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- PDB-3ohx: Molecular Basis for Complement Recognition and Inhibition Determi... -

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Basic information

Entry
Database: PDB / ID: 3ohx
TitleMolecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b
Components
  • (Complement C3) x 3
  • Staphylococcal complement inhibitor
KeywordsIMMUNE SYSTEM / Complement Component C3 / Complement alternate pathway / Complement Pathway / Convertase / Immune evasion / Innate Immunity / Secreted Virulence Factor
Function / homology
Function and homology information


C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment ...C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / 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 / complement receptor mediated signaling pathway / complement-dependent cytotoxicity / positive regulation of D-glucose transmembrane transport / complement activation / complement activation, alternative pathway / endopeptidase inhibitor activity / neuron remodeling / amyloid-beta clearance / B cell activation / positive regulation of vascular endothelial growth factor production / complement activation, classical pathway / Purinergic signaling in leishmaniasis infection / 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 / positive regulation of protein phosphorylation / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / blood microparticle / G alpha (i) signalling events / secretory granule lumen / immune response / G protein-coupled receptor signaling pathway / receptor ligand activity / inflammatory response / endoplasmic reticulum lumen / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / 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 / Substrate Binding Domain Of Dnak; Chain:A; Domain 2 - #10 ...Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / 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 / Substrate Binding Domain Of Dnak; Chain:A; Domain 2 - #10 / 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 / : / 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 / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Macroglobulin domain MG4 / Macroglobulin domain MG4 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / 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 / Heat shock protein 70kD, C-terminal domain superfamily / Substrate Binding Domain Of Dnak; Chain:A; Domain 2 / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Single Sheet / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Immunoglobulin-like fold / Immunoglobulins / Up-down Bundle / Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Complement C3 / Staphylococcal complement inhibitor
Similarity search - Component
Biological speciesStaphylococcus aureus (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.503 Å
AuthorsGeisbrecht, B.V. / Garcia, B.L.
CitationJournal: J.Mol.Biol. / Year: 2010
Title: Molecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b.
Authors: Garcia, B.L. / Ramyar, K.X. / Tzekou, A. / Ricklin, D. / McWhorter, W.J. / Lambris, J.D. / Geisbrecht, B.V.
History
DepositionAug 18, 2010Deposition site: RCSB / Processing site: RCSB
SupersessionSep 1, 2010ID: 3NSA
Revision 1.0Sep 1, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Apr 24, 2013Group: Refinement description
Revision 1.3Nov 8, 2017Group: Refinement description / Category: software
Revision 1.4Jul 29, 2020Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_ref_seq_dif / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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: Complement C3
E: Complement C3
M: Staphylococcal complement inhibitor
P: Staphylococcal complement inhibitor
F: Complement C3
D: Complement C3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)289,67510
Polymers289,2338
Non-polymers4422
Water00
1
A: Complement C3
B: Complement C3
C: Complement C3
M: Staphylococcal complement inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,8385
Polymers144,6164
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
E: Complement C3
P: Staphylococcal complement inhibitor
F: Complement C3
D: Complement C3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)144,8385
Polymers144,6164
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)231.159, 231.497, 68.885
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212

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Components

#1: Protein Complement C3


Mass: 71393.320 Da / Num. of mol.: 2 / Fragment: Complement C3 beta chain / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#2: Protein Complement C3


Mass: 23621.244 Da / Num. of mol.: 2 / Fragment: Complement C3 alpha' chain fragment 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#3: Protein Complement C3


Mass: 39537.418 Da / Num. of mol.: 2 / Fragment: Complement C3 alpha' chain fragment 2 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#4: Protein Staphylococcal complement inhibitor / SCIN


Mass: 10064.370 Da / Num. of mol.: 2 / Fragment: Staphylococcal Complement Inhibitor-A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria) / Strain: Mu50 / ATCC 700699 / Gene: SAV1942, scn / Plasmid: PT7HMT / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q931M7
#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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 2
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
Has protein modificationY

