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- PDB-5igq: WD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2) bound to pe... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5igq
TitleWD40 domain of Human E3 Ubiquitin Ligase COP1 (RFWD2) bound to peptide from Trib1
Components
  • (Tribbles homolog 1) x 2
  • E3 ubiquitin-protein ligase RFWD2
KeywordsHydrolase/Peptide / WD40 domain E3 ligase / Tribbles / Hydrolase-Peptide Complex
Function / homology
Function and homology information


ubiquitin-protein transferase regulator activity / positive regulation of eosinophil differentiation / negative regulation of smooth muscle cell migration / regulation of MAP kinase activity / negative regulation of neutrophil differentiation / positive regulation of macrophage differentiation / negative regulation of lipopolysaccharide-mediated signaling pathway / NGF-stimulated transcription / mitogen-activated protein kinase kinase binding / Cul4A-RING E3 ubiquitin ligase complex ...ubiquitin-protein transferase regulator activity / positive regulation of eosinophil differentiation / negative regulation of smooth muscle cell migration / regulation of MAP kinase activity / negative regulation of neutrophil differentiation / positive regulation of macrophage differentiation / negative regulation of lipopolysaccharide-mediated signaling pathway / NGF-stimulated transcription / mitogen-activated protein kinase kinase binding / Cul4A-RING E3 ubiquitin ligase complex / response to ionizing radiation / protein kinase inhibitor activity / JNK cascade / negative regulation of smooth muscle cell proliferation / Autodegradation of the E3 ubiquitin ligase COP1 / negative regulation of protein kinase activity / RING-type E3 ubiquitin transferase / negative regulation of DNA-binding transcription factor activity / ubiquitin-protein transferase activity / ubiquitin protein ligase activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / proteasome-mediated ubiquitin-dependent protein catabolic process / RNA polymerase II-specific DNA-binding transcription factor binding / response to lipopolysaccharide / protein ubiquitination / nuclear speck / Golgi membrane / ubiquitin protein ligase binding / nucleoplasm / nucleus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Tribbles homologue 1 / Pseudokinase tribbles family/serine-threonine-protein kinase 40 / E3 ubiquitin-protein ligase COP1 / Zinc finger, C3HC4 type (RING finger) / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger ...Tribbles homologue 1 / Pseudokinase tribbles family/serine-threonine-protein kinase 40 / E3 ubiquitin-protein ligase COP1 / Zinc finger, C3HC4 type (RING finger) / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Ring finger / Zinc finger RING-type profile. / Zinc finger, RING-type / Zinc finger, RING/FYVE/PHD-type / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / Protein kinase domain / WD40/YVTN repeat-like-containing domain superfamily / Serine/Threonine protein kinases, catalytic domain / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Mainly Beta
Similarity search - Domain/homology
E3 ubiquitin-protein ligase COP1 / Tribbles homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.9 Å
AuthorsUljon, S. / Blacklow, S.C.
CitationJournal: Structure / Year: 2016
Title: Structural Basis for Substrate Selectivity of the E3 Ligase COP1.
Authors: Uljon, S. / Xu, X. / Durzynska, I. / Stein, S. / Adelmant, G. / Marto, J.A. / Pear, W.S. / Blacklow, S.C.
History
DepositionFeb 28, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 20, 2016Provider: repository / Type: Initial release
Revision 1.1May 11, 2016Group: Database references
Revision 1.2Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / pdbx_initial_refinement_model / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_oper_list.symmetry_operation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: E3 ubiquitin-protein ligase RFWD2
U: Tribbles homolog 1
B: E3 ubiquitin-protein ligase RFWD2
V: Tribbles homolog 1
C: E3 ubiquitin-protein ligase RFWD2
W: Tribbles homolog 1
D: E3 ubiquitin-protein ligase RFWD2
X: Tribbles homolog 1
E: E3 ubiquitin-protein ligase RFWD2
Y: Tribbles homolog 1
F: E3 ubiquitin-protein ligase RFWD2
Z: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)245,67012
Polymers245,67012
Non-polymers00
Water00
1
A: E3 ubiquitin-protein ligase RFWD2
U: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)41,2552
Polymers41,2552
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1220 Å2
ΔGint-7 kcal/mol
Surface area13840 Å2
MethodPISA
2
B: E3 ubiquitin-protein ligase RFWD2
V: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)40,8832
Polymers40,8832
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1210 Å2
ΔGint-6 kcal/mol
Surface area13440 Å2
MethodPISA
3
C: E3 ubiquitin-protein ligase RFWD2
W: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)40,8832
Polymers40,8832
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1210 Å2
ΔGint-6 kcal/mol
Surface area13510 Å2
MethodPISA
4
D: E3 ubiquitin-protein ligase RFWD2
X: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)40,8832
Polymers40,8832
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1150 Å2
ΔGint-6 kcal/mol
Surface area13460 Å2
MethodPISA
5
E: E3 ubiquitin-protein ligase RFWD2
Y: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)40,8832
Polymers40,8832
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1230 Å2
ΔGint-6 kcal/mol
Surface area13420 Å2
MethodPISA
6
F: E3 ubiquitin-protein ligase RFWD2
Z: Tribbles homolog 1


