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- PDB-8vk9: Structure of UbV.d2.3 in complex with Ube2d2-S22R -

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Basic information

Entry
Database: PDB / ID: 8vk9
TitleStructure of UbV.d2.3 in complex with Ube2d2-S22R
Components
  • Ubiquitin variant D2.3
  • Ubiquitin-conjugating enzyme E2 D2
KeywordsTRANSFERASE / Ubiquitin conjugating enzyme / Ubiquitin variant / E2 enzyme / inhibitor
Function / homology
Function and homology information


(E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / protein autoubiquitination / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / PINK1-PRKN Mediated Mitophagy / Negative regulators of DDX58/IFIH1 signaling ...(E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / protein autoubiquitination / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / TICAM1, RIP1-mediated IKK complex recruitment / IKK complex recruitment mediated by RIP1 / PINK1-PRKN Mediated Mitophagy / Negative regulators of DDX58/IFIH1 signaling / Peroxisomal protein import / Regulation of TNFR1 signaling / Inactivation of CSF3 (G-CSF) signaling / protein modification process / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / CLEC7A (Dectin-1) signaling / FCERI mediated NF-kB activation / protein polyubiquitination / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / Downstream TCR signaling / Antigen processing: Ubiquitination & Proteasome degradation / E3 ubiquitin ligases ubiquitinate target proteins / Neddylation / ubiquitin-dependent protein catabolic process / protein ubiquitination / protein-containing complex / extracellular exosome / nucleoplasm / ATP binding / nucleus / cytosol
Similarity search - Function
Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like
Similarity search - Domain/homology
Ubiquitin-conjugating enzyme E2 D2
Similarity search - Component
Biological speciesHomo sapiens (human)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsMiddleton, A.J.
Funding support New Zealand, 1items
OrganizationGrant numberCountry
Health Research Council (HRC) New Zealand
CitationJournal: Febs J. / Year: 2024
Title: Structural and biophysical characterisation of ubiquitin variants that inhibit the ubiquitin conjugating enzyme Ube2d2.
Authors: McAlpine, J.M.R.B. / Zhu, J. / Pudjihartono, N. / Teyra, J. / Currie, M.J. / Tillett, Z.D. / Dobson, R.C.J. / Sidhu, S.S. / Day, C.L. / Middleton, A.J.
History
DepositionJan 8, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 25, 2024Provider: repository / Type: Initial release
Revision 1.1Nov 13, 2024Group: Database references / Structure summary / Category: citation / citation_author / pdbx_entry_details
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _pdbx_entry_details.has_protein_modification
Revision 1.2Dec 18, 2024Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID / _citation_author.name

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-conjugating enzyme E2 D2
B: Ubiquitin variant D2.3
C: Ubiquitin-conjugating enzyme E2 D2
D: Ubiquitin variant D2.3
E: Ubiquitin-conjugating enzyme E2 D2
F: Ubiquitin variant D2.3
G: Ubiquitin-conjugating enzyme E2 D2
H: Ubiquitin variant D2.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)110,90613
Polymers110,4468
Non-polymers4605
Water6,521362
1
A: Ubiquitin-conjugating enzyme E2 D2
B: Ubiquitin variant D2.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7043
Polymers27,6112
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1640 Å2
ΔGint-12 kcal/mol
Surface area11770 Å2
MethodPISA
2
C: Ubiquitin-conjugating enzyme E2 D2
D: Ubiquitin variant D2.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7964
Polymers27,6112
Non-polymers1842
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1930 Å2
ΔGint-11 kcal/mol
Surface area11970 Å2
MethodPISA
3
E: Ubiquitin-conjugating enzyme E2 D2
F: Ubiquitin variant D2.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7043
Polymers27,6112
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1580 Å2
ΔGint-10 kcal/mol
Surface area11820 Å2
MethodPISA
4
G: Ubiquitin-conjugating enzyme E2 D2
H: Ubiquitin variant D2.3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)27,7043
Polymers27,6112
Non-polymers921
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1400 Å2
ΔGint-9 kcal/mol
Surface area11410 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.850, 56.314, 117.499
Angle α, β, γ (deg.)86.48, 78.47, 60.32
Int Tables number1
Space group name H-MP1

