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- PDB-9d1y: Structure of G75R Ubiquitin bound to KLHDC3-EloB/C -

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Basic information

Entry
Database: PDB / ID: 9d1y
TitleStructure of G75R Ubiquitin bound to KLHDC3-EloB/C
Components
  • Elongin-B
  • Elongin-C
  • Kelch domain-containing protein 3
  • Ubiquitin
KeywordsLIGASE / KLHDC3 / Ubiquitin / C-degron / Cullin-RING / E3
Function / homology
Function and homology information


XBP1(S) activates chaperone genes / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / target-directed miRNA degradation / VCB complex / elongin complex / reciprocal meiotic recombination / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery ...XBP1(S) activates chaperone genes / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / target-directed miRNA degradation / VCB complex / elongin complex / reciprocal meiotic recombination / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / Maturation of protein E / Maturation of protein E / RNA Polymerase II Pre-transcription Events / 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 / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / 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 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLK / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Regulation of activated PAK-2p34 by proteasome mediated degradation / Translesion synthesis by POLI / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / transcription corepressor binding / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Negative regulation of FGFR3 signaling
Similarity search - Function
: / Kelch motif / KLHDC2/KLHL20/DRC7 Kelch-repeats domain / Elongin-C / Elongin B / Kelch-type beta propeller / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family ...: / Kelch motif / KLHDC2/KLHL20/DRC7 Kelch-repeats domain / Elongin-C / Elongin B / Kelch-type beta propeller / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily
Similarity search - Domain/homology
Polyubiquitin-C / Elongin-C / Elongin-B / Kelch domain-containing protein 3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.6 Å
AuthorsSchulman, B.A. / Scott, D.C.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute on Aging (NIH/NIA)AG011085 United States
CitationJournal: Nat Commun / Year: 2024
Title: Structural basis for C-degron selectivity across KLHDCX family E3 ubiquitin ligases.
Authors: Daniel C Scott / Sagar Chittori / Nicholas Purser / Moeko T King / Samuel A Maiwald / Kelly Churion / Amanda Nourse / Chan Lee / Joao A Paulo / Darcie J Miller / Stephen J Elledge / J Wade ...Authors: Daniel C Scott / Sagar Chittori / Nicholas Purser / Moeko T King / Samuel A Maiwald / Kelly Churion / Amanda Nourse / Chan Lee / Joao A Paulo / Darcie J Miller / Stephen J Elledge / J Wade Harper / Gary Kleiger / Brenda A Schulman /
Abstract: Specificity of the ubiquitin-proteasome system depends on E3 ligase-substrate interactions. Many such pairings depend on E3 ligases binding to peptide-like sequences - termed N- or C-degrons - at the ...Specificity of the ubiquitin-proteasome system depends on E3 ligase-substrate interactions. Many such pairings depend on E3 ligases binding to peptide-like sequences - termed N- or C-degrons - at the termini of substrates. However, our knowledge of structural features distinguishing closely related C-degron substrate-E3 pairings is limited. Here, by systematically comparing ubiquitylation activities towards a suite of common model substrates, and defining interactions by biochemistry, crystallography, and cryo-EM, we reveal principles of C-degron recognition across the KLHDCX family of Cullin-RING ligases (CRLs). First, a motif common across these E3 ligases anchors a substrate's C-terminus. However, distinct locations of this C-terminus anchor motif in different blades of the KLHDC2, KLHDC3, and KLHDC10 β-propellers establishes distinct relative positioning and molecular environments for substrate C-termini. Second, our structural data show KLHDC3 has a pre-formed pocket establishing preference for an Arg or Gln preceding a C-terminal Gly, whereas conformational malleability contributes to KLHDC10's recognition of varying features adjacent to substrate C-termini. Finally, additional non-consensus interactions, mediated by C-degron binding grooves and/or by distal propeller surfaces and substrate globular domains, can substantially impact substrate binding and ubiquitylatability. Overall, the data reveal combinatorial mechanisms determining specificity and plasticity of substrate recognition by KLDCX-family C-degron E3 ligases.
History
DepositionAug 8, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 20, 2024Provider: repository / Type: Initial release
Revision 1.1Feb 5, 2025Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _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: Kelch domain-containing protein 3
B: Elongin-B
C: Elongin-C
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,7106
Polymers77,5264
Non-polymers1842
Water6,521362
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)114.560, 121.543, 152.949
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11A-637-

HOH

21A-721-

HOH

31A-747-

HOH

41A-765-

HOH

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Components

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Protein , 4 types, 4 molecules ABCD

#1: Protein Kelch domain-containing protein 3 / Testis intracellular mediator protein


Mass: 43245.082 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KLHDC3, PEAS / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q9BQ90
#2: Protein Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 11748.406 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15370
#3: Protein Elongin-C / EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / ...EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / Transcription elongation factor B polypeptide 1


Mass: 13855.611 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q15369
#4: Protein Ubiquitin


Mass: 8676.973 Da / Num. of mol.: 1 / Mutation: G75R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48

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Non-polymers , 2 types, 364 molecules

