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- PDB-8oyp: Crystal structure of Ubiquitin specific protease 11 (USP11) in co... -

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Basic information

Entry
Database: PDB / ID: 8oyp
TitleCrystal structure of Ubiquitin specific protease 11 (USP11) in complex with a substrate mimetic
Components
  • Polyubiquitin-B
  • Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS
KeywordsHYDROLASE / Protease / Ubiquitin / Substrate complex / Deubiquitinating enzyme
Function / homology
Function and homology information


hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / mitochondrion transport along microtubule / fat pad development / female gonad development / seminiferous tubule development / protein deubiquitination / male meiosis I / phosphorelay signal transduction system ...hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein monoubiquitination / mitochondrion transport along microtubule / fat pad development / female gonad development / seminiferous tubule development / protein deubiquitination / male meiosis I / phosphorelay signal transduction system / Association of TriC/CCT with target proteins during biosynthesis / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / energy homeostasis / regulation of neuron apoptotic process / regulation of proteasomal protein catabolic process / 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 / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / p75NTR recruits signalling complexes / Downregulation of ERBB4 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / Pexophagy / Regulation of innate immune responses to cytosolic DNA / InlA-mediated entry of Listeria monocytogenes into host cells / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NF-kB is activated and signals survival / NRIF signals cell death from the nucleus / Regulation of PTEN localization / Activated NOTCH1 Transmits Signal to the Nucleus / Regulation of BACH1 activity / Translesion synthesis by REV1 / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLK / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / Josephin domain DUBs / neuron projection morphogenesis / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / transcription corepressor binding / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / regulation of mitochondrial membrane potential / 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 / positive regulation of protein ubiquitination / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / AUF1 (hnRNP D0) binds and destabilizes mRNA / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / Regulation of NF-kappa B signaling / TNFR2 non-canonical NF-kB pathway / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / NOTCH3 Activation and Transmission of Signal to the Nucleus / Negative regulators of DDX58/IFIH1 signaling / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Hh mutants are degraded by ERAD / Recognition of DNA damage by PCNA-containing replication complex / Peroxisomal protein import
Similarity search - Function
Ubiquitin-like domain, USP-type / Ubiquitin-like domain / Peptidase C19, ubiquitin-specific peptidase, DUSP domain / DUSP-like superfamily / DUSP domain / DUSP domain profile. / Domain in ubiquitin-specific proteases. / Ubiquitin carboxyl-terminal hydrolase, C-terminal / Ubiquitin-specific protease C-terminal / Ubiquitin specific protease (USP) domain signature 2. ...Ubiquitin-like domain, USP-type / Ubiquitin-like domain / Peptidase C19, ubiquitin-specific peptidase, DUSP domain / DUSP-like superfamily / DUSP domain / DUSP domain profile. / Domain in ubiquitin-specific proteases. / Ubiquitin carboxyl-terminal hydrolase, C-terminal / Ubiquitin-specific protease C-terminal / Ubiquitin specific protease (USP) domain signature 2. / Ubiquitin specific protease (USP) domain signature 1. / Ubiquitin specific protease, conserved site / Peptidase C19, ubiquitin carboxyl-terminal hydrolase / Ubiquitin carboxyl-terminal hydrolase / Ubiquitin specific protease domain / Ubiquitin specific protease (USP) domain profile. / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Papain-like cysteine peptidase 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
: / NITRATE ION / PHOSPHATE ION / Polyubiquitin-B / Ubiquitin carboxyl-terminal hydrolase 11 / Response regulator FrzS
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.44 Å
AuthorsMaurer, S.K. / Caulton, S.G. / Ward, S.J. / Emsley, J. / Dreveny, I.
Funding support United Kingdom, 2items
OrganizationGrant numberCountry
Biotechnology and Biological Sciences Research Council (BBSRC)BB/H012656/1 United Kingdom
Biotechnology and Biological Sciences Research Council (BBSRC)BB/M008770/1 United Kingdom
CitationJournal: J.Biol.Chem. / Year: 2023
Title: Ubiquitin-specific protease 11 structure in complex with an engineered substrate mimetic reveals a molecular feature for deubiquitination selectivity.
Authors: Maurer, S.K. / Mayer, M.P. / Ward, S.J. / Boudjema, S. / Halawa, M. / Zhang, J. / Caulton, S.G. / Emsley, J. / Dreveny, I.
History
DepositionMay 5, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 18, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2023Group: Database references / Category: citation / Item: _citation.journal_volume / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS
B: Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS
C: Polyubiquitin-B
D: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,74816
Polymers127,8304
Non-polymers91812
Water9,098505
1
A: Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS
C: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,3748
Polymers63,9152
Non-polymers4596
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5720 Å2
ΔGint-26 kcal/mol
Surface area22010 Å2
2
B: Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS
D: Polyubiquitin-B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,3748
Polymers63,9152
Non-polymers4596
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5960 Å2
ΔGint-23 kcal/mol
Surface area22720 Å2
Unit cell
Length a, b, c (Å)94.321, 186.102, 75.761
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11A-1182-

