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- PDB-6hpr: Crystal structure of cIAP1 RING domain bound to UbcH5B-Ub and a n... -

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Basic information

Entry
Database: PDB / ID: 6hpr
TitleCrystal structure of cIAP1 RING domain bound to UbcH5B-Ub and a non-covalent Ub
Components
  • Baculoviral IAP repeat-containing protein 2
  • Polyubiquitin-B
  • Ubiquitin-conjugating enzyme E2 D2
KeywordsLIGASE / Ubiquitin / E3 / cIAP1 / UbcH5B / ubiquitin ligase
Function / homology
Function and homology information


negative regulation of ripoptosome assembly involved in necroptotic process / FBXO family protein binding / regulation of RIG-I signaling pathway / positive regulation of protein K48-linked ubiquitination / regulation of non-canonical NF-kappaB signal transduction / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / regulation of necroptotic process / regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway / positive regulation of protein K63-linked ubiquitination / CD40 receptor complex ...negative regulation of ripoptosome assembly involved in necroptotic process / FBXO family protein binding / regulation of RIG-I signaling pathway / positive regulation of protein K48-linked ubiquitination / regulation of non-canonical NF-kappaB signal transduction / TNF receptor superfamily (TNFSF) members mediating non-canonical NF-kB pathway / regulation of necroptotic process / regulation of nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway / positive regulation of protein K63-linked ubiquitination / CD40 receptor complex / (E3-independent) E2 ubiquitin-conjugating enzyme / negative regulation of necroptotic process / XY body / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / non-canonical NF-kappaB signal transduction / hypothalamus gonadotrophin-releasing hormone neuron development / TNFR1-induced proapoptotic signaling / female meiosis I / positive regulation of protein monoubiquitination / RIPK1-mediated regulated necrosis / regulation of reactive oxygen species metabolic process / fat pad development / mitochondrion transport along microtubule / E2 ubiquitin-conjugating enzyme / regulation of toll-like receptor signaling pathway / regulation of innate immune response / Apoptotic cleavage of cellular proteins / female gonad development / seminiferous tubule development / necroptotic process / male meiosis I / ubiquitin conjugating enzyme activity / regulation of cell differentiation / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / canonical NF-kappaB signal transduction / protein K48-linked ubiquitination / protein autoubiquitination / response to cAMP / energy homeostasis / tumor necrosis factor-mediated signaling pathway / regulation of neuron apoptotic process / regulation of proteasomal protein catabolic process / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of innate immune responses to cytosolic DNA / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / neuron projection morphogenesis / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / regulation of mitochondrial membrane potential / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / ubiquitin binding / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Translesion synthesis by POLI / Regulation of activated PAK-2p34 by proteasome mediated degradation / positive regulation of protein ubiquitination / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER
Similarity search - Function
BIRC2/BIRC3, UBA domain / : / BIRC2/3-like, UBA domain / : / Caspase recruitment domain / BIR repeat. / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat ...BIRC2/BIRC3, UBA domain / : / BIRC2/3-like, UBA domain / : / Caspase recruitment domain / BIR repeat. / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Zinc/RING finger domain, C3HC4 (zinc finger) / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Herpes Virus-1 / Ubiquitin-conjugating enzyme/RWD-like / Death-like domain superfamily / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-B / Ubiquitin-conjugating enzyme E2 D2 / Baculoviral IAP repeat-containing protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.7 Å
AuthorsPatel, A. / Huang, D.T.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Cancer Research UKA23278 United Kingdom
CitationJournal: J. Biol. Chem. / Year: 2019
Title: Structural insights into non-covalent ubiquitin activation of the cIAP1-UbcH5B∼ubiquitin complex.
Authors: Patel, A. / Sibbet, G.J. / Huang, D.T.
History
DepositionSep 21, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 12, 2018Provider: repository / Type: Initial release
Revision 1.1Dec 19, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _citation_author.name
Revision 1.2Dec 26, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ..._citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID
Revision 1.3Mar 6, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation.year / _citation_author.identifier_ORCID
Revision 1.4May 8, 2019Group: Advisory / Data collection / Derived calculations
Category: diffrn_source / pdbx_validate_close_contact ...diffrn_source / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.5Jul 10, 2019Group: Data collection / Category: diffrn_source / Item: _diffrn_source.pdbx_synchrotron_site
Revision 1.6Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _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: Baculoviral IAP repeat-containing protein 2
B: Polyubiquitin-B
C: Ubiquitin-conjugating enzyme E2 D2
D: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,0626
Polymers41,9314
Non-polymers1312
Water3,999222
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: surface plasmon resonance, Other biochemical assays, NMR
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4810 Å2
ΔGint-19 kcal/mol
Surface area16870 Å2
MethodPISA
Unit cell
Length a, b, c (Å)79.190, 53.600, 78.540
Angle α, β, γ (deg.)90.00, 107.57, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Baculoviral IAP repeat-containing protein 2 / Cellular inhibitor of apoptosis 1 / C-IAP1 / IAP homolog B / Inhibitor of apoptosis protein 2 / ...Cellular inhibitor of apoptosis 1 / C-IAP1 / IAP homolog B / Inhibitor of apoptosis protein 2 / hIAP2 / RING finger protein 48 / RING-type E3 ubiquitin transferase BIRC2 / TNFR2-TRAF-signaling complex protein 2


