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- PDB-9d1z: Structure of G75Q Ubiquitin bound to KLHDC3-EloB/C -

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Basic information

Entry
Database: PDB / ID: 9d1z
TitleStructure of G75Q 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 / 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 / Tat-mediated elongation of the HIV-1 transcript / 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) / ubiquitin-like ligase-substrate adaptor activity / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / Formation of HIV-1 elongation complex containing HIV-1 Tat / Constitutive Signaling by NOTCH1 HD Domain Mutants / 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 / Formation of HIV elongation complex in the absence of HIV Tat / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / Regulation of pyruvate metabolism / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Pexophagy / VLDLR internalisation and degradation / RNA Polymerase II Transcription Elongation / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Formation of RNA Pol II elongation complex / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / InlB-mediated entry of Listeria monocytogenes into host cell / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / TICAM1, RIP1-mediated IKK complex recruitment / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / RNA Polymerase II Pre-transcription Events / IKK complex recruitment mediated by RIP1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / Regulation of activated PAK-2p34 by proteasome mediated degradation / TNFR1-induced NF-kappa-B signaling pathway / PINK1-PRKN Mediated Mitophagy / TCF dependent signaling in response to WNT / Autodegradation of Cdh1 by Cdh1:APC/C / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / APC/C:Cdc20 mediated degradation of Securin / activated TAK1 mediates p38 MAPK activation / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / Regulation of signaling by CBL / NIK-->noncanonical NF-kB signaling / NOTCH3 Activation and Transmission of Signal to the Nucleus / SCF-beta-TrCP mediated degradation of Emi1 / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / TNFR2 non-canonical NF-kB pathway / Negative regulation of FGFR3 signaling / AUF1 (hnRNP D0) binds and destabilizes mRNA / Fanconi Anemia Pathway / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Negative regulation of FGFR2 signaling / Degradation of DVL / Peroxisomal protein import
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 / Ubiquitin domain signature. / Ubiquitin conserved site / 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: 1.88 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)77,9868
Polymers77,5134
Non-polymers4734
Water12,214678
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)114.949, 120.873, 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-544-

HOH

21A-873-

HOH

31A-941-

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: 13871.611 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 (butterflies/moths) / References: UniProt: Q15369
#4: Protein Ubiquitin


Mass: 8647.907 Da / Num. of mol.: 1 / Mutation: G75Q
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, 682 molecules

#5: Chemical
ChemComp-MPD / (4S)-2-METHYL-2,4-PENTANEDIOL


Mass: 118.174 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H14O2 / Feature type: SUBJECT OF INVESTIGATION / Comment: precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 678 / 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: 3.43 Å3/Da / Density % sol: 64.1 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / Details: 10%%KMME, 5% Tacsimate pH=7.0, 0.1M HEPES 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: 1.88→50 Å / Num. obs: 85054 / % possible obs: 100 % / Redundancy: 8.1 % / CC1/2: 0.997 / CC star: 0.999 / Rmerge(I) obs: 0.092 / Rpim(I) all: 0.035 / Rrim(I) all: 0.099 / Χ2: 0.995 / Net I/σ(I): 5.9
Reflection shell

Diffraction-ID: 1 / % possible all: 100

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2CC starRpim(I) allRrim(I) allΧ2
1.9-1.977.40.77783780.7890.9390.310.8380.524
1.97-2.058.20.54184770.8930.9710.2020.5780.513
2.05-2.148.30.484230.9380.9840.1480.4270.565
2.14-2.258.30.30884280.9610.990.1140.3290.657
2.25-2.398.30.23484750.9760.9940.0870.250.752
2.39-2.587.80.18384400.9820.9960.070.1960.856
2.58-2.847.70.13284910.990.9980.0510.1421.049
2.84-3.258.70.09685320.9950.9990.0350.1021.447
3.25-4.098.50.07185760.9970.9990.0260.0761.94
4.09-508.10.04888340.99810.0180.0511.498