HOH

21A-1318-

HOH

31B-1267-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 302 or resid 304 through 348...
21(chain B and (resid 303 through 348 or resid 350...
12(chain C and (resid 1 through 23 or resid 25 through 201))
22(chain D and (resid 1 through 23 or resid 25 through 201))

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PHEPHELEULEU(chain A and (resid 302 or resid 304 through 348...AA302 - 9368 - 477
21LYSLYSHISHIS(chain B and (resid 303 through 348 or resid 350...BB303 - 9419 - 482
12METMETGLYGLY(chain C and (resid 1 through 23 or resid 25 through 201))CC1 - 791 - 79
22METMETGLYGLY(chain D and (resid 1 through 23 or resid 25 through 201))DD1 - 791 - 79

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Ubiquitin carboxyl-terminal hydrolase 11,Response regulator FrzS / Deubiquitinating enzyme 11 / Ubiquitin thioesterase 11 / Ubiquitin-specific-processing protease 11


Mass: 55166.938 Da / Num. of mol.: 2 / Mutation: C318S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: USP11, UHX1, frzS, MXAN_4149 / Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: P51784, UniProt: Q1D4U9, ubiquitinyl hydrolase 1
#2: Protein Polyubiquitin-B


Mass: 8747.987 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P0CG47

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Non-polymers , 6 types, 517 molecules

#3: Chemical ChemComp-CD / CADMIUM ION


Mass: 112.411 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cd
#4: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#5: Chemical
ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: NO3
#6: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO4
#7: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 505 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 2.6 Å3/Da / Density % sol: 52.71 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 100 mM Tris/Bicine pH 8.5, 30 mM sodium nitrate, 30 mM sodium phosphate dibasic, 30 mM ammonium sulphate, 11.25% v/v MPD; 11.25% PEG 1000; 11.25% w/v PEG 3350 with 5 mM CdCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.999995 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: May 19, 2020
RadiationMonochromator: Bartels Monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.999995 Å / Relative weight: 1
ReflectionResolution: 2.44→48 Å / Num. obs: 50488 / % possible obs: 99.8 % / Redundancy: 13.4 % / CC1/2: 0.988 / Rmerge(I) obs: 0.404 / Rpim(I) all: 0.114 / Rrim(I) all: 0.42 / Net I/σ(I): 7.6 / Num. measured all: 675489
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.44-2.5213.32.7826003445150.4370.7822.8911.198.4
9.76-4812.50.059113809080.9980.0170.06135.799.2

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Processing

Software
NameVersionClassification
Aimless0.7.4data scaling
PHENIX1.20.1refinement
PDB_EXTRACT3.27data extraction
xia2data reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.44→48 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.38 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2351 2520 5 %
Rwork0.1697 47898 -
obs0.173 50418 99.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 140.02 Å2 / Biso mean: 44.2121 Å2 / Biso min: 16.97 Å2
Refinement stepCycle: final / Resolution: 2.44→48 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8730 0 42 505 9277
Biso mean--49.43 39.94 -
Num. residues----1102
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A4179X-RAY DIFFRACTION12.71TORSIONAL
12B4179X-RAY DIFFRACTION12.71TORSIONAL
21C764X-RAY DIFFRACTION12.71TORSIONAL
22D764X-RAY DIFFRACTION12.71TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 18

