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- PDB-5sb8: Tubulin-maytansinoid-3-complex -

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Basic information

Entry
Database: PDB / ID: 5sb8
TitleTubulin-maytansinoid-3-complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine LigaseTubulin—tyrosine ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / nervous system development / mitotic cell cycle / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. ...Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / Beta tubulin, autoregulation binding site / Beta tubulin / Tubulin / Tubulin, C-terminal / Tubulin C-terminal domain / Tubulin, conserved site / Tubulin subunits alpha, beta, and gamma signature. / Tubulin/FtsZ family, C-terminal domain / Tubulin/FtsZ-like, C-terminal domain / Tubulin/FtsZ, C-terminal / Tubulin/FtsZ, 2-layer sandwich domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ family, GTPase domain / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily
Similarity search - Domain/homology
Chem-5IS / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / Tubulin tyrosine ligase / Stathmin-4 / Tubulin alpha-1B chain / Tubulin beta-2B chain
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
Gallus gallus (chicken)
Bos taurus (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / DIFFERENCE FOURIER / Resolution: 2.3 Å
AuthorsMarzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. ...Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
H2020-MSCA-ITN-2019860070 TUBINTRAINEuropean Union
CitationJournal: Chemistry / Year: 2022
Title: Maytansinol Derivatives: Side Reactions as a Chance for New Tubulin Binders.
Authors: Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Altmann, K.H. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
History
DepositionJul 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 9, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2Mar 9, 2022Group: Data collection / Category: reflns
Item: _reflns.number_obs / _reflns.pdbx_number_measured_all ..._reflns.number_obs / _reflns.pdbx_number_measured_all / _reflns.pdbx_redundancy / _reflns.pdbx_scaling_rejects
Revision 1.3May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tubulin alpha-1B chain
B: Tubulin beta-2B chain
C: Tubulin alpha-1B chain
D: Tubulin beta-2B chain
E: Stathmin-4
F: Tubulin-Tyrosine Ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,12222
Polymers261,6316
Non-polymers3,49116
Water8,215456
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.664, 157.491, 181.511
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 6 molecules ACBDEF

#1: Protein Tubulin alpha-1B chain / Alpha-tubulin ubiquitous / Tubulin K-alpha-1 / Tubulin alpha-ubiquitous chain


Mass: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: Brain / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Organ: Brain / References: UniProt: Q6B856
#3: Protein Stathmin-4 / / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Production host: Escherichia coli (E. coli) / References: UniProt: P63043
#4: Protein Tubulin-Tyrosine Ligase / