0.06880.14480.5499-0.03950.9076-61.3756-63.800513.6533
152.84040.1488-1.07682.81691.02782.62570.0339-0.1431-0.05390.0237-0.22430.1991-0.1501-0.1914-0.00050.4129-0.0165-0.01720.2106-0.040.19-42.9122-38.46259.6221
162.3718-0.3032-0.36673.13040.10782.70380.21220.34930.1725-0.239-0.0431-0.1491-0.0993-0.05460.00020.4420.01540.04890.20250.01290.191-41.5895-60.4735-10.4939
173.154-0.4225-0.96271.1843-0.05692.87030.23810.29410.2403-0.3041-0.1766-0.2137-0.25430.2218-0.00020.56580.11490.09510.28670.08020.2534-75.9849-36.6759-12.8985
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 1:101A1 - 101
2X-RAY DIFFRACTION2chain A and (resseq 102:199 or resseq 187:187)A102 - 199
3X-RAY DIFFRACTION2chain A and (resseq 102:199 or resseq 187:187)A187
4X-RAY DIFFRACTION3chain A and resseq 200:318A200 - 318
5X-RAY DIFFRACTION4chain A and resseq 319:412A319 - 412
6X-RAY DIFFRACTION5chain A and resseq 413:520A413 - 520
7X-RAY DIFFRACTION6(chain A or chain B) and (resseq 521:559 or resseq 729:789)A0
8X-RAY DIFFRACTION7chain A and resseq 560:627A560 - 627
9X-RAY DIFFRACTION8chain B and resseq 711:728B711 - 728
10X-RAY DIFFRACTION9chain B and resseq 790:896B790 - 896
11X-RAY DIFFRACTION10(chain B or chain C) and (resseq 897:946 or resseq 1251:1313)B0
12X-RAY DIFFRACTION11chain C and (resseq 1314:1452 or resseq 1324:1324)C1314 - 1452
13X-RAY DIFFRACTION11chain C and (resseq 1314:1452 or resseq 1324:1324)C1324
14X-RAY DIFFRACTION12chain C and resseq 1453:1475C1453 - 1475
15X-RAY DIFFRACTION13chain C and resseq 1476:1620C1476 - 1620
16X-RAY DIFFRACTION14chain D and resseq 1:75D1 - 75
17X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D76 - 199
18X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D9097 - 9099
19X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D9117 - 9118
20X-RAY DIFFRACTION16chain D and (resseq 200:449 or resseq 9353:9353)D200 - 449
21X-RAY DIFFRACTION16chain D and (resseq 200:449 or resseq 9353:9353)D9353
22X-RAY DIFFRACTION17chain D and resseq 450:742D450 - 742

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