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- PDB-4v3l: RNF38-UB-UbcH5B-Ub complex -

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Basic information

Entry
Database: PDB / ID: 4v3l
TitleRNF38-UB-UbcH5B-Ub complex
Components
  • E3 UBIQUITIN-PROTEIN LIGASE RNF38
  • POLYUBIQUITIN-C
  • UBIQUITIN-CONJUGATING ENZYME E2 D2
KeywordsLIGASE / UBIQUITIN / RING E3 / E2
Function / homology
Function and homology information


(E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / sperm flagellum / protein autoubiquitination / ubiquitin ligase complex / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) ...(E3-independent) E2 ubiquitin-conjugating enzyme / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / protein K48-linked ubiquitination / sperm flagellum / protein autoubiquitination / ubiquitin ligase complex / 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of FZD by ubiquitination / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / Translesion synthesis by REV1 / NF-kB is activated and signals survival / Regulation of PTEN localization / Translesion synthesis by POLK / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / Regulation of NF-kappa B signaling / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Recognition of DNA damage by PCNA-containing replication complex / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Peroxisomal protein import / Termination of translesion DNA synthesis / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Stabilization of p53 / EGFR downregulation
Similarity search - Function
Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like ...Ring finger domain / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Ring finger / Ubiquitin conserved site / Ubiquitin domain / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin domain signature. / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin-conjugating enzyme E2 D2 / E3 ubiquitin-protein ligase RNF38
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.53 Å
AuthorsBuetow, L. / Gabrielsen, M. / Anthony, N.G. / Dou, H. / Patel, A. / Aitkenhead, H. / Sibbet, G.J. / Smith, B.O. / Huang, D.T.
CitationJournal: Mol.Cell / Year: 2015
Title: Activation of a Primed Ring E3-E2-Ubiquitin Complex by Non-Covalent Ubiquitin.
Authors: Buetow, L. / Gabrielsen, M. / Anthony, N.G. / Dou, H. / Patel, A. / Aitkenhead, H. / Sibbet, G.J. / Smith, B.O. / Huang, D.T.
History
DepositionOct 20, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 8, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2015Group: Database references
Revision 1.2Jul 31, 2019Group: Advisory / Data collection / Derived calculations
Category: pdbx_struct_conn_angle / pdbx_validate_close_contact ...pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id ..._pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value

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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: POLYUBIQUITIN-C
C: E3 UBIQUITIN-PROTEIN LIGASE RNF38
D: POLYUBIQUITIN-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)43,8858
Polymers43,6304
Non-polymers2554
Water6,972387
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5080 Å2
ΔGint-15.7 kcal/mol
Surface area17220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)62.840, 62.840, 191.060
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221
Components on special symmetry positions
IDModelComponents
11A-2151-

HOH

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Components

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Protein , 3 types, 4 molecules ABDC

#1: Protein UBIQUITIN-CONJUGATING ENZYME E2 D2 / UBIQUITIN CARRIER PROTEIN D2 / UBIQUITIN-CONJUGATING ENZYME E2(17)KB 2 / UBIQUITIN-CONJUGATING ...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 / UBCH5B


Mass: 16650.068 Da / Num. of mol.: 1 / Fragment: RESIDUES 2-147 / Mutation: YES
Source method: isolated from a genetically manipulated source
Details: K85 SIDE CHAIN IS COVALENTLY LINKED TO G76 IN CHAIN B.
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62837, ubiquitin-protein ligase
#2: Protein POLYUBIQUITIN-C / UBIQUITIN


Mass: 8922.141 Da / Num. of mol.: 2 / Fragment: RESIDUES 77-152
Source method: isolated from a genetically manipulated source
Details: G76 IN CHAIN B IS COVALENTLY LINKED TO K85 SIDE CHAIN IN CHAIN A.
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0CG48
#3: Protein E3 UBIQUITIN-PROTEIN LIGASE RNF38 / RING FINGER PROTEIN 38 / RNF38


Mass: 9135.328 Da / Num. of mol.: 1 / Fragment: RESIDUES 439-515
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: Q9H0F5, ubiquitin-protein ligase

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Non-polymers , 3 types, 391 molecules

#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 387 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsN-TERMINAL METHIONINE IS CLEAVED DURING PURIFICATION. CYS85 IS MUTATED TO LYSINE. CONTAINS N- ...N-TERMINAL METHIONINE IS CLEAVED DURING PURIFICATION. CYS85 IS MUTATED TO LYSINE. CONTAINS N-TERMINAL GSGGS DUE TO CLONING CONTAIN N-TERMINAL GS DUE TO CLONING