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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: 3.19 Å3/Da / Density % sol: 61.4 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 2.5mg/ml protein, 0.1M HEPES, 10% PEG6000, 5% 2-Methyl-2,4-pentanediol, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 93 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 13, 2009 / Details: Mirror
RadiationMonochromator: Si(220) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionRedundancy: 7.4 % / Av σ(I) over netI: 10.55 / Number: 329081 / Rmerge(I) obs: 0.121 / Χ2: 1.01 / D res high: 3.5 Å / D res low: 50 Å / Num. obs: 44393 / % possible obs: 93.4
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
7.535099.910.0551.08912.9
5.987.5399.610.1170.98311.7
5.235.9896.910.1460.9749.6
4.755.2395.310.1411.0758.1
4.414.7594.410.1521.0646.8
4.154.4194.310.1851.0695.7
3.944.1591.710.2530.9335
3.773.9489.110.3240.8884.5
3.633.7786.910.3860.8424
3.53.6385.110.4660.8693.7
ReflectionResolution: 3.5→50 Å / Num. all: 44393 / Num. obs: 44393 / % possible obs: 93.4 % / Observed criterion σ(F): 2.4 / Observed criterion σ(I): 2.4 / Redundancy: 7.4 % / Rmerge(I) obs: 0.121 / Χ2: 1.01 / Net I/σ(I): 6.6
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique allΧ2Diffraction-ID% possible all
3.5-3.633.70.46639990.869185.1
3.63-3.7740.38640430.842186.9
3.77-3.944.50.32441610.888189.1
3.94-4.1550.25342990.933191.7
4.15-4.415.70.18544311.069194.3
4.41-4.756.80.15244291.064194.4
4.75-5.238.10.14145361.075195.3
5.23-5.989.60.14646250.974196.9
5.98-7.5311.70.11748180.983199.6
7.53-5012.90.05550521.089199.9

