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- PDB-2y1l: Caspase-8 in Complex with DARPin-8.4 -

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Basic information

Entry
Database: PDB / ID: 2y1l
TitleCaspase-8 in Complex with DARPin-8.4
Components
  • (CASPASE-8Caspase 8) x 2
  • AC-IETD-CHO
  • DARPIN-8.4
KeywordsHYDROLASE/INHIBITOR / HYDROLASE-INHIBITOR COMPLEX / DEVD DARPIN / ANKYRIN REPEAT PROTEIN / RIBOSOME DISPLAY / APOPTOSIS
Function / homology
Function and homology information


caspase-8 / syncytiotrophoblast cell differentiation involved in labyrinthine layer development / death effector domain binding / FasL/ CD95L signaling / TRAIL signaling / CD95 death-inducing signaling complex / ripoptosome / Defective RIPK1-mediated regulated necrosis / Apoptotic execution phase / Activation, myristolyation of BID and translocation to mitochondria ...caspase-8 / syncytiotrophoblast cell differentiation involved in labyrinthine layer development / death effector domain binding / FasL/ CD95L signaling / TRAIL signaling / CD95 death-inducing signaling complex / ripoptosome / Defective RIPK1-mediated regulated necrosis / Apoptotic execution phase / Activation, myristolyation of BID and translocation to mitochondria / TRAIL-activated apoptotic signaling pathway / TRIF-mediated programmed cell death / TLR3-mediated TICAM1-dependent programmed cell death / Microbial modulation of RIPK1-mediated regulated necrosis / Regulation by c-FLIP / CASP8 activity is inhibited / Dimerization of procaspase-8 / Caspase activation via Death Receptors in the presence of ligand / positive regulation of macrophage differentiation / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / self proteolysis / response to cobalt ion / cysteine-type endopeptidase activity involved in apoptotic signaling pathway / death-inducing signaling complex / natural killer cell activation / negative regulation of necroptotic process / CLEC7A/inflammasome pathway / regulation of tumor necrosis factor-mediated signaling pathway / activation of cysteine-type endopeptidase activity / tumor necrosis factor receptor binding / death receptor binding / cysteine-type endopeptidase activity involved in apoptotic process / TNFR1-induced proapoptotic signaling / execution phase of apoptosis / RIPK1-mediated regulated necrosis / regulation of innate immune response / B cell activation / pyroptosis / Apoptotic cleavage of cellular proteins / positive regulation of proteolysis / macrophage differentiation / protein maturation / cellular response to organic cyclic compound / extrinsic apoptotic signaling pathway via death domain receptors / Caspase-mediated cleavage of cytoskeletal proteins / response to tumor necrosis factor / cysteine-type peptidase activity / negative regulation of canonical NF-kappaB signal transduction / extrinsic apoptotic signaling pathway / regulation of cytokine production / T cell activation / proteolysis involved in protein catabolic process / positive regulation of interleukin-1 beta production / Regulation of NF-kappa B signaling / apoptotic signaling pathway / Regulation of TNFR1 signaling / NOD1/2 Signaling Pathway / Regulation of necroptotic cell death / cellular response to mechanical stimulus / positive regulation of neuron apoptotic process / response to estradiol / lamellipodium / cell body / heart development / peptidase activity / scaffold protein binding / angiogenesis / positive regulation of canonical NF-kappaB signal transduction / response to ethanol / mitochondrial outer membrane / response to lipopolysaccharide / cytoskeleton / positive regulation of cell migration / positive regulation of apoptotic process / cysteine-type endopeptidase activity / apoptotic process / ubiquitin protein ligase binding / protein-containing complex binding / protein-containing complex / mitochondrion / proteolysis / nucleoplasm / identical protein binding / cytosol / cytoplasm
Similarity search - Function
Caspase-8 / Death effector domain / Death effector domain / Death effector domain (DED) profile. / Death effector domain / Caspase-like / Rossmann fold - #1460 / Ankyrin repeat-containing domain / Peptidase family C14A, His active site / Caspase family histidine active site. ...Caspase-8 / Death effector domain / Death effector domain / Death effector domain (DED) profile. / Death effector domain / Caspase-like / Rossmann fold - #1460 / Ankyrin repeat-containing domain / Peptidase family C14A, His active site / Caspase family histidine active site. / Peptidase C14, caspase non-catalytic subunit p10 / Peptidase family C14A, cysteine active site / Caspase family cysteine active site. / Caspase family p10 domain profile. / Peptidase C14A, caspase catalytic domain / Caspase, interleukin-1 beta converting enzyme (ICE) homologues / Peptidase C14, p20 domain / Caspase family p20 domain profile. / : / Caspase domain / Caspase-like domain superfamily / Death-like domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Alpha-Beta Plaits / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Biological speciesHOMO SAPIENS (human)
SYNTHETIC CONSTRUCT (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsBarandun, J. / Schroeder, T. / Mittl, P.R.E. / Grutter, M.G.
CitationJournal: To be Published
Title: Caspase-8 in Complex with Darpin-8.4
Authors: Schroeder, T. / Barandun, J. / Grutter, M.G.
History
DepositionDec 8, 2010Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 28, 2011Provider: repository / Type: Initial release
Revision 1.1Apr 11, 2012Group: Other
Revision 1.2Oct 3, 2012Group: Derived calculations
Revision 1.3Mar 12, 2014Group: Source and taxonomy
Revision 1.4Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CASPASE-8
B: CASPASE-8
C: CASPASE-8
D: CASPASE-8
E: DARPIN-8.4
F: DARPIN-8.4
G: AC-IETD-CHO
H: AC-IETD-CHO
hetero molecules


Theoretical massNumber of molelcules
Total (without water)98,11316
Polymers97,5148
Non-polymers5998
Water12,340685
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20210 Å2
ΔGint-129.4 kcal/mol
Surface area27030 Å2
MethodPISA
Unit cell
Length a, b, c (Å)61.000, 81.600, 163.200
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 , 3 types, 6 molecules ACBDEF

#1: Protein CASPASE-8 / Caspase 8 / CASP-8 / APOPTOTIC CYSTEINE PROTEASE / APOPTOTIC PROTEASE MCH- CAP4 / FADD-HOMOLOGOUS ICE/CED-3- ...CASP-8 / APOPTOTIC CYSTEINE PROTEASE / APOPTOTIC PROTEASE MCH- CAP4 / FADD-HOMOLOGOUS ICE/CED-3-LIKE PROTEASE / FADD-LIKE ICE / FLICE / ICE-LIKE APOPTOTIC PROTEASE 5 / MORT1-ASSOCIATED CED-3 HOMOLOG / MACH


Mass: 18027.570 Da / Num. of mol.: 2 / Fragment: P18 SUBUNIT, RESIDUES 218-374
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q14790, caspase-8
#2: Protein CASPASE-8 / Caspase 8 / CASP-8 / APOPTOTIC CYSTEINE PROTEASE / APOPTOTIC PROTEASE MCH- CAP4 / FADD-HOMOLOGOUS ICE/CED-3- ...CASP-8 / APOPTOTIC CYSTEINE PROTEASE / APOPTOTIC PROTEASE MCH- CAP4 / FADD-HOMOLOGOUS ICE/CED-3-LIKE PROTEASE / FADD-LIKE ICE / FLICE / ICE-LIKE APOPTOTIC PROTEASE 5 / MORT1-ASSOCIATED CED-3 HOMOLOG / MACH


Mass: 12036.565 Da / Num. of mol.: 2 / Fragment: P10 SUBUNIT, RESIDUES 376-479
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q14790, caspase-8
#3: Protein DARPIN-8.4


Mass: 18216.504 Da / Num. of mol.: 2 / Fragment: N3C, RESIDUES 1-169
Source method: isolated from a genetically manipulated source
Details: IN-VITRO EVOLVED SEQUENCE / Source: (gene. exp.) SYNTHETIC CONSTRUCT (others) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): K-12 / Variant (production host): XL1BLUE

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Protein/peptide , 1 types, 2 molecules GH