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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: 2.5 Å3/Da / Density % sol: 50.72 % / Description: NONE
Crystal growDetails: 50 MM HEPES, PH 7.5, 0.2 M MAGNESIUM ACETATE AND 13% (W/V) PEG 8K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.97949
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 7, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97949 Å / Relative weight: 1
ReflectionResolution: 1.53→63.7 Å / Num. obs: 66991 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 9.5 % / Biso Wilson estimate: 20.99 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 30.1
Reflection shellResolution: 1.53→1.57 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 3.6 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.53→63.687 Å / SU ML: 0.43 / σ(F): 1.34 / Phase error: 18.26 / Stereochemistry target values: ML
Details: IN CHAIN C, RESIDUES 389-393 AND 463-C ARE DISORDERED. IN CHAIN D, RESIDUES 72-76 ARE DISORDERED. RESIDUES WITH POOR SIDE CHAIN ELECTRON DENSITY WERE BUILT AS ALANINE.
RfactorNum. reflection% reflection
Rfree0.1926 3391 5.1 %
Rwork0.1828 --
obs0.1833 66991 99.78 %
Solvent computationShrinkage radii: 1.06 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 35.894 Å2 / ksol: 0.328 e/Å3
Displacement parametersBiso mean: 31.1 Å2
Baniso -1Baniso -2Baniso -3
1-4.0557 Å20 Å20 Å2
2--4.0557 Å20 Å2
3----8.1114 Å2
Refinement stepCycle: LAST / Resolution: 1.53→63.687 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2856 0 10 387 3253
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072991
X-RAY DIFFRACTIONf_angle_d1.2334077
X-RAY DIFFRACTIONf_dihedral_angle_d13.1411142
X-RAY DIFFRACTIONf_chiral_restr0.095464
X-RAY DIFFRACTIONf_plane_restr0.009532
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.5301-1.55190.30661350.31042598X-RAY DIFFRACTION99
1.5519-1.57510.35091340.30312613X-RAY DIFFRACTION99
1.5751-1.59970.3151420.28532592X-RAY DIFFRACTION100
1.5997-1.62590.27011600.26252556X-RAY DIFFRACTION99
1.6259-1.6540.2641590.25722654X-RAY DIFFRACTION100
1.654-1.6840.28631350.22882563X-RAY DIFFRACTION100
1.684-1.71640.24951360.24322610X-RAY DIFFRACTION99
1.7164-1.75150.26111190.22182647X-RAY DIFFRACTION100
1.7515-1.78960.26741330.22082640X-RAY DIFFRACTION100
1.7896-1.83120.25581430.19662590X-RAY DIFFRACTION100
1.8312-1.8770.20481530.1812632X-RAY DIFFRACTION100
1.877-1.92770.18651440.17392598X-RAY DIFFRACTION100
1.9277-1.98450.18411530.16662632X-RAY DIFFRACTION100
1.9845-2.04850.19141450.1722628X-RAY DIFFRACTION100
2.0485-2.12170.19381480.16712620X-RAY DIFFRACTION100
2.1217-2.20670.18481190.1632664X-RAY DIFFRACTION100
2.2067-2.30710.19331420.16672666X-RAY DIFFRACTION100
2.3071-2.42880.19631370.18212673X-RAY DIFFRACTION100
2.4288-2.58090.18931260.17232686X-RAY DIFFRACTION100
2.5809-2.78020.19411370.1812671X-RAY DIFFRACTION100
2.7802-3.060.19771440.18742692X-RAY DIFFRACTION100
3.06-3.50280.20271430.17512725X-RAY DIFFRACTION100
3.5028-4.4130.14691550.15332739X-RAY DIFFRACTION100
4.413-63.74190.16271490.18782911X-RAY DIFFRACTION100
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)
14.8859-1.73120.00357.50663.35197.4060.6936-0.4881-1.09070.4903-0.16150.11991.3273-0.2302-0.47330.2568-0.0049-0.14140.27420.03740.3299-26.967418.667324.5908
25.6025.6094.58139.19695.85526.04490.2963-0.1593-0.29710.3817-0.2309-0.01530.47210.0306-0.08410.15420.0847-0.0110.215-0.00370.1724-23.525117.136214.1599
32.6738-0.85280.39481.43931.52015.20460.18480.2327-0.36040.0025-0.0424-0.12240.64540.3319-0.17250.20570.0822-0.02960.1587-0.00120.1761-28.765715.30442.4941
41.2448-0.2738-0.52831.56041.91365.07290.14360.09760.0232-0.1393-0.0418-0.0673-0.23360.2957-0.13050.10090.0287-0.00630.13460.00260.1573-27.699726.895111.0374
53.205-0.6328-2.95280.33180.82112.97290.14290.10810.1304-0.0499-0.0441-0.0538-0.16260.0641-0.09540.11740.0226-0.00940.16020.00530.1699-33.754128.037.2843
60.937-0.12250.3540.3494-0.67584.62010.04280.0988-0.0437-0.097-0.0494-0.00870.25360.01550.02490.13760.0535-0.00370.1574-0.01690.1714-37.24923.7422-1.5326