Mass: 7305.725 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: cIAP1 residues 556-C with N-terminal GS resulted from TEV cleavage
Source: (gene. exp.) Homo sapiens (human) / Gene: BIRC2, API1, MIHB, RNF48 / Production host: Escherichia coli (E. coli)
References: UniProt: Q13490, RING-type E3 ubiquitin transferase
#2: Protein Polyubiquitin-B


Mass: 8922.141 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Ubiquitin residues 1-76 contains N-terminal GSGGS after TEV cleavage. Chain D Gly76 forms isopeptide linkage with Chain C Lys85.
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG47
#3: Protein Ubiquitin-conjugating enzyme E2 D2 / (E3-independent) E2 ubiquitin-conjugating enzyme D2 / E2 ubiquitin-conjugating enzyme D2 / ...(E3-independent) E2 ubiquitin-conjugating enzyme D2 / E2 ubiquitin-conjugating enzyme D2 / Ubiquitin carrier protein D2 / Ubiquitin-conjugating enzyme E2(17)KB 2 / Ubiquitin-conjugating enzyme E2-17 kDa 2 / Ubiquitin-protein ligase D2 / p53-regulated ubiquitin-conjugating enzyme 1


Mass: 16781.264 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: UbcH5B residues 1-147. Cys85 is mutated to Lys and forms isopeptide linkage with ubiquitin's Gly76 in chain D.
Source: (gene. exp.) Homo sapiens (human) / Gene: UBE2D2, PUBC1, UBC4, UBC5B, UBCH4, UBCH5B / Production host: Escherichia coli (E. coli)
References: UniProt: P62837, E2 ubiquitin-conjugating enzyme, (E3-independent) E2 ubiquitin-conjugating enzyme
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: Zn
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 222 / 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: 1.89 Å3/Da / Density % sol: 34.94 %
Crystal growTemperature: 292 K / Method: vapor diffusion, sitting drop / Details: 0.2 M ammonium fluoride and 15% (w/v) PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: May 27, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 1.7→23.52 Å / Num. obs: 34206 / % possible obs: 98.8 % / Redundancy: 3.3 % / CC1/2: 0.998 / Rmerge(I) obs: 0.063 / Rpim(I) all: 0.04 / Rrim(I) all: 0.075 / Net I/σ(I): 13.8
Reflection shellResolution: 1.7→1.74 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.539 / Mean I/σ(I) obs: 2 / CC1/2: 0.632 / % possible all: 94.7

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Processing

Software
NameVersionClassification
PHENIX(1.10_2142: ???)refinement
xia2data reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3EB6, 3ZNI

3eb6

3zni


Resolution: 1.7→23.515 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 20.46
RfactorNum. reflection% reflection
Rfree0.1972 1744 5.1 %
Rwork0.1704 --
obs0.1718 34206 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.7→23.515 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2784 0 2 222 3008
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072851
X-RAY DIFFRACTIONf_angle_d0.9223880
X-RAY DIFFRACTIONf_dihedral_angle_d16.1671758
X-RAY DIFFRACTIONf_chiral_restr0.06457
X-RAY DIFFRACTIONf_plane_restr0.006500
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.750.29951400.25582578X-RAY DIFFRACTION95
1.75-1.80650.26091330.22872663X-RAY DIFFRACTION98
1.8065-1.8710.23711520.20612681X-RAY DIFFRACTION98
1.871-1.94590.22371490.20072688X-RAY DIFFRACTION99
1.9459-2.03440.23431480.1952686X-RAY DIFFRACTION99
2.0344-2.14160.21231340.18012728X-RAY DIFFRACTION99
2.1416-2.27570.24431490.16892700X-RAY DIFFRACTION99
2.2757-2.45120.22031340.1752737X-RAY DIFFRACTION99
2.4512-2.69760.19131540.16942723X-RAY DIFFRACTION99
2.6976-3.08720.18731420.16662741X-RAY DIFFRACTION100
3.0872-3.88670.17971640.15352732X-RAY DIFFRACTION100
3.8867-23.51760.15211450.14652805X-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)
12.37813.39362.59356.84874.58593.2009-0.76051.0463-0.4041-0.44660.9886-0.5349-1.09940.7152-0.16030.7581-0.26830.08820.4848-0.12440.3938-8.30434.688733.4518
25.00420.5566-1.60294.1905-1.52524.5867-0.0265-0.0785-0.0134-0.03050.00640.316-0.0268-0.45850.01960.1156-0.0287-0.00350.1787-0.02490.0971-11.3224-15.576828.6709
37.8282-7.53593.04032.1048-4.58042.1223-0.6008-0.12580.46540.84430.334-0.3488-0.17820.20090.17090.31350.0302-0.06250.321-0.09130.41537.035515.83622.0174
42.0362-0.53851.99922.0224-0.00924.0627-0.3089-0.57271.2232-0.03240.496-0.7479-0.6120.2218-0.16920.3354-0.02760.03280.2593-0.11080.63819.290822.737814.5544
55.12874.99461.29946.1381-0.02134.5975-0.3624-0.48850.2254-0.59080.2441-1.4109-0.42291.01170.08920.2541-0.09580.08230.3249-0.12230.623416.490315.445511.9651
65.8583-1.5190.25812.0432-0.15363.41480.16690.31790.465-1.07130.0669-0.1921-0.43860.1665-0.20.2937-0.05480.04560.1708-0.00280.2784.695314.40117.0938
74.65561.7546-2.08924.28510.28722.00530.2988-0.09450.6198-0.07250.16750.2707-0.4507-0.54-0.5360.18040.06150.020.2632-0.0130.2757-2.146815.93213.1253
85.418-2.5476-0.55565.82270.64992.66110.0079-0.24270.7364-0.22920.2695-1.0683-0.00770.9336-0.26060.2044-0.0042-0.02110.3988-0.10180.414715.29810.435814.283
98.81483.9388-1.78072.0526-0.76548.4831-0.2078-0.36021.16980.69090.14790.9979-0.6643-0.44310.15740.26340.0879-0.01690.1816-0.02220.3281-7.13581.169817.6806
102.1046-3.90737.58617.6492-2.34355.98210.2133-0.21990.56270.3748-0.2412-0.31980.4386-0.28990.09220.1709-0.03930.01390.32680.03690.18412.0663.63413.827
112.0416-0.71956.62152.8349-0.79217.4844-0.44180.13650.7384-0.04330.01090.1356-0.1443-0.04830.48890.1628-0.0119-0.0120.1093-0.01480.1403-0.40270.34988.3637
122.0345-4.6766-3.44139.8284-1.55544.2868-0.2428-0.60440.11170.38510.1203-0.4264-0.23120.42920.14910.1337-0.0263-0.03420.1993-0.00670.157421.0745-1.171914.0071
138.07717.4184-2.10649.4101-1.02292.1728-0.46980.3050.3598-0.7590.28150.2214-0.0027-0.09070.18860.1448-0.0001-0.00420.070.01070.09325.8132-1.78156.4637
143.7499-2.6436-2.69295.8448-3.03692.041-0.19750.3935-0.4692-0.1055-0.00530.48090.3547-0.66010.13380.1495-0.05060.00650.1877-0.03240.1368-7.7191-10.586611.6642