Theoretical massNumber of molelcules
Total (without water)40,8832
Polymers40,8832
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1210 Å2
ΔGint-7 kcal/mol
Surface area13460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)247.646, 249.576, 124.512
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number21
Space group name H-MC222

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Components

#1: Protein
E3 ubiquitin-protein ligase RFWD2 / Constitutive photomorphogenesis protein 1 homolog / hCOP1 / RING finger and WD repeat domain ...Constitutive photomorphogenesis protein 1 homolog / hCOP1 / RING finger and WD repeat domain protein 2 / RING finger protein 200


Mass: 39932.883 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RFWD2, COP1, RNF200 / Production host: Trichoplusia ni (cabbage looper)
References: UniProt: Q8NHY2, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#2: Protein/peptide Tribbles homolog 1 / TRB-1 / G-protein-coupled receptor-induced gene 2 protein / GIG-2 / SKIP1


Mass: 1322.331 Da / Num. of mol.: 1 / Fragment: UNP residues 188-198 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q96RU8
#3: Protein/peptide
Tribbles homolog 1 / TRB-1 / G-protein-coupled receptor-induced gene 2 protein / GIG-2 / SKIP1


Mass: 950.001 Da / Num. of mol.: 5 / Fragment: UNP residues 188-195 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q96RU8

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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: 3.92 Å3/Da / Density % sol: 68.59 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 0.1M Bis-Tris pH 5.5, 20% glycerol, 5% PEG 5000 MME

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Apr 10, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 3.9→29.766 Å / Num. obs: 35006 / % possible obs: 98 % / Redundancy: 2 % / CC1/2: 0.997 / Rmerge(I) obs: 0.06869 / Net I/σ(I): 8
Reflection shellResolution: 3.9→4.039 Å / Redundancy: 2 % / Rmerge(I) obs: 0.7334 / Mean I/σ(I) obs: 1.2 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.10_2155refinement
XDSdata reduction
Aimlessdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5HQG