77.4929-3.18191.93912.9635-0.9882.95120.31910.5479-0.4351-0.3148-0.1875-0.18970.72670.532-0.14770.29750.12120.01930.2396-0.04460.1883-30.140415.7747-10.4486
85.32811.64640.17627.17630.86110.14710.218-0.4532-1.11940.5071-0.2252-0.28881.0349-0.329-0.07840.7378-0.16020.0110.25430.04730.3725-45.51197.958520.1962
93.0770.82070.35973.58521.53121.71760.05820.0369-0.41180.3011-0.17050.4230.947-1.03220.10510.3246-0.16370.00760.329-0.01140.2839-51.687514.115914.786
103.69413.1368-3.00015.5346-2.13412.4887-0.18211.2336-0.1894-0.5878-0.13860.88490.9778-1.30790.25630.4285-0.1156-0.06790.3976-0.14170.335-46.831211.33445.0964
113.09181.0033-0.18592.5990.89540.4564-0.10220.3105-0.5497-0.17650.1386-0.06861.0421-0.5794-0.01670.5478-0.117-0.02420.1883-0.07010.2457-44.058911.94869.6986
127.0343-5.0482.78735.6428-0.41015.6124-0.0251-0.5761-0.23780.83610.12360.5815-0.1852-0.083-0.08180.2254-0.05740.07070.32050.00610.2166-46.444325.598539.7988
135.7443-0.8884-2.64875.8164-0.46395.98820.1828-0.3475-0.51410.0645-0.1040.66810.7171-0.32440.06720.1621-0.0774-0.02150.17580.03330.1832-41.850620.112132.061
144.7692-1.03972.52115.09540.18125.5514-0.0816-0.2504-0.06490.365-0.03910.129-0.0689-0.27290.08980.1157-0.00870.06350.26550.00280.1368-45.026326.563834.779
155.75450.1696-1.10315.1264-4.47348.04690.2179-0.38080.32740.2368-0.0842-0.066-0.46990.1458-0.14450.145-0.01190.01610.1612-0.04530.1737-39.597231.671529.2735
164.06421.16680.33273.30491.73357.71970.217-0.06930.2495-0.0309-0.27340.2776-0.8156-0.47170.03910.16210.04950.01180.1661-0.00590.1525-45.779931.24620.7248
178.35630.29844.90532.09280.64312.9634-0.4051-0.29270.44280.9962-0.10611.3774-0.0558-2.1670.49030.46280.1210.15630.84870.02590.5232-56.129333.78423.1738
189.0594-1.50914.89139.2884-2.59793.0458-0.0793-0.3979-0.32241.3750.28190.3065-0.2332-0.4097-0.18430.48020.04440.04180.3578-0.02560.2655-22.07490.380218.7785
192.9834-1.2999-3.58382.2117-0.1416.2912-0.43260.72210.0699-0.07920.2550.97920.6125-0.8790.04030.439-0.108-0.13480.32590.04380.535-25.1616-1.661914.188
204.67592.2541-0.12741.9291.33722.31850.312-1.1345-0.49720.6319-0.512-0.37540.11150.0631-0.16010.33880.0885-0.60840.5211-0.23220.7535-9.54880.800619.9924
213.73241.5188-0.1587.59081.63742.1294-0.03850.2412-0.09350.12970.286-0.73650.02930.0687-0.20480.17130.0834-0.03040.1922-0.02920.2253-16.6461-2.44727.7961
224.8139-4.75410.64555.03660.84776.72780.31350.81760.3938-0.3820.0925-1.3033-0.63580.686-0.31710.22730.1242-0.06310.2757-0.09570.5049-13.23338.841411.9648
236.3020.7931-2.69315.9302-0.36877.080.3222-0.63370.14750.7867-0.2055-0.0711-0.3115-0.3085-0.08250.36830.0943-0.05430.1573-0.03720.2575-18.91046.512116.3841
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESSEQ 2:15)
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESSEQ 16:38)
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESSEQ 39:55)
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESSEQ 56:74)
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESSEQ 75:98)
6X-RAY DIFFRACTION6CHAIN 'A' AND (RESSEQ 99:130)
7X-RAY DIFFRACTION7CHAIN 'A' AND (RESSEQ 131:147)
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESSEQ 0:17)
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESSEQ 18:44)
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESSEQ 45:56)
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESSEQ 57:76)
12X-RAY DIFFRACTION12CHAIN 'C' AND (RESSEQ 394:405)
13X-RAY DIFFRACTION13CHAIN 'C' AND (RESSEQ 406:420)
14X-RAY DIFFRACTION14CHAIN 'C' AND (RESSEQ 421:433)
15X-RAY DIFFRACTION15CHAIN 'C' AND (RESSEQ 434:446)
16X-RAY DIFFRACTION16CHAIN 'C' AND (RESSEQ 447:456)
17X-RAY DIFFRACTION17CHAIN 'C' AND (RESSEQ 457:462)
18X-RAY DIFFRACTION18CHAIN 'D' AND (RESSEQ 0:7)
19X-RAY DIFFRACTION19CHAIN 'D' AND (RESSEQ 8:17)
20X-RAY DIFFRACTION20CHAIN 'D' AND (RESSEQ 18:22)
21X-RAY DIFFRACTION21CHAIN 'D' AND (RESSEQ 23:44)
22X-RAY DIFFRACTION22CHAIN 'D' AND (RESSEQ 45:56)
23X-RAY DIFFRACTION23CHAIN 'D' AND (RESSEQ 57:71)

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