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Components

#1: 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: 17188.605 Da / Num. of mol.: 4 / Mutation: C21S, S22R, C107S, C111S
Source method: isolated from a genetically manipulated source
Details: Contains an N-terminal linker / 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
#2: Protein
Ubiquitin variant D2.3


Mass: 10422.864 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: Contains N-terminal linker. Obtained from phage display.
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli (E. coli)
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 362 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationN

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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: 2.85 Å3/Da / Density % sol: 56.77 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7 / Details: 0.1 M Sodium HEPES pH 7.0, 15% w/v PEG 20,000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 25, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2→41.2 Å / Num. obs: 80451 / % possible obs: 97.5 % / Redundancy: 3 % / Biso Wilson estimate: 63.7 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.0528 / Net I/σ(I): 10.2
Reflection shellResolution: 2→2.07 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.765 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 7996 / CC1/2: 0.678 / % possible all: 96.7

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Processing

Software
NameVersionClassification
Aimlessdata scaling
XDSdata reduction
PHASERphasing
PHENIX1.20.1-4487refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→41.2 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 26.54 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2235 4061 5.05 %
Rwork0.1891 --
obs0.1908 80451 97.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2→41.2 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7233 0 30 362 7625
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037444
X-RAY DIFFRACTIONf_angle_d0.72210103
X-RAY DIFFRACTIONf_dihedral_angle_d6.2391003
X-RAY DIFFRACTIONf_chiral_restr0.0471125
X-RAY DIFFRACTIONf_plane_restr0.0071308
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.020.41891590.36322606X-RAY DIFFRACTION96
2.02-2.050.35781310.32872534X-RAY DIFFRACTION97
2.05-2.070.36041430.31452651X-RAY DIFFRACTION96
2.07-2.10.33261510.30532590X-RAY DIFFRACTION97
2.1-2.130.34581290.27722617X-RAY DIFFRACTION97
2.13-2.160.29751670.25552616X-RAY DIFFRACTION96
2.16-2.190.27081250.24362616X-RAY DIFFRACTION99
2.19-2.220.27351370.23952648X-RAY DIFFRACTION97
2.22-2.260.29881510.23932637X-RAY DIFFRACTION97
2.26-2.30.30261540.23512626X-RAY DIFFRACTION99
2.3-2.340.26111430.2312609X-RAY DIFFRACTION96
2.34-2.390.271480.22682622X-RAY DIFFRACTION99
2.39-2.440.26811660.22352658X-RAY DIFFRACTION97
2.44-2.490.26141440.22782613X-RAY DIFFRACTION98
2.49-2.550.26341230.23222682X-RAY DIFFRACTION97
2.55-2.610.2801940.22522661X-RAY DIFFRACTION99
2.61-2.680.27071430.23022664X-RAY DIFFRACTION97
2.68-2.760.25561160.22372656X-RAY DIFFRACTION99
2.76-2.850.24071390.2142663X-RAY DIFFRACTION97