5hqg


Resolution: 3.9→29.766 Å / SU ML: 0.58 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.44
RfactorNum. reflection% reflection
Rfree0.2768 1735 4.96 %
Rwork0.2283 --
obs0.2306 34980 98.64 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 3.9→29.766 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15331 0 0 0 15331
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00215697
X-RAY DIFFRACTIONf_angle_d0.65221309
X-RAY DIFFRACTIONf_dihedral_angle_d13.779214
X-RAY DIFFRACTIONf_chiral_restr0.0472385
X-RAY DIFFRACTIONf_plane_restr0.0032693
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.9-4.01450.37381510.33832750X-RAY DIFFRACTION100
4.0145-4.14380.36731490.32562756X-RAY DIFFRACTION100
4.1438-4.29140.3161430.27332785X-RAY DIFFRACTION100
4.2914-4.46270.32151450.24692739X-RAY DIFFRACTION100
4.4627-4.66510.25921360.22332789X-RAY DIFFRACTION100
4.6651-4.910.28111290.21772782X-RAY DIFFRACTION99
4.91-5.21610.25381440.20092774X-RAY DIFFRACTION99
5.2161-5.61640.2841660.23452739X-RAY DIFFRACTION99
5.6164-6.1770.25311540.22382784X-RAY DIFFRACTION99
6.177-7.06040.24861410.22282778X-RAY DIFFRACTION98
7.0604-8.85630.2831520.23152763X-RAY DIFFRACTION97
8.8563-29.7670.25191250.20122806X-RAY DIFFRACTION94
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)
12.91330.77810.21650.2081-1.29430.4332-0.1581-0.62710.4708-0.81751.22381.6919-0.7060.45550.06241.0229-0.0450.00191.8576-0.36910.9135-24.0874-57.602845.6561
2-0.18430.08710.09952.12080.62310.3764-0.7355-1.32841.1341-1.83110.7996-1.5001-0.31311.8246-0.14161.3328-1.102-0.31552.705-0.39451.0757-12.4128-55.157834.8424
34.2489-0.0073-0.71232.33850.9643-0.0062-0.47120.4678-0.5343-1.11120.1654-1.14930.2176-0.08320.00031.3338-0.1182-0.01171.7916-0.49731.5883-14.7847-74.54930.8015
40.6737-0.7108-0.77291.03210.46460.68630.97011.2167-0.2248-0.0121-0.12931.20261.68950.45070.00691.3562-0.0648-0.14142.0899-0.22691.3098-26.404-80.14738.1934
53.23261.00450.73782.40882.17351.0333-0.60070.1394-0.1626-0.4170.57971.40540.3691-0.0286-01.3169-0.1108-0.13991.5320.04921.4736-34.2334-70.12342.7677
60.2739-0.26910.57210.56920.48260.62630.2768-0.55990.64660.06950.02431.1723-0.11131.21410.00011.0775-0.2721-0.11591.9148-0.13351.5668-24.7382-55.540442.6512
75.1557-3.3212-1.0667.1156-5.49989.6066-0.9869-1.9881-1.9121-0.37271.39370.88132.4536-1.3069-2.02360.6532-0.2412-0.30521.40310.54070.6787-36.3682-70.998224.7195
80.979-1.23580.19261.5904-0.64060.41330.3014-0.94482.1946-1.4988-1.1560.99060.87970.27320.00092.06740.136-0.29741.4331-0.21511.308-51.7761-113.2484-1.4228
90.87880.7216-0.74260.89020.11961.23740.086-0.03651.9384-0.1766-0.44-1.4059-2.17130.43410.00031.6641-0.13740.09771.31860.03831.5674-34.6144-98.07759.1345
100.05560.13970.52581.7947-0.54112.26110.0362-0.48430.86581.8674-0.2805-0.0911-1.29710.34280.00021.8852-0.1308-0.09351.3758-0.12390.9548-40.4749-99.62626.8496
113.5803-0.8088-0.820.2120.2230.3615-2.0965-2.4698-2.64121.45771.17780.67741.3658-0.69530.02032.4498-0.2440.1011.0381-0.11881.3703-49.8461-111.065527.1424
12-0.18921.029-1.31533.10820.50270.4932-0.2161-0.5649-0.80040.2349-0.7143-0.57450.75410.4555-0.00081.8187-0.06040.10071.18490.05090.9516-48.6905-118.375115.8734
130.143-0.0174-0.41760.4047-0.0591.6289-0.1008-0.03880.7363-0.4224-0.6092-0.49250.23290.611-0.01421.67460.1081-0.07730.77870.08431.3452-40.7969-108.37523.9378
140.13020.10870.21140.17160.27440.5181-0.2775-1.2875-0.7640.1626-1.61910.6586-0.0689-1.0831-0.02572.3711-0.1808-0.20221.4210.07351.2568-32.8162-118.197623.1967