#4: Protein/peptide AC-IETD-CHO


Mass: 476.478 Da / Num. of mol.: 2 / Fragment: AC-IETD-CHO INHIBITOR, RESIDUES 1-4 / Source method: obtained synthetically / Source: (synth.) SYNTHETIC CONSTRUCT (others)

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Non-polymers , 3 types, 693 molecules

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


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#6: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C2H6O2
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 685 / 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: 4

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Sample preparation

CrystalDensity Matthews: 2.01 Å3/Da / Density % sol: 38 % / Description: NONE
Crystal growpH: 4.8
Details: 100 MM CITRIC ACID PH 4.9 (RT), 200 MM LI2SO4, 22.5% PEG 4K.

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Data collection

DiffractionMean temperature: 90 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 23, 2010
RadiationMonochromator: SI / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.8→48.86 Å / Num. obs: 75862 / % possible obs: 99.4 % / Observed criterion σ(I): 3.76 / Redundancy: 4.9 % / Biso Wilson estimate: 17.41 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 13.29
Reflection shellResolution: 1.8→1.85 Å / Redundancy: 4.88 % / Rmerge(I) obs: 0.51 / Mean I/σ(I) obs: 3.76 / % possible all: 98.9

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 1QDU AND 2QYJ

1qdu

2qyj


Resolution: 1.8→48.857 Å / SU ML: 0.23 / σ(F): 1.34 / Phase error: 20.21 / Stereochemistry target values: ML
Details: RAMACHANDRAN OUTLIERS LYS A 320, LYS C 229 ARE IN CLOSE PROXIMITY TO CRYSTAL CONTACTS OR DARPIN BINDING SITE. ELECTRON DENSITY WELL RESOLVED. ASN B 408, MET C 228, ASN D 408 ARE ALSO PRESENT ...Details: RAMACHANDRAN OUTLIERS LYS A 320, LYS C 229 ARE IN CLOSE PROXIMITY TO CRYSTAL CONTACTS OR DARPIN BINDING SITE. ELECTRON DENSITY WELL RESOLVED. ASN B 408, MET C 228, ASN D 408 ARE ALSO PRESENT IN HIGH RESOLUTION CASPASE-8 STRUCTURES SUCH AS 1QTN, 3KJN, 3KJQ.
RfactorNum. reflection% reflection
Rfree0.2178 3812 5 %
Rwork0.1801 --
obs0.182 75836 99.37 %
Solvent computationShrinkage radii: 0.61 Å / VDW probe radii: 0.9 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 27.637 Å2 / ksol: 0.369 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--0.081 Å20 Å20 Å2
2---0.2874 Å20 Å2
3---0.3685 Å2
Refinement stepCycle: LAST / Resolution: 1.8→48.857 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6203 0 35 685 6923
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096391
X-RAY DIFFRACTIONf_angle_d1.2018639
X-RAY DIFFRACTIONf_dihedral_angle_d13.0012382
X-RAY DIFFRACTIONf_chiral_restr0.061965
X-RAY DIFFRACTIONf_plane_restr0.0041132
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.86430.30793650.25367049X-RAY DIFFRACTION99
1.8643-1.9390.2663870.21797115X-RAY DIFFRACTION99
1.939-2.02720.24623440.19757175X-RAY DIFFRACTION99
2.0272-2.13410.23943840.18977101X-RAY DIFFRACTION99
2.1341-2.26780.23644120.17887168X-RAY DIFFRACTION99
2.2678-2.44290.22263590.17347178X-RAY DIFFRACTION100
2.4429-2.68870.20453880.16967203X-RAY DIFFRACTION100
2.6887-3.07780.21653600.17347274X-RAY DIFFRACTION100