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Processing

Software
NameVersionClassification
PHENIX1.21_5207refinement
HKL-2000data scaling
HKL-2000data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.88→45.95 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 18.96 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1903 4189 4.94 %
Rwork0.1686 --
obs0.1697 84718 98.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.88→45.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5028 0 32 678 5738
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0075188
X-RAY DIFFRACTIONf_angle_d0.9757049
X-RAY DIFFRACTIONf_dihedral_angle_d14.6151880
X-RAY DIFFRACTIONf_chiral_restr0.061775
X-RAY DIFFRACTIONf_plane_restr0.009909
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.88-1.90.3023820.27661686X-RAY DIFFRACTION62
1.9-1.930.2931500.23762645X-RAY DIFFRACTION99
1.93-1.950.24171320.232699X-RAY DIFFRACTION99
1.95-1.980.25811280.21112661X-RAY DIFFRACTION99
1.98-20.21851470.19922688X-RAY DIFFRACTION99
2-2.030.2091500.18582679X-RAY DIFFRACTION100
2.03-2.060.21531410.18432693X-RAY DIFFRACTION100
2.06-2.090.21411390.18212692X-RAY DIFFRACTION100
2.09-2.120.20351200.18252726X-RAY DIFFRACTION100
2.12-2.160.19551240.18172704X-RAY DIFFRACTION100
2.16-2.190.21971350.17752697X-RAY DIFFRACTION100
2.19-2.230.19641450.18162701X-RAY DIFFRACTION100
2.23-2.280.21871310.17022679X-RAY DIFFRACTION100
2.28-2.320.1981290.17272761X-RAY DIFFRACTION100
2.32-2.370.19961260.16722696X-RAY DIFFRACTION100
2.37-2.430.1971440.18362698X-RAY DIFFRACTION100
2.43-2.490.22971290.18172716X-RAY DIFFRACTION100
2.49-2.560.21081530.18082705X-RAY DIFFRACTION100
2.56-2.630.21961770.1872679X-RAY DIFFRACTION100
2.63-2.720.22061470.18572705X-RAY DIFFRACTION100
2.72-2.810.22011530.18742718X-RAY DIFFRACTION100
2.81-2.930.22421430.17972705X-RAY DIFFRACTION100
2.93-3.060.17221390.17882756X-RAY DIFFRACTION100
3.06-3.220.1841630.16632722X-RAY DIFFRACTION100
3.22-3.420.15231330.15882740X-RAY DIFFRACTION100
3.42-3.690.1751530.15442727X-RAY DIFFRACTION100
3.69-4.060.14331400.14462777X-RAY DIFFRACTION100
4.06-4.640.13841460.12662768X-RAY DIFFRACTION100
4.64-5.850.18141390.15152795X-RAY DIFFRACTION100
5.85-45.950.21971510.18272911X-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)
11.6928-0.04810.07851.4344-0.10931.7375-0.03690.084-0.0342-0.06490.04010.2598-0.0565-0.4034-0.00910.1919-0.0146-0.0250.2556-0.00480.209-26.9898-7.2676-14.016
21.45860.1704-0.60542.01540.04382.1373-0.00730.12010.1703-0.15710.04470.3139-0.3613-0.3414-0.00840.24470.0628-0.02370.28710.01190.2596-27.56925.3027-16.4485
31.5060.0671-1.0443.46510.27911.33450.05540.2050.0983-0.3671-0.00390.3562-0.4257-0.3836-0.00740.26070.0908-0.04340.33670.00990.2702-29.90268.8328-17.3748
40.9849-0.3458-0.02171.49440.02590.93490.0580.18170.0835-0.3301-0.0403-0.1267-0.1124-0.0434-0.01540.2932-0.00350.03190.24810.01530.2032-10.68882.972-27.6968
54.58680.54451.35664.34560.65894.5670.07450.0557-0.237-0.3845-0.07450.06610.0988-0.27370.10480.1914-0.00060.02190.1850.0020.2039-16.9726-11.3991-20.1301
61.8336-0.33041.06881.4563-0.80421.71530.0148-0.102-0.2633-0.02850.03870.11180.1709-0.1808-0.06060.2258-0.02340.01680.2188-0.0010.2687-15.4304-22.0951-7.1771
78.0813-0.61162.0693.99232.65463.3880.02821.01840.1874-0.3690.1568-0.092-0.22250.3104-0.08510.16520.00990.02520.29360.02720.351219.0768-23.4196-2.5571