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Phasing

PhasingMethod: molecular replacement
Phasing MRRfactor: 53.64 / Model details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation3.5 Å46.96 Å
Translation3.5 Å46.96 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
PHASER2.1.4phasing
RESOLVEphasing
PHENIX1.5_2refinement
PDB_EXTRACT3.1data extraction
HKL-2000data collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.503→46.275 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.76 / SU ML: 0.47 / σ(F): 1.34 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2938 2014 4.55 %Random
Rwork0.2738 ---
obs0.2747 44269 93.09 %-
all-44338 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 12.826 Å2 / ksol: 0.29 e/Å3
Displacement parametersBiso max: 246.51 Å2 / Biso mean: 69.1916 Å2 / Biso min: 12.33 Å2
Baniso -1Baniso -2Baniso -3
1-5.9083 Å2-0 Å20 Å2
2---13.7816 Å20 Å2
3---22.3679 Å2
Refinement stepCycle: LAST / Resolution: 3.503→46.275 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19091 0 28 0 19119
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0119508
X-RAY DIFFRACTIONf_angle_d1.31826407
X-RAY DIFFRACTIONf_chiral_restr0.0783011
X-RAY DIFFRACTIONf_plane_restr0.0073393
X-RAY DIFFRACTIONf_dihedral_angle_d20.3637260
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.503-3.62860.35641790.33423730390984
3.6286-3.77380.32591920.32953869406187
3.7738-3.94540.29451880.31443967415589
3.9454-4.15330.33181910.30764115430691
4.1533-4.41340.30552010.27114242444394
4.4134-4.75380.27462110.24814229444094
4.7538-5.23160.24292010.23314342454395
5.2316-5.98730.31472070.24984405461297
5.9873-7.5380.27562180.25846084826100
7.538-46.2790.2552260.24184748497499
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)
10.2186-0.4192-0.08460.23670.38930.5250.12890.12150.13880.8610.25-0.3885-0.0936-0.463700.4027-0.1226-0.22870.38530.02710.4952-29.5919-56.370156.4155
20.45890.22730.10990.0222-0.2760.62150.05190.01880.1567-0.08840.0953-0.07370.099-0.028300.28510.0042-0.04320.1918-0.0173-0.0334-29.455-21.72527.8025
30.49720.2493-0.26020.0727-0.30460.3818-0.12280.06240.1795-0.03260.3122-0.47640.2778-0.267300.6525-0.0595-0.09180.4919-0.01420.3104-45.5454-50.571419.474
40.5659-0.00230.08240.37560.05760.56980.0770.0085-0.0308-0.0832-0.09580.30220.0792-0.0167-00.3298-0.0214-0.04820.2941-0.0540.4791-47.5963-56.107142.1339
5-0.27450.28470.32610.3576-0.6197-1.74670.2683-0.38730.28220.02760.18180.0812-0.33050.377500.20170.1003-0.12840.21640.11730.0097-39.0263-28.167242.5059
60.02590.02810.04370.0221-0.0516-0.00330.16910.0233-0.0873-0.2251-0.30980.0799-0.7885-0.2078-00.6882-0.09790.10210.39750.0630.469-25.1557-53.272838.0294
70.4899-0.10320.15410.25530.2055-0.04640.0016-0.30190.4570.05590.12350.33560.01210.0333-00.3577-0.02160.07150.1478-0.04260.0934-40.8368-5.093145.6067
80.09060.08680.01340.0344-0.2160.2661-0.24190.1386-0.2725-0.0580.2624-0.0079-0.0327-0.077300.2557-0.00520.05550.2054-0.04590.4359-32.856711.972729.2754
90.02810.2245-0.02330.1894-0.39470.0912-0.0388-0.04150.29030.0070.05440.0136-0.0317-0.01200.31890.04510.04570.2551-0.08360.4494-29.669216.436134.1339
100.98030.3724-0.09480.70650.06070.7742-0.03270.29320.4328-0.10780.1129-0.0745-0.15460.120400.3229-0.04320.10570.28210.08970.5013-23.677814.025513.671
110.70380.3110.17120.7339-0.17360.18960.0423-0.11470.25610.3634-0.11660.1771-0.06260.095500.5946-0.11880.09330.4386-0.13890.9321-6.94739.918338.3663
12-0.0398-0.10240.0958-0.0266-0.1086-0.015-0.05151.46120.6761-0.6561-0.9114-0.1630.57090.63020-0.1904-0.95810.2063-0.7097-0.38641.6985-10.284356.296741.8388
130.15680.09970.09680.1331-0.15720.4059-0.09630.48150.47070.14940.1156-0.14510.4260.0457-00.8045-0.1593-0.25510.74410.02750.6723-83.7983-57.126410.5457
140.5564-0.29430.84630.22090.19680.2890.11810.07270.06190.07440.08070.21040.0564-0.1588-00.1976-0.10740.02010.33570.18850.2387-92.7755-21.974721.0476
150.7620.3305-0.15190.23330.34280.14440.1084-0.19080.2759-0.120.0929-0.06660.12910.035700.3595-0.0162-0.05960.40470.05360.1872-79.3668-22.823751.6183
160.2881-0.1784-0.1657-0.00930.29910.22750.06720.0591-0.13650.35660.4591-0.3220.49340.551500.83750.0102-0.10520.64310.01530.4712-67.9655-50.873747.4238