2.85-2.950.27261440.21762669X-RAY DIFFRACTION98
2.95-3.070.27971470.22172616X-RAY DIFFRACTION99
3.07-3.210.25041510.21342628X-RAY DIFFRACTION98
3.21-3.380.25131420.21162624X-RAY DIFFRACTION97
3.38-3.590.23531220.19272659X-RAY DIFFRACTION97
3.59-3.870.21431320.17432620X-RAY DIFFRACTION97
3.87-4.250.20241660.1532685X-RAY DIFFRACTION99
4.25-4.870.1751530.13442620X-RAY DIFFRACTION98
4.87-6.130.17551160.15422691X-RAY DIFFRACTION98
6.13-41.20.13651250.14922609X-RAY DIFFRACTION96
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)
13.6061-2.0042.00914.2829-0.42264.62150.5103-0.336-0.51950.1925-0.12160.12380.3891-0.2732-0.07380.6790.06470.04270.35370.02380.4512-31.4994-31.6864-34.0816
22.1847-2.32460.49824.6736-0.63482.39670.26020.33010.0709-0.3953-0.4506-0.0696-0.0418-0.13240.01840.65120.05670.03210.3775-0.02610.3599-35.5509-19.3007-37.3316
33.1782-2.62410.00424.5144-0.04842.29370.075-0.06510.11770.1286-0.16740.2126-0.2806-0.2180.04160.59030.07410.02040.3724-0.05960.3944-45.1253-11.2159-33.6384
43.2442-0.8994-0.89723.5779-0.043.51050.24550.5907-0.0958-0.5247-0.2327-0.77480.58470.5142-0.02320.67990.22130.07350.50280.03640.5061-15.9359-38.5443-40.9437
53.0852-1.06680.4671.2606-0.36342.87660.40130.50251.2052-0.4464-0.1548-1.5943-0.90750.61170.11250.95450.27930.40570.9130.31451.1227-9.0925-30.7785-47.9046
62.9048-1.0867-0.51411.0368-1.27683.70650.39310.49650.4209-0.6629-0.1874-0.9718-0.16410.2947-0.08890.66810.11290.19890.57750.15430.8083-14.0485-31.2856-44.1701
72.57230.031-0.17662.46480.34946.1640.0056-0.04680.34310.71190.1106-0.5839-0.05190.99440.01330.4916-0.1693-0.03420.3708-0.01090.4635-20.8978-16.4905-2.0167
81.64541.07890.20643.424-0.52693.0978-0.0343-0.0139-0.1314-0.01920.07860.08160.0839-0.0716-0.01220.2754-0.06890.00930.32130.01840.359-29.9079-28.1937-7.9912
91.43520.162-0.01521.2511-0.20672.29410.1077-0.0533-0.32960.1273-0.0817-0.20390.36130.076-0.04620.3305-0.07230.00190.3710.03190.4164-27.4009-37.607-2.5635
101.0215-0.78520.98374.01711.6894.56970.2601-0.2914-1.52830.2765-0.29850.44090.8042-0.2039-0.07140.6566-0.1639-0.06870.4230.08530.6848-36.3666-52.6381-6.0795
111.8538-0.76610.70624.1658-0.77032.6059-0.20890.694-0.0571-1.32140.20130.32850.2827-0.0756-0.14280.5927-0.1649-0.05370.3797-0.02660.5101-38.5504-44.7413-16.8212
123.2918-0.5232-0.45172.78821.00713.8262-0.04280.25250.37380.72160.0432-0.1938-0.0724-0.01620.14020.7524-0.1307-0.05420.2943-0.04120.4995-24.1283-8.5658-3.2374
131.9011-1.37150.58291.71031.00863.0739-0.2168-0.56791.49811.9693-0.0207-0.568-1.83180.6906-0.97171.3271-0.2522-0.150.1565-0.09550.6625-24.03090.8081-2.7571
143.06770.92580.66550.68890.05762.7738-0.12530.60951.03780.67040.17920.31-1.45850.42620.17010.7377-0.0228-0.02020.2620.09820.6218-26.45983.638-13.0809
152.12350.0780.50853.39950.13632.32240.25630.42550.2776-0.00530.76560.769-1.6834-1.0810.31721.21750.19910.2850.5380.14861.0807-37.15910.8065-5.6327
164.9609-3.50.69913.7799-0.08030.20910.0858-0.77230.88931.12820.34750.7071-1.1763-1.09940.34721.02140.20620.34770.591-0.06790.8517-35.6237-4.31041.3004
175.24812.561-1.71346.1724-4.08172.78270.00010.22760.60730.57540.73851.6503-0.5182-0.61460.03080.5428-0.0542-0.03910.34620.04260.6522-30.4585-2.6631-13.3117