153.92841.07171.35892.7343-0.89430.3349-0.8643-1.4397-0.80520.1160.73091.73520.27180.5198-0.00341.02260.2297-0.00451.97690.17240.8729-17.0733-45.345465.5883
161.41120.8967-0.62640.55920.05450.1559-1.00142.78251.7013-0.26820.44423.0485-1.3349-2.2859-0.01151.65780.6176-0.38341.7719-0.30572.0128-28.3225-34.423669.2166
171.0509-1.9406-0.41176.3647-1.15994.0437-1.7078-2.6545-1.05760.63952.79914.0122-1.4453-2.09850.73231.23220.99650.46513.0707-0.52720.0328-26.5584-41.551687.6752
183.4137-2.23640.11361.2942-1.3911.0319-1.2653-1.1181-0.08670.23840.5424-0.038-0.38610.658-0.0411.26520.3676-0.13292.1846-0.23040.9434-9.1604-50.448580.3138
190.5738-0.6305-1.09010.78391.39051.7679-0.5096-0.1809-0.2484-0.2699-0.7265-0.727-0.45040.60280.00010.98530.0686-0.28661.82230.05331.4225-16.2695-41.709665.4767
202.93341.31010.3310.8361-0.3621.0968-1.2521.90710.9142.28520.74861.96612.684-0.2443-0.01441.71840.2862-0.44252.5472-0.37951.4509-7.5618-34.482385.4711
211.5278-1.95-1.29111.89870.89641.555-0.103-0.37891.9556-0.9577-0.18541.0596-0.15710.3404-0.00461.456-0.053-0.10541.19910.0221.9117-50.3012-66.0164-11.4502
221.9163-0.1569-0.50070.69610.66380.69810.6434-0.20862.5395-2.6932-0.5617-1.1682-1.47141.46060.10592.0049-0.02270.34681.52860.54251.6041-41.6848-54.7809-19.0604
231.0986-0.43311.03120.7153-0.50890.6905-0.1312-0.06410.8042-0.67580.406-3.1508-1.16321.9972-0.00011.5877-0.25030.08271.86260.16262.6183-30.7393-55.1732-7.5416
240.56140.39390.8551.6325-1.02432.1499-0.285-0.75930.97991.6888-0.0188-2.0045-0.51111.1880.00021.7689-0.2809-0.28011.42540.08332.1287-29.8357-63.06453.6939
251.3838-1.82291.64682.9005-1.66351.33310.6163-0.08680.3667-0.1051-0.6308-0.62650.66550.56620.00011.5142-0.0167-0.0041.36210.09491.1598-41.6244-75.8948-0.5985
262.31610.5231-0.65390.1416-0.1421-0.00781.0011-1.0352-0.0423-2.7086-0.4630.29090.22181.10580.06692.08140.21120.05920.7424-0.09511.446-48.7432-68.3695-13.3945
270.01030.08860.13140.21810.44411.05260.67730.3562-0.425-1.2396-0.3556-1.47381.1882-1.4223-0.01221.90010.08950.12861.13490.14642.6407-49.4865-66.4555-16.8187
280.1492-0.05030.013-0.0413-0.0308-0.00910.67-0.64882.06640.8209-0.93890.9156-0.481-0.97770.00061.8390.0858-0.16691.64820.24621.5802-27.567-75.8876-11.0594
293.01313.1570.27892.6127-0.13850.85180.75470.27071.13610.3429-0.0759-1.43080.5638-0.1837-0.0010.98240.0560.10691.272-0.2312.1407-65.7615-73.795247.8182
300.23660.04090.50920.0972-0.0810.6803-0.90651.5677-0.82160.6480.1055-0.65450.96761.1495-0.05261.6623-0.03140.73911.7744-0.19132.4887-55.3265-82.500939.2768
312.0128-0.5277-0.37760.6108-0.14670.7605-0.4341-1.2438-0.6561-0.3835-0.0626-2.01891.3360.510.00251.64730.13950.31861.42770.04612.4235-57.2818-95.746454.026
320.2885-0.41490.53730.3361-0.42150.2766-1.06851.2118-0.99250.21960.31470.08032.2806-0.4618-0.00041.57270.05820.21432.004-0.25752.3829-67.8683-91.532663.5408
331.04331.1145-0.22470.8286-0.31450.0015-0.8645-0.0391-0.47340.5715-0.6992-0.24291.1191-0.119501.3482-0.20890.44181.18860.0081.9989-72.9219-91.593163.9538
341.1084-1.0309-0.02710.75960.1195-0.2814-1.1044-0.229-1.22130.54930.6530.7381-0.1121-1.82620.00011.3639-0.04610.25421.7075-0.18741.4552-76.2342-81.436758.2943
350.2938-0.1584-0.90512.00550.07120.86320.29320.49041.2896-0.10060.7512-1.07880.407-0.46570.03971.0473-0.00710.10221.8299-0.49971.9815-70.6245-74.42346.7649