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.44-2.490.35021350.27482549268497
2.49-2.540.30661370.253926072744100
2.54-2.590.31381380.240226232761100
2.59-2.650.30761370.225326182755100
2.65-2.720.30451390.231326522791100
2.72-2.790.29621400.213326412781100
2.79-2.870.33111370.223226272764100
2.87-2.970.31051390.201826492788100
2.97-3.070.25821390.185926282767100
3.07-3.20.21881390.171626512790100
3.2-3.340.2111400.159226482788100
3.34-3.520.21411390.155626672806100
3.52-3.740.20751400.13926552795100
3.74-4.030.2041420.126426902832100
4.03-4.430.15021420.11126862828100
4.43-5.070.16961420.113727002842100
5.07-6.390.23291440.171727462890100
6.39-480.27921510.200928613012100
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)
13.7397-1.33461.62522.9126-1.46085.16190.05060.2035-0.4624-0.46640.03360.28490.36210.1539-0.01790.233-0.0208-0.04110.2638-0.08480.3827-25.9989-8.482426.0423
24.0588-1.2776-0.61144.00630.57331.5242-0.0921-0.1656-0.91540.5598-0.05870.67580.2213-0.15950.1520.3265-0.0570.01970.28140.03840.4733-35.1104-2.073342.2899
32.6561-2.94950.40967.1026-1.29322.1193-0.02470.1455-0.81340.2091-0.17820.83290.0443-0.31190.17090.2884-0.12680.01570.341-0.05690.5194-34.5991-7.715534.7389
41.13520.075-0.36061.14840.46151.7508-0.06890.2886-0.2165-0.105-0.01730.4170.1567-0.20180.04880.229-0.0466-0.07080.3683-0.04490.4372-33.2394-1.752426.9965
52.43760.33140.08936.37341.21071.58790.22-0.2120.20720.5741-0.25830.5815-0.3857-0.11910.02340.44750.00510.07480.32280.01070.2636-31.890620.201947.7285
61.7680.8975-0.84962.8516-0.41681.08230.1415-0.18850.13610.4175-0.09750.1951-0.17140.0041-0.03450.2425-0.0305-0.00670.2713-0.00610.24-21.621119.225842.1567
73.41261.67-1.39156.30140.0162.7956-0.07490.30810.0678-0.19-0.0080.03290.1121-0.3390.0580.3335-0.0106-0.00170.360.02260.2382.177826.58810.3172
81.3273-0.5212-0.3862.39430.5821.24890.02580.07960.1656-0.2336-0.0228-0.1723-0.33670.07080.02770.267-0.0685-0.01340.29530.0080.2085-14.542522.184929.1485
93.0148-0.29940.45274.2183-0.05762.2256-0.0932-0.1599-0.20720.23350.0858-0.2447-0.0480.1502-0.0240.1847-0.01930.02350.26890.00270.2451-12.8620.876131.5509
103.19760.564-0.54813.6658-0.97764.35880.1831-0.17230.02770.12420.22980.69470.2902-0.4744-0.17530.25160.01040.02820.25570.06370.328-60.003514.931482.2099
112.71170.9602-0.91123.5318-0.41493.4893-0.25740.2276-0.6194-0.7990.26410.12040.8151-0.20110.09250.6601-0.1187-0.01880.2589-0.0320.3357-51.92278.784965.0116
127.4357-0.0555-1.37983.4214-0.91573.7373-0.36770.3884-0.7584-0.49130.39510.60260.5043-0.4079-0.00910.4408-0.0799-0.06450.25090.02420.3721-58.28647.663473.5333
132.74870.7576-0.9163.8359-1.06243.6765-0.129-0.2259-0.26120.27970.0906-0.08140.4340.19060.06680.30950.01930.00760.22980.04540.2884-49.938312.295980.4074
147.61722.9612-3.28373.5117-1.7612.9349-0.19940.0018-0.6858-0.6359-0.1167-0.13980.67010.09190.33350.44760.01920.04210.34-0.01870.2304-38.500914.863359.3633
158.8072-1.3674-0.71727.6121-2.53115.67950.10850.40881.2498-0.1271-0.438-0.4838-0.59790.41510.10660.6892-0.00270.04580.34370.09410.4102-32.775134.358553.2264
161.35682.0143-0.46855.6208-0.27251.8872-0.21240.2494-0.0944-0.55960.258-0.2887-0.0366-0.0879-0.10590.25760.0003-0.01570.21830.0220.2205-41.81831.642562.1701
176.2146-1.1241-2.41544.11093.0498.35880.01240.21430.2053-0.09320.4637-0.83450.01220.7277-0.46020.50830.02690.03320.5777-0.19340.5669-45.240658.646499.1954