3.0778-3.87740.23830.16867272X-RAY DIFFRACTION99
3.8774-48.87540.19374300.17297489X-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)
11.8997-0.38560.55012.5038-1.3661.43150.1396-0.0259-0.2772-0.41-0.11110.08140.27090.0616-0.02180.13240.01120.0230.0702-0.00260.1106-10.1337-0.1054-18.5611
20.18650.3399-0.1771.7005-0.76570.15190.0511-0.0149-0.01340.2761-0.079-0.0117-0.04430.02520.02230.12380.00720.01820.0571-0.00650.0438-12.712825.5246-13.393
30.46960.2229-0.04660.297-0.23280.52960.01820.02360.06640.10790.01190.1295-0.0726-0.0162-0.0250.08860.01620.02220.09670.01030.092-16.180126.8476-16.4851
40.43260.01330.06831.2039-0.12120.98480.0153-0.02580.00670.1233-0.0495-0.0847-0.07440.11610.03090.0890.00050.0090.07420.00890.0634-5.186623.5717-14.8853
50.3752-0.20310.01360.46410.17950.5109-0.05650.05330.02710.0840.04740.0363-0.04030.09610.01570.0513-0.01230.01970.06480.00480.0615-6.375119.4943-24.4428
60.0539-0.19210.24011.8677-1.50132.01030.04410.08090.10460.0955-0.1536-0.2837-0.11250.35160.11690.10650.0016-0.00360.11230.01290.1004-2.115414.1596-25.0854
70.45890.5517-0.00511.68520.29560.296-0.0390.12050.0738-0.0940.03860.1372-0.0275-0.0346-0.0080.09880.01040.01470.15440.0270.1035-19.885823.7881-26.8754
83.05354.1968-0.12485.9702-1.00844.4736-0.20580.32480.5719-0.35060.22040.68540.411-0.6511-0.00270.1258-0.03690.00870.16890.00150.1843-20.44086.8276-25.6358
90.37590.1859-0.16321.50920.10910.6139-0.03630.18360.0613-0.2177-0.0160.23690.0034-0.21990.01080.11130.0262-0.01040.16450.01560.1318-20.2421.5377-35.157
100.323-0.3246-0.08970.11420.28230.7717-0.0864-0.05510.0060.00320.0328-0.02640.1363-0.06620.04850.0950.00110.02140.1212-0.00210.0855-10.586810.9469-27.203
110.6653-0.7161-1.26691.03611.58783.4970.03750.1621-0.12110.0232-0.17840.1887-0.0426-0.33190.18790.1256-0.02450.00360.1249-0.03870.1215-14.30845.9003-48.4504
120.2556-0.4545-0.08571.4595-0.0650.8949-0.072-0.10230.17640.04980.0312-0.3229-0.01720.27370.03130.0876-0.0156-0.01160.1601-0.04560.160317.331714.6268-45.3473
131.4788-0.66980.2040.9873-0.08560.84650.0390.1823-0.123-0.0591-0.0131-0.04820.14890.1233-0.02880.11360.01830.01650.1066-0.01740.10422.52042.1908-49.4491
141.4213-0.1309-0.27760.3615-0.09220.78010.0127-0.00280.1891-0.0680.0044-0.0371-0.09580.0556-0.02090.0928-0.00940.00460.0597-0.02590.08193.479917.1653-48.6486
151.344-0.7613-0.391.0844-0.03461.0214-0.0075-0.16660.1467-0.02410.0087-0.15460.00450.1381-0.11720.06440.00270.010.0853-0.0260.0812-0.194415.659-39.7892
162.3582-0.4233-1.93971.66140.17881.5489-0.09150.29210.22930.19190.04990.15-0.0004-0.32990.04720.11590.0088-0.01570.1203-0.01420.1082-13.906119.3569-42.1983
170.5465-0.4578-0.50190.90230.5650.917-0.0389-0.21220.05950.00780.0721-0.16590.07960.1771-0.04170.14270.0267-0.00030.1585-0.03180.12347.22444.8169-35.8904
182.66070.46230.56160.09430.0221.83440.0593-0.1693-0.42960.35710.1741-0.350.337-0.0341-0.18290.1666-0.0142-0.00220.1118-0.02040.1852-8.1439-2.404-38.0222
190.2056-0.30820.30592.4604-0.34742.9964-0.1303-0.0632-0.03030.01510.0666-0.30720.07320.51210.06430.1130.06160.00450.195-0.00430.13125.65892.7696-28.4232
200.70360.06090.09740.1667-0.26371.1793-0.07230.0007-0.04630.09160.0799-0.0080.0637-0.04410.01680.09450.01420.01710.0801-0.02350.0664-11.15067.9773-39.6595