360.2588-0.433-0.21760.41990.12890.09230.346-0.13180.97890.34481.0273-1.02170.49991.60550.00261.4195-0.30360.43981.5201-0.16692.0059-76.6417-95.792147.3009
371.90441.37760.55764.6142-0.15432.85960.60260.6909-0.5126-0.6553-0.37030.09321.14340.11390.01642.35330.3658-0.94220.9844-0.36121.4939-63.7678-106.6802-26.7544
384.47580.148-1.62360.0190.09160.77370.64720.44662.76810.04280.04780.0549-0.2565-0.56070.56582.77140.2255-1.09131.1904-0.36551.5007-78.2839-97.5102-23.3959
390.7865-0.66640.0973.51011.6370.4770.87080.70071.594-0.561-0.952-0.20030.3486-0.08070.00881.68210.1999-0.48761.2868-0.14291.4768-68.5416-89.7935-18.0179
400.25270.45640.01240.54690.34690.28290.5367-0.29151.5040.4510.22710.4170.13870.35430.01922.11270.2798-0.48631.11610.01741.2748-53.6973-98.8776-18.769
410.89181.29950.46071.90110.69090.18151.2979-0.7310.58453.2496-0.4004-0.83353.06070.62640.4151.79880.8039-0.48341.4854-0.07751.9824-66.1908-89.0726-35.2384
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 391 through 434 )
2X-RAY DIFFRACTION2chain 'A' and (resid 435 through 472 )
3X-RAY DIFFRACTION3chain 'A' and (resid 473 through 557 )
4X-RAY DIFFRACTION4chain 'A' and (resid 558 through 584 )
5X-RAY DIFFRACTION5chain 'A' and (resid 585 through 679 )
6X-RAY DIFFRACTION6chain 'A' and (resid 680 through 731 )
7X-RAY DIFFRACTION7chain 'U' and (resid 354 through 364 )
8X-RAY DIFFRACTION8chain 'B' and (resid 391 through 412 )
9X-RAY DIFFRACTION9chain 'B' and (resid 413 through 472 )
10X-RAY DIFFRACTION10chain 'B' and (resid 473 through 557 )
11X-RAY DIFFRACTION11chain 'B' and (resid 558 through 584 )
12X-RAY DIFFRACTION12chain 'B' and (resid 585 through 679 )
13X-RAY DIFFRACTION13chain 'B' and (resid 680 through 731 )
14X-RAY DIFFRACTION14chain 'V' and (resid 354 through 361 )
15X-RAY DIFFRACTION15chain 'C' and (resid 391 through 434 )
16X-RAY DIFFRACTION16chain 'C' and (resid 435 through 472 )
17X-RAY DIFFRACTION17chain 'C' and (resid 473 through 557 )
18X-RAY DIFFRACTION18chain 'C' and (resid 558 through 679 )
19X-RAY DIFFRACTION19chain 'C' and (resid 680 through 731 )
20X-RAY DIFFRACTION20chain 'W' and (resid 354 through 361 )
21X-RAY DIFFRACTION21chain 'D' and (resid 391 through 434 )
22X-RAY DIFFRACTION22chain 'D' and (resid 435 through 472 )
23X-RAY DIFFRACTION23chain 'D' and (resid 473 through 521 )
24X-RAY DIFFRACTION24chain 'D' and (resid 522 through 584 )
25X-RAY DIFFRACTION25chain 'D' and (resid 585 through 675 )
26X-RAY DIFFRACTION26chain 'D' and (resid 676 through 714 )
27X-RAY DIFFRACTION27chain 'D' and (resid 715 through 731 )
28X-RAY DIFFRACTION28chain 'X' and (resid 354 through 361 )
29X-RAY DIFFRACTION29chain 'E' and (resid 391 through 434 )
30X-RAY DIFFRACTION30chain 'E' and (resid 435 through 472 )
31X-RAY DIFFRACTION31chain 'E' and (resid 473 through 557 )
32X-RAY DIFFRACTION32chain 'E' and (resid 558 through 584 )
33X-RAY DIFFRACTION33chain 'E' and (resid 585 through 607 )
34X-RAY DIFFRACTION34chain 'E' and (resid 608 through 659 )
35X-RAY DIFFRACTION35chain 'E' and (resid 660 through 731 )
36X-RAY DIFFRACTION36chain 'Y' and (resid 354 through 361 )
37X-RAY DIFFRACTION37chain 'F' and (resid 391 through 557 )
38X-RAY DIFFRACTION38chain 'F' and (resid 558 through 584 )
39X-RAY DIFFRACTION39chain 'F' and (resid 585 through 679 )
40X-RAY DIFFRACTION40chain 'F' and (resid 680 through 731 )
41X-RAY DIFFRACTION41chain 'Z' and (resid 354 through 361 )

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