183.44131.4701-0.83483.3441-1.18681.59740.08620.14960.33810.19920.18390.485-0.1736-0.2406-0.18290.27990.07650.03920.25970.00410.3445-53.33233.746474.3208
192.6654-0.7685-3.29565.44523.85768.11870.23110.27730.4414-0.1929-0.1423-0.1571-0.5085-0.0452-0.10350.21530.0285-0.03450.29340.05360.2632-22.357127.699328.9355
207.10112.0943-1.10155.38390.98216.2691-0.00970.57520.7847-0.5356-0.33780.741-0.9092-0.52140.37610.37570.0796-0.12330.29650.02190.3829-32.702427.745425.6312
212.78211.0954-1.18621.79180.54494.53880.0120.12040.0236-0.01730.1220.4923-0.0222-0.308-0.16460.2480.0252-0.05910.26380.01460.3616-30.300820.101730.0518
224.01970.9155-0.92333.05660.31683.8101-0.21160.7411-0.6207-0.42590.25310.33040.2817-0.3428-0.01670.3435-0.0141-0.10740.3454-0.05940.3021-26.27485.714716.6592
235.6756-3.8766-3.69727.03224.4646.85860.3538-0.13350.78070.0093-0.0598-0.9112-0.29610.1725-0.33910.3124-0.0385-0.08470.28210.05620.3045-32.869236.656174.1312
241.6577-1.35981.65262.47840.66034.62290.2796-0.2072-0.51380.18570.1112-1.43780.09090.8962-0.3250.35550.1430.04230.4560.10880.5837-24.264925.624170.3167
255.38252.4161-1.514.03073.37816.35620.177-0.7299-0.13091.3057-0.1359-0.82490.80451.00890.05460.4939-0.0294-0.15550.43590.17590.548-28.232630.066180.4083
263.11231.4545-1.62814.7761-1.16616.3778-0.0418-0.1304-0.32180.2-0.2356-0.32010.3140.07970.2310.30090.0185-0.07140.2290.0640.31-35.147325.847174.2015
274.59723.10135.62779.85793.77666.87270.534-1.57480.04590.9645-0.67430.5114-0.2254-0.48190.03730.48760.0292-0.01530.36050.10230.3016-48.33123.394689.2638
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 302 through 329 )A302 - 329
2X-RAY DIFFRACTION2chain 'A' and (resid 330 through 356 )A330 - 356
3X-RAY DIFFRACTION3chain 'A' and (resid 357 through 369 )A357 - 369
4X-RAY DIFFRACTION4chain 'A' and (resid 370 through 415 )A370 - 415
5X-RAY DIFFRACTION5chain 'A' and (resid 416 through 434 )A416 - 434
6X-RAY DIFFRACTION6chain 'A' and (resid 435 through 489 )A435 - 489
7X-RAY DIFFRACTION7chain 'A' and (resid 490 through 609 )A490 - 609
8X-RAY DIFFRACTION8chain 'A' and (resid 610 through 612 )A610 - 612
9X-RAY DIFFRACTION9chain 'A' and (resid 778 through 936 )A778 - 936
10X-RAY DIFFRACTION10chain 'B' and (resid 303 through 329 )B303 - 329
11X-RAY DIFFRACTION11chain 'B' and (resid 330 through 356 )B330 - 356
12X-RAY DIFFRACTION12chain 'B' and (resid 357 through 371 )B357 - 371
13X-RAY DIFFRACTION13chain 'B' and (resid 372 through 415 )B372 - 415
14X-RAY DIFFRACTION14chain 'B' and (resid 416 through 425 )B416 - 425
15X-RAY DIFFRACTION15chain 'B' and (resid 426 through 434 )B426 - 434
16X-RAY DIFFRACTION16chain 'B' and (resid 435 through 489 )B435 - 489
17X-RAY DIFFRACTION17chain 'B' and (resid 490 through 609 )B490 - 609
18X-RAY DIFFRACTION18chain 'B' and (resid 610 through 941 )B610 - 941
19X-RAY DIFFRACTION19chain 'C' and (resid 1 through 16 )C1 - 16
20X-RAY DIFFRACTION20chain 'C' and (resid 17 through 34 )C17 - 34
21X-RAY DIFFRACTION21chain 'C' and (resid 35 through 70 )C35 - 70
22X-RAY DIFFRACTION22chain 'C' and (resid 71 through 79 )C71 - 79
23X-RAY DIFFRACTION23chain 'D' and (resid 1 through 16 )D1 - 16
24X-RAY DIFFRACTION24chain 'D' and (resid 17 through 22 )D17 - 22
25X-RAY DIFFRACTION25chain 'D' and (resid 23 through 34 )D23 - 34
26X-RAY DIFFRACTION26chain 'D' and (resid 35 through 70 )D35 - 70
27X-RAY DIFFRACTION27chain 'D' and (resid 71 through 79 )D71 - 79

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