184.0216-1.49541.0813.3214-0.25273.9121-0.12860.3473-0.1995-0.21240.05250.03160.26530.4391-0.02230.40430.01040.02250.51020.00040.4731-14.5074-35.366621.9789
193.5313-0.4580.83751.1293-0.533.0685-0.2209-0.10850.17580.20320.20290.0607-0.145-0.1717-0.01560.35650.00710.02260.45660.02540.3613-27.0695-31.412919.933
202.56420.25170.66551.392-0.01693.22360.0211-0.52430.47530.8720.31120.0184-0.54130.0578-0.06510.4147-0.01640.10090.70810.05160.496-38.8873-30.523722.8309
213.2287-0.16892.30881.1672-0.54324.0425-0.1171-0.6688-0.2887-0.04940.05120.34680.2713-0.743-0.02490.4520.04830.03880.70180.07060.4342-27.5997-36.682732.3826
222.53750.19290.6821.3154-0.86451.374-0.2744-0.5525-0.3330.25420.38430.36840.2195-0.537-0.08840.3862-0.03890.07580.68470.10570.4624-40.2479-38.698924.1604
231.9321-0.0078-0.77021.3095-0.51622.9608-0.1260.2096-0.0969-0.17270.1780.29170.0528-0.1532-0.09810.4053-0.12850.03890.61650.07090.5067-44.8-36.377211.1124
243.5855-0.14080.13914.2753-0.78072.9734-0.1494-0.16620.32140.18180.0559-0.3960.05720.21610.12230.3724-0.0562-0.02970.59970.00720.5416-5.6813-26.254920.7138
254.4404-0.7582-3.84830.54971.61955.5467-0.1806-0.40220.40920.059-0.2529-0.6963-0.59420.85680.19270.8738-0.2751-0.28750.8421-0.25581.39070.9101-15.206926.2901
260.3093-0.61150.63871.6358-0.20163.7991-0.26360.28820.722-0.55710.2925-0.48340.22110.78410.2560.3734-0.19260.06030.81910.21911.00483.6208-22.84914.6385
271.614-0.51760.74215.7275-1.75476.9077-0.20530.32590.6550.06080.13740.07360.1256-0.48880.14620.6223-0.1439-0.18880.76620.29661.3096-9.7-13.61612.6852
283.1655-0.3242-0.42833.30320.46530.44450.34370.55741.2917-0.40440.0366-1.2211-1.24640.99370.24720.6137-0.2813-0.05940.5820.12041.3857-1.2559-10.486218.2644
292.94761.24291.22122.7064-1.67055.3499-0.4273-1.25782.06680.83290.0357-0.1234-1.1184-0.47910.14360.48760.0092-0.13240.57880.0271.1289-9.9969-16.062424.2498
304.88460.8824-0.39325.1244-1.33865.8101-0.14410.69351.1583-0.9734-0.4543-0.328-0.24690.45490.09040.5423-0.0655-0.05220.63890.28340.7648-3.6721-22.24528.9324
311.7418-1.2979-0.12642.94830.80463.8197-0.4486-0.79160.47570.4960.6481-0.139-0.1982-0.0041-0.03020.68780.247-0.05740.6967-0.10030.4454-23.5058-28.978950.3391
321.15360.59110.34513.13810.49292.8924-0.4257-0.39090.50120.83880.4927-0.2101-0.1878-0.252-0.24930.63770.3878-0.06390.6876-0.09440.3023-17.1698-37.887450.98
337.2014-0.1831-1.1541.75221.88942.402-0.9752-0.3229-1.30421.44921.06240.52440.78020.13940.08580.72540.35330.00280.70530.07980.3923-17.3121-46.762848.6951
343.1953-1.9282-0.50423.26530.45235.0586-0.2438-1.1553-1.15160.94920.53780.04790.6026-0.2161-0.0480.82580.2869-0.02450.86630.050.4835-14.1171-48.915252.827
350.17820.16760.18770.99240.14210.3363-0.3707-0.8750.2131.04850.2174-0.23140.0564-0.0323-1.24981.19550.622-0.35291.1562-0.39280.5647-13.0482-35.343261.459
362.5164-0.6121-0.52840.4254-0.67082.256-1.0245-1.3780.48571.40411.0489-1.16740.2460.37140.31780.83850.3156-0.28010.9752-0.19260.6294-8.4211-40.544753.0795
374.5443-0.653-0.77733.37551.80550.9970.1027-0.7158-0.80681.3410.4719-0.6320.88080.26370.16690.85250.477-0.25150.967-0.08880.7157-2.1123-55.492352.2696