84.8442-0.95220.31591.6821-1.16413.2735-0.18810.33910.424-0.059-0.0226-0.3673-0.06160.32950.19650.22440.0301-0.0130.23650.03290.413927.3921-23.56821.4846
92.06670.52890.08341.14410.26020.4095-0.08351.38820.1064-0.5084-0.3396-0.07610.32380.48540.05920.45590.06470.09210.64910.05790.45425.1588-24.1201-11.299
103.626-0.77270.16892.30330.05870.90930.27940.5907-0.128-0.2784-0.13110.01760.31680.15440.05120.25390.04870.0090.2583-0.00460.317218.3845-26.295-3.2939
117.5026-0.6204-0.38648.2109-0.22978.296-0.1682-1.1615-0.10380.50480.3648-0.0341-0.40391.0345-0.21920.28840.0741-0.00680.4970.00610.32732.6237-33.388810.654
121.0242.0059-1.81855.9822-0.72727.31260.1009-0.443-1.41930.45430.03240.87810.6278-0.6089-0.11340.28820.0005-0.00230.2780.04720.65539.6597-36.22045.4814
134.13530.39220.23932.9715-0.21032.385-0.0939-0.4150.260.2696-0.0279-0.3573-0.04210.10390.02540.24530.0571-0.0430.2568-0.01860.31549.9417-17.56578.8047
143.9572-3.4603-1.64693.31620.22624.7283-0.3186-0.76360.91580.57520.3546-0.6774-0.52990.27870.15760.41720.1061-0.08750.5561-0.05020.46578.5192-15.515617.3213
153.75-0.1126-0.0190.6932-0.11023.9759-0.01820.1137-0.0163-0.0562-0.0032-0.0969-0.08810.0294-0.0040.18540.0289-0.01250.17750.02410.2732.6825-22.3358-2.6011
162.16-0.24440.41124.1489-1.00054.50860.19650.7622-0.6291-0.9035-0.09320.47080.5966-0.615-0.12871.2650.0994-0.2071.4242-0.45680.2676-27.8541-10.0545-54.1082
172.5161.0477-1.97066.3119-0.46911.5601-0.43180.6212-1.11890.01840.41220.54170.8995-0.6690.02421.0935-0.0892-0.20020.6092-0.05530.5773-26.4187-12.2584-48.5717
180.04110.043-0.01710.054-0.01590.03530.36090.4682-0.5533-0.1580.03620.26380.1499-0.336-0.27041.03980.0934-0.47691.82160.27760.9003-37.7305-3.1961-58.2029
193.52910.3718-0.1065.94450.89294.86240.21160.3991-0.5139-0.2647-0.33421.41940.8242-1.49780.14760.6812-0.0587-0.18050.942-0.06070.5013-34.107-4.9876-44.8175
204.48620.70851.4740.4975-0.30391.4123-0.40180.64690.8261-0.9431-0.04470.5323-0.9873-0.87770.34261.2870.2769-0.25441.07210.0020.5745-29.01933.6751-52.1984
210.47140.27670.00074.11621.5640.6228-0.07620.866-0.5653-0.842-0.1658-0.0671-0.2532-0.41620.06241.32880.1462-0.20131.4720.10270.4308-28.552-1.2683-59.787
221.030.19280.67520.2489-0.93885.90260.08560.1964-0.0377-0.7861-0.10190.4729-0.1167-0.80380.12390.63240.037-0.1390.4417-0.04210.263-25.6704-4.9246-39.8403
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 93 )
3X-RAY DIFFRACTION3chain 'A' and (resid 94 through 124 )
4X-RAY DIFFRACTION4chain 'A' and (resid 125 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 55 )
9X-RAY DIFFRACTION9chain 'B' and (resid 56 through 65 )
10X-RAY DIFFRACTION10chain 'B' and (resid 66 through 79 )
11X-RAY DIFFRACTION11chain 'B' and (resid 80 through 89 )
12X-RAY DIFFRACTION12chain 'B' and (resid 90 through 97 )
13X-RAY DIFFRACTION13chain 'C' and (resid 15 through 46 )
14X-RAY DIFFRACTION14chain 'C' and (resid 47 through 66 )
15X-RAY DIFFRACTION15chain 'C' and (resid 67 through 112 )
16X-RAY DIFFRACTION16chain 'D' and (resid 1 through 7 )
17X-RAY DIFFRACTION17chain 'D' and (resid 8 through 16 )
18X-RAY DIFFRACTION18chain 'D' and (resid 17 through 22 )
19X-RAY DIFFRACTION19chain 'D' and (resid 23 through 44 )
20X-RAY DIFFRACTION20chain 'D' and (resid 45 through 56 )
21X-RAY DIFFRACTION21chain 'D' and (resid 57 through 65 )
22X-RAY DIFFRACTION22chain 'D' and (resid 66 through 76 )

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