159.7785-3.56071.64832.1501-0.33990.33460.07420.49770.1611-0.0979-0.2101-0.2341-0.0001-0.00290.12630.1731-0.016-0.01010.14910.00250.117111.5442-6.13573.8525
164.2667-0.1472-2.20570.7850.07012.06030.01670.0889-0.1268-0.0644-0.0507-0.0108-0.0074-0.11360.02770.14230.0054-0.02070.07330.01210.08136.6881-11.446112.3047
177.5817-0.30540.47631.81470.77343.4644-0.00150.0999-0.77640.1248-0.00340.01860.38620.0304-0.01190.17640.01080.01910.0927-0.01780.175921.0971-17.79718.3946
188.6721-6.66833.41487.6831-5.02315.4945-0.10180.27470.6281-0.0614-0.1-0.7275-0.18920.23580.17690.1267-0.03830.02670.1387-0.0170.14724.6545-4.52335.4611
192.10623.17998.33855.42262.89169.3064-0.4005-0.98250.6050.1379-0.02930.0391-0.4866-0.43940.37680.1767-0.00370.02230.362-0.12490.19927.1575-3.177833.9148
208.1227-2.85834.36682.4952-0.88852.6294-0.4292-0.73610.44390.18530.0547-0.1191-0.628-0.56990.34860.2239-0.03240.01110.4701-0.10560.20168.0933-3.703237.5422
213.8833.63113.17882.00242.00958.9525-0.1991-0.3699-0.19890.58890.7506-0.70460.16940.4177-0.59750.16660.0107-0.01010.2829-0.04750.262120.1035-8.009938.6956
229.26671.069-3.87674.97011.20749.17320.0312-0.9443-0.40730.3746-0.25750.08580.4861-0.12480.24040.209-0.0709-0.03620.270.03410.11119.5931-13.179435.9903
233.94442.3161-1.87614.3453-1.23974.50170.0301-0.4195-0.12310.0486-0.17780.02690.0350.06180.14050.1143-0.0183-0.00130.18510.00320.10037.8959-14.677727.994
246.978-3.87237.06057.1078-6.392.06440.20630.212-0.2514-0.4462-0.2431-0.24430.3550.4034-0.01440.20620.01410.04310.19130.00380.157818.666-9.193326.6194
256.03392.3452.60145.44792.13743.944-0.0749-0.57460.7050.0224-0.1048-0.1018-0.32840.01290.19310.1598-0.03640.01450.154-0.03640.165514.9378-3.259329.9188
268.1604-8.8541.98539.91312.00772.0006-0.40890.1979-0.32980.39640.10130.3491.5685-0.53920.46190.2055-0.04480.03280.0794-0.03160.11399.4386-17.674917.0306
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 556 through 569 )
2X-RAY DIFFRACTION2chain 'A' and (resid 570 through 618 )
3X-RAY DIFFRACTION3chain 'B' and (resid 0 through 17 )
4X-RAY DIFFRACTION4chain 'B' and (resid 18 through 34 )
5X-RAY DIFFRACTION5chain 'B' and (resid 35 through 44 )
6X-RAY DIFFRACTION6chain 'B' and (resid 45 through 56 )
7X-RAY DIFFRACTION7chain 'B' and (resid 57 through 65 )
8X-RAY DIFFRACTION8chain 'B' and (resid 66 through 74 )
9X-RAY DIFFRACTION9chain 'C' and (resid 2 through 15 )
10X-RAY DIFFRACTION10chain 'C' and (resid 16 through 28 )
11X-RAY DIFFRACTION11chain 'C' and (resid 29 through 38 )
12X-RAY DIFFRACTION12chain 'C' and (resid 39 through 48 )
13X-RAY DIFFRACTION13chain 'C' and (resid 49 through 55 )
14X-RAY DIFFRACTION14chain 'C' and (resid 56 through 65 )
15X-RAY DIFFRACTION15chain 'C' and (resid 66 through 74 )
16X-RAY DIFFRACTION16chain 'C' and (resid 75 through 110 )
17X-RAY DIFFRACTION17chain 'C' and (resid 111 through 130 )
18X-RAY DIFFRACTION18chain 'C' and (resid 131 through 147 )
19X-RAY DIFFRACTION19chain 'D' and (resid -1 through 11 )
20X-RAY DIFFRACTION20chain 'D' and (resid 12 through 17 )
21X-RAY DIFFRACTION21chain 'D' and (resid 18 through 22 )
22X-RAY DIFFRACTION22chain 'D' and (resid 23 through 34 )
23X-RAY DIFFRACTION23chain 'D' and (resid 35 through 44 )
24X-RAY DIFFRACTION24chain 'D' and (resid 45 through 56 )
25X-RAY DIFFRACTION25chain 'D' and (resid 57 through 71 )
26X-RAY DIFFRACTION26chain 'D' and (resid 72 through 76 )

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