383.7529-2.01121.72272.712-1.08313.41450.12261.0514-0.316-0.8474-0.04510.03750.2810.5362-0.03160.71050.2433-0.05850.6797-0.18040.5723-7.841-52.017840.3818
390.98940.7756-0.13581.35540.69451.3943-1.0702-1.04250.81380.87771.11460.4805-0.8466-0.9537-0.46560.82220.67360.08551.1097-0.04360.64-39.7029-19.225250.6575
401.09531.36130.18832.733-0.66921.9539-0.2656-0.4275-0.8419-0.11250.20720.5679-0.0182-0.6955-0.15750.66220.1950.0541.01990.23691.0134-44.2762-29.142144.0561
411.72080.0326-0.62040.96040.87181.5985-0.5736-0.9503-0.60670.10890.54940.88570.0893-0.3307-0.1850.70570.26710.16350.95650.19030.8465-44.5688-26.688448.8785
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid -3 through 24 )
2X-RAY DIFFRACTION2chain 'A' and (resid 25 through 74 )
3X-RAY DIFFRACTION3chain 'A' and (resid 75 through 147 )
4X-RAY DIFFRACTION4chain 'B' and (resid -1 through 45 )
5X-RAY DIFFRACTION5chain 'B' and (resid 46 through 56 )
6X-RAY DIFFRACTION6chain 'B' and (resid 57 through 72 )
7X-RAY DIFFRACTION7chain 'C' and (resid -3 through 15 )
8X-RAY DIFFRACTION8chain 'C' and (resid 16 through 74 )
9X-RAY DIFFRACTION9chain 'C' and (resid 75 through 120 )
10X-RAY DIFFRACTION10chain 'C' and (resid 121 through 130 )
11X-RAY DIFFRACTION11chain 'C' and (resid 131 through 147 )
12X-RAY DIFFRACTION12chain 'D' and (resid -3 through 12 )
13X-RAY DIFFRACTION13chain 'D' and (resid 13 through 34 )
14X-RAY DIFFRACTION14chain 'D' and (resid 35 through 44 )
15X-RAY DIFFRACTION15chain 'D' and (resid 45 through 56 )
16X-RAY DIFFRACTION16chain 'D' and (resid 57 through 65 )
17X-RAY DIFFRACTION17chain 'D' and (resid 66 through 72 )
18X-RAY DIFFRACTION18chain 'E' and (resid -2 through 24 )
19X-RAY DIFFRACTION19chain 'E' and (resid 25 through 74 )
20X-RAY DIFFRACTION20chain 'E' and (resid 75 through 84 )
21X-RAY DIFFRACTION21chain 'E' and (resid 85 through 98 )
22X-RAY DIFFRACTION22chain 'E' and (resid 99 through 130 )
23X-RAY DIFFRACTION23chain 'E' and (resid 131 through 147 )
24X-RAY DIFFRACTION24chain 'F' and (resid -1 through 17 )
25X-RAY DIFFRACTION25chain 'F' and (resid 18 through 22 )
26X-RAY DIFFRACTION26chain 'F' and (resid 23 through 44 )
27X-RAY DIFFRACTION27chain 'F' and (resid 45 through 49 )
28X-RAY DIFFRACTION28chain 'F' and (resid 50 through 59 )
29X-RAY DIFFRACTION29chain 'F' and (resid 60 through 65 )
30X-RAY DIFFRACTION30chain 'F' and (resid 66 through 73 )
31X-RAY DIFFRACTION31chain 'G' and (resid -1 through 38 )
32X-RAY DIFFRACTION32chain 'G' and (resid 39 through 65 )
33X-RAY DIFFRACTION33chain 'G' and (resid 66 through 74 )
34X-RAY DIFFRACTION34chain 'G' and (resid 75 through 84 )
35X-RAY DIFFRACTION35chain 'G' and (resid 85 through 98 )
36X-RAY DIFFRACTION36chain 'G' and (resid 99 through 120 )
37X-RAY DIFFRACTION37chain 'G' and (resid 121 through 130 )
38X-RAY DIFFRACTION38chain 'G' and (resid 131 through 147 )
39X-RAY DIFFRACTION39chain 'H' and (resid -2 through 40 )
40X-RAY DIFFRACTION40chain 'H' and (resid 41 through 49 )
41X-RAY DIFFRACTION41chain 'H' and (resid 50 through 72 )

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