212.1018-0.66551.70832.62720.7162.60050.0523-0.0984-0.5417-0.0398-0.12850.70670.1245-0.29590.07060.12640.0021-0.04880.1497-0.05940.2448-12.26976.5587-68.8792
220.9028-0.2631-0.22581.37990.27610.25020.04280.1839-0.024-0.3308-0.01910.0337-0.1114-0.0338-0.01340.19470.0206-0.0240.1095-0.02110.0763-5.110415.5202-69.7497
231.72290.6451-0.30190.8638-0.26141.2303-0.00090.1302-0.0104-0.2482-0.0257-0.1841-0.08620.0142-0.03180.1958-0.00850.07540.0802-0.020.11438.413419.3893-69.0508
241.3838-0.71550.40480.4713-0.30973.22550.0131-0.0770.3559-0.07660.1123-0.6926-0.73390.2157-0.13740.218-0.05960.0730.0564-0.03010.296814.264129.2079-63.1277
250.06460.16590.35912.76051.21563.24230.12690.4480.70410.15890.2451-1.60540.06091.5602-0.27570.14460.04650.0490.6259-0.02170.701522.632421.799-64.3526
263.22050.3766-1.07183.8271-2.01593.0111-0.1819-0.2803-0.5667-0.49660.17180.59760.4314-0.2251-0.07320.1746-0.0877-0.08190.15330.10750.2816-10.90485.19465.9277
270.1255-0.08760.06850.69-0.8051.09550.1254-0.2018-0.3038-0.20580.00610.10540.42470.0869-0.110.1332-0.0001-0.04080.16760.0940.1853-2.78936.15528.2481
280.66010.10660.29670.78770.01741.62240.0549-0.1866-0.00650.01020.01930.09060.07210.0479-0.04230.0671-0.0138-0.00810.12420.03490.0825-4.793116.6576.3324
291.05310.58680.55681.8155-0.8171.4828-0.0209-0.10110.03580.1218-0.0656-0.0386-0.21360.09450.07310.1011-0.01110.00080.0962-0.00850.067-2.099831.43213.9108
302.3942-0.18981.28080.4346-1.38894.8906-0.1841-0.04730.4676-0.014-0.15150.1189-1.5606-0.15940.25930.45160.0465-0.03520.1635-0.0320.2393-5.804742.6698-0.5667
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 222:231)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 232:247)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 248:284)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 285:335)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 336:371)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 392:407)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 408:429)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 430:440)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 441:460)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 461:478)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 223:235)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 236:260)
13X-RAY DIFFRACTION13(CHAIN C AND RESID 261:284)
14X-RAY DIFFRACTION14(CHAIN C AND RESID 285:334)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 335:370)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 390:402)
17X-RAY DIFFRACTION17(CHAIN D AND RESID 403:429)
18X-RAY DIFFRACTION18(CHAIN D AND RESID 430:440)
19X-RAY DIFFRACTION19(CHAIN D AND RESID 441:464)
20X-RAY DIFFRACTION20(CHAIN D AND RESID 465:479)
21X-RAY DIFFRACTION21(CHAIN E AND RESID 13:34)
22X-RAY DIFFRACTION22(CHAIN E AND RESID 35:89)
23X-RAY DIFFRACTION23(CHAIN E AND RESID 90:135)
24X-RAY DIFFRACTION24(CHAIN E AND RESID 136:156)
25X-RAY DIFFRACTION25(CHAIN E AND RESID 157:168)
26X-RAY DIFFRACTION26(CHAIN F AND RESID 13:33)
27X-RAY DIFFRACTION27(CHAIN F AND RESID 34:46)
28X-RAY DIFFRACTION28(CHAIN F AND RESID 47:88)
29X-RAY DIFFRACTION29(CHAIN F AND RESID 89:154)
30X-RAY DIFFRACTION30(CHAIN F AND RESID 155:168)

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