170.22380.096-0.06550.3279-0.19530.53660.2178-0.14220.1353-0.21150.0288-0.20720.2472-0.0583-00.2922-0.0774-0.15920.26490.0480.3058-67.6267-42.30924.0362
180.1693-0.15540.0788-0.0992-0.0737-0.25541.78391.09851.20230.96510.44110.8181-2.317-1.61760-1.7068-0.7195-1.79720.1721-0.3155-1.0494-82.2646-49.405927.5219
190.76220.27690.39590.0790.28690.34330.00230.16180.2455-0.14070.07280.14740.06750.035100.2438-0.04590.05030.22120.15710.259-73.9222-5.532721.3039
200.0375-0.1081-0.15750.00830.33030.4240.46780.1618-0.03470.0726-0.1054-0.12210.1652-0.0557-00.1515-0.04120.11420.32730.20280.7361-85.80988.824237.736
210.1113-0.2750.15350.1063-0.06220.2385-0.15310.21270.15850.15160.25960.0218-0.1231-0.141300.22870.0330.06360.40680.15770.6233-84.152715.995933.311
220.5492-0.41290.440.449-0.04861.30810.1683-0.2915-0.1070.07310.05670.1763-0.58960.527600.4775-0.13470.26850.4727-0.0450.5961-90.518612.749254.9496
23-0.08740.0766-0.0628-0.01320.0441-0.01830.16180.0869-0.52650.19390.16520.2353-0.4431-0.0532-00.72070.02520.18870.63910.24590.8897-103.911624.84731.9399
240.7742-0.12210.35930.71470.10450.4450.3559-0.1296-0.0838-0.5026-0.21560.4398-0.05350.009600.0076-0.03540.07430.1864-0.06860.6397-108.990838.802428.5049
250.08630.04460.0601-0.0680.0963-0.03980.1239-0.22850.19160.057-0.4640.25280.12150.0327-00.1709-0.0858-0.06440.46520.19230.8434-105.768654.314221.8708
260.0011-0.01240.0214-0.0475-0.0591-0.03970.0956-0.00540.01390.2795-0.12960.16220.13660.1459-00.5817-0.11720.23170.4726-0.17030.8983-65.223626.047450.3181
270.1348-0.05170.07440.10570.1117-0.07510.0767-0.04930.59160.1846-0.3019-0.03310.05890.220200.4901-0.01440.19460.452-0.09490.6378-51.085516.760148.4337
280.00350.0067-0.00530.00310.01140.0070.0540.0599-0.13790.1036-0.12640.13630.1199-0.2801-00.7032-0.0752-0.03920.853-0.12130.8454-47.95413.819162.3835
290.03020.01850.0880.0389-0.11-0.07480.08330.18620.5087-0.165-0.0620.2947-0.4785-0.0344-00.4999-0.00660.16380.45230.1570.7903-50.360526.202716.5562
300.0998-0.0703-0.01150.123-0.1230.18690.01650.04510.5123-0.1020.15180.25930.0942-0.0328-00.3934-0.01640.05520.52710.19550.4532-64.251516.55518.4657
31-0.0005-0.0074-0.01520.00450.00090.01350.04210.0012-0.1946-0.07280.1342-0.13930.10470.300700.9789-0.05160.05110.95830.16530.5022-67.05173.51124.5391
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:105)A1 - 105
2X-RAY DIFFRACTION2(CHAIN A AND RESID 106:362)A106 - 362
3X-RAY DIFFRACTION3(CHAIN A AND RESID 363:433)A363 - 433
4X-RAY DIFFRACTION4(CHAIN A AND RESID 434:533)A434 - 533
5X-RAY DIFFRACTION5(CHAIN A AND RESID 534:629)A534 - 629
6X-RAY DIFFRACTION6(CHAIN A AND RESID 630:645)A630 - 645
7X-RAY DIFFRACTION7(CHAIN B AND RESID 729:812)B729 - 812
8X-RAY DIFFRACTION8(CHAIN B AND RESID 813:843)B813 - 843
9X-RAY DIFFRACTION9(CHAIN B AND RESID 844:912)B844 - 912
10X-RAY DIFFRACTION10(CHAIN C AND RESID 1336:1493)C1336 - 1493
11X-RAY DIFFRACTION11(CHAIN C AND RESID 1494:1609)C1494 - 1609
12X-RAY DIFFRACTION12(CHAIN C AND RESID 1610:1641)C1610 - 1641
13X-RAY DIFFRACTION13(CHAIN D AND RESID 1:105)D1 - 105
14X-RAY DIFFRACTION14(CHAIN D AND RESID 106:208)D106 - 208
15X-RAY DIFFRACTION15(CHAIN D AND RESID 209:362)D209 - 362
16X-RAY DIFFRACTION16(CHAIN D AND RESID 363:433)D363 - 433
17X-RAY DIFFRACTION17(CHAIN D AND RESID 434:586)D434 - 586
18X-RAY DIFFRACTION18(CHAIN D AND RESID 587:645)D587 - 645
19X-RAY DIFFRACTION19(CHAIN E AND RESID 729:812)E729 - 812
20X-RAY DIFFRACTION20(CHAIN E AND RESID 813:835)E813 - 835
21X-RAY DIFFRACTION21(CHAIN E AND RESID 836:912)E836 - 912
22X-RAY DIFFRACTION22(CHAIN F AND RESID 1336:1481)F1336 - 1481
23X-RAY DIFFRACTION23(CHAIN F AND RESID 1482:1498)F1482 - 1498
24X-RAY DIFFRACTION24(CHAIN F AND RESID 1503:1609)F1503 - 1609
25X-RAY DIFFRACTION25(CHAIN F AND RESID 1610:1641)F1610 - 1641
26X-RAY DIFFRACTION26(CHAIN M AND RESID 2:27)M2 - 27
27X-RAY DIFFRACTION27(CHAIN M AND RESID 28:77)M28 - 77
28X-RAY DIFFRACTION28(CHAIN M AND RESID 78:85)M78 - 85
29X-RAY DIFFRACTION29(CHAIN P AND RESID 2:27)P2 - 27
30X-RAY DIFFRACTION30(CHAIN P AND RESID 28:77)P28 - 77
31X-RAY DIFFRACTION31(CHAIN P AND RESID 78:85)P78 - 85

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