#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3 / Feature type: SUBJECT OF INVESTIGATION
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 362 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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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: 3.45 Å3/Da / Density % sol: 64.31 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop
Details: 10%PEG5KMME, 5% Tacsimate pH=7.0, 0.1M HEPES pH=7.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.1 / Wavelength: 0.97741 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 19, 2023
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97741 Å / Relative weight: 1
ReflectionResolution: 2.6→50 Å / Num. obs: 33218 / % possible obs: 100 % / Redundancy: 8.4 % / CC1/2: 1 / CC star: 1 / Rmerge(I) obs: 0.146 / Rpim(I) all: 0.053 / Rrim(I) all: 0.156 / Χ2: 0.485 / Net I/σ(I): 3.4
Reflection shell

Diffraction-ID: 1 / % possible all: 100

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2CC starRpim(I) allRrim(I) allΧ2
2.6-2.698.70.78232750.8490.9580.2760.830.433
2.69-2.88.70.58732570.9040.9740.2080.6240.432
2.8-2.938.60.44932760.9390.9840.160.4770.442
2.93-3.088.50.33433100.9590.990.1210.3560.46
3.08-3.2880.24832730.9710.9930.0930.2650.484
3.28-3.537.90.1733110.9870.9970.0640.1820.501
3.53-3.888.40.1233230.9930.9980.0440.1270.503
3.88-4.458.70.07833420.9970.9990.0280.0830.509
4.45-5.68.30.06533530.9980.9990.0240.0690.49
5.6-5080.06234980.9970.9990.0230.0660.603

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Processing

Software
NameVersionClassification
PHENIX1.21_5207refinement
HKL-2000data scaling
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.6→45.85 Å / SU ML: 0.28 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 20.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2162 1589 4.83 %
Rwork0.1677 --
obs0.1701 32925 99.14 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.6→45.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4962 0 12 362 5336
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0085102
X-RAY DIFFRACTIONf_angle_d0.9216925
X-RAY DIFFRACTIONf_dihedral_angle_d15.7491849
X-RAY DIFFRACTIONf_chiral_restr0.053762
X-RAY DIFFRACTIONf_plane_restr0.008894
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.6-2.680.23821310.19962757X-RAY DIFFRACTION97
2.68-2.780.31681210.19942811X-RAY DIFFRACTION98
2.78-2.890.24331490.21662791X-RAY DIFFRACTION98
2.89-3.020.25491430.19832820X-RAY DIFFRACTION99
3.02-3.180.26451300.19442840X-RAY DIFFRACTION99
3.18-3.380.25571330.18182862X-RAY DIFFRACTION100
3.38-3.640.24981360.18662874X-RAY DIFFRACTION100
3.64-4.010.20871370.15052860X-RAY DIFFRACTION100
4.01-4.590.14211470.12462880X-RAY DIFFRACTION100
4.59-5.770.18812050.13472833X-RAY DIFFRACTION100
5.78-45.850.21591570.17183008X-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)
12.8756-0.9279-0.53921.93620.01912.39730.10520.0895-0.0821-0.17670.01490.2913-0.1235-0.4861-0.09060.2248-0.0306-0.03180.30250.02530.281-27.1684-7.1999-13.9286
21.75430.2279-0.95862.5084-0.23192.1371-0.0460.19490.0872-0.17970.0650.4236-0.286-0.56910.00820.28440.0676-0.02930.36620.02740.3423-28.90937.2614-16.89
31.1970.1213-0.66022.50650.39952.44310.04460.19070.0568-0.41610.03930.0187-0.3968-0.3486-0.00380.35850.0637-0.01360.33390.05050.3-19.439812.568-24.8479
41.1329-0.56470.16581.899-0.96071.55260.0640.16460.0768-0.3031-0.0955-0.13420.03240.02240.01990.3103-0.01460.04860.2818-0.01030.2262-7.9447-0.3503-28.7548
53.3222-0.70880.60922.6947-2.33662.75140.15390.1357-0.3276-0.34240.02070.08590.2574-0.251-0.03090.28980.02220.02880.2526-0.01340.2711-17.1168-11.6331-20.22
61.3559-0.54920.67032.5194-1.85552.9679-0.002-0.0887-0.3822-0.11010.03680.07790.3982-0.1665-0.09340.2932-0.02390.03130.2283-0.01080.3784-15.6104-22.0085-7.2381
78.6696-0.18231.60023.92173.35393.416-0.20130.84250.8493-0.18510.2734-0.5651-0.16940.11240.09310.20180.02060.01660.2741-0.01730.482818.8694-23.3827-2.5318
86.0394-2.30540.69272.0023-0.16493.906-0.12990.41210.9595-0.23680.0973-0.5522-0.67750.08650.08220.3328-0.0107-0.03280.23310.06790.561724.0764-20.71351.5243
95.7131-2.49360.8413.37680.40885.1324-0.308-0.22250.7162-0.0052-0.0623-0.6205-0.06850.46670.06120.30560.0467-0.03580.3255-0.00870.451531.0367-25.50696.7946
103.909-1.65745.38394.79380.28569.0070.6470.1742-0.2314-0.6554-0.0494-0.21720.3714-0.0719-0.5440.2670.01680.07610.51540.01210.476927.3691-34.1077-4.6864
114.7244-2.10132.58944.5449-0.37662.20450.23241.34560.6323-0.5534-0.3701-0.39020.41220.65650.19840.3990.0740.04420.53690.09570.448527.3315-24.668-9.383
124.9029-1.1261.631.6039-0.124.6679-0.256-0.3323-0.53340.25560.3040.2695-0.1554-0.2457-0.03430.27870.03430.0120.19830.0250.43920.6928-31.54373.9335
134.8081-0.08450.89893.01561.37592.71-0.2782-0.56540.41040.21220.1459-0.5328-0.304-0.1090.1450.32820.096-0.00520.34260.01610.421311.3053-19.72748.1165
142.2116-2.8767-1.13684.67833.74685.0332-0.5416-0.81250.0650.45540.0770.368-0.0747-0.34720.51750.35980.13480.00120.50320.00390.46824.2746-17.667613.7078
154.56260.12450.45153.3169-0.33874.6149-0.190.13420.07970.21980.1493-0.0897-0.20660.31880.01210.28070.04280.00490.27210.05350.37616.4067-21.4004-1.5175
162.63631.8006-2.03399.11-6.45187.8035-0.24590.57920.1513-0.0132-0.2061-0.985-0.3017-0.1310.29820.3640.11080.01250.39120.06350.56833.7286-19.1795-11.8723
174.41090.76821.43993.24571.34235.9413-0.0256-0.7221-0.5370.12320.2824-0.4466-0.0706-0.5585-0.20980.22690.01860.03720.29550.12950.3685-3.4052-25.95063.1805
187.84681.84295.21529.34741.98596.84240.79091.6176-1.6497-1.0635-0.29730.37821.0512-0.5531-0.68521.1378-0.0771-0.09891.1103-0.23440.6608-26.5442-10.6235-50.893
191.3452-0.4932-0.91517.0432.13851.09790.04351.6095-0.1128-1.4386-0.25731.46340.1088-1.77940.33721.2116-0.2883-0.53681.7504-0.01981.1682-36.1062-6.4665-55.9978
205.15970.21520.3014.00363.82778.83840.17991.0984-0.3627-0.7851-0.73632.07121.0555-1.550.55621.0012-0.2422-0.32631.1426-0.25541.0363-36.9597-6.4814-47.2389
213.42643.9559-0.43945.6146-3.36378.02070.184-0.01700.02880.26691.40020.1465-1.2225-0.15050.6917-0.04080.01180.9668-0.00240.6159-31.9662-2.6949-41.7515
229.34580.1561-0.41874.9802-3.93746.6454-0.16081.36140.756-1.1621-0.15631.2059-0.9011-1.24180.29261.0340.1673-0.3961.1074-0.11440.7385-29.39563.9054-52.065
231.576-0.16630.17970.2948-1.03194.21860.01091.0552-0.1774-1.20130.22530.4758-0.6773-0.4693-0.13421.1784-0.1086-0.14280.832-0.0140.341-27.4213-3.2821-48.135
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 68 )
2X-RAY DIFFRACTION2chain 'A' and (resid 69 through 124 )
3X-RAY DIFFRACTION3chain 'A' and (resid 125 through 169 )
4X-RAY DIFFRACTION4chain 'A' and (resid 170 through 294 )
5X-RAY DIFFRACTION5chain 'A' and (resid 295 through 322 )
6X-RAY DIFFRACTION6chain 'A' and (resid 323 through 377 )
7X-RAY DIFFRACTION7chain 'B' and (resid 1 through 9 )
8X-RAY DIFFRACTION8chain 'B' and (resid 10 through 35 )
9X-RAY DIFFRACTION9chain 'B' and (resid 36 through 45 )
10X-RAY DIFFRACTION10chain 'B' and (resid 46 through 50 )
11X-RAY DIFFRACTION11chain 'B' and (resid 51 through 66 )
12X-RAY DIFFRACTION12chain 'B' and (resid 67 through 97 )
13X-RAY DIFFRACTION13chain 'C' and (resid 17 through 38 )
14X-RAY DIFFRACTION14chain 'C' and (resid 39 through 66 )
15X-RAY DIFFRACTION15chain 'C' and (resid 67 through 83 )
16X-RAY DIFFRACTION16chain 'C' and (resid 84 through 96 )
17X-RAY DIFFRACTION17chain 'C' and (resid 97 through 112 )
18X-RAY DIFFRACTION18chain 'D' and (resid 1 through 12 )
19X-RAY DIFFRACTION19chain 'D' and (resid 13 through 22 )
20X-RAY DIFFRACTION20chain 'D' and (resid 23 through 34 )
21X-RAY DIFFRACTION21chain 'D' and (resid 35 through 44 )
22X-RAY DIFFRACTION22chain 'D' and (resid 45 through 56 )
23X-RAY DIFFRACTION23chain 'D' and (resid 57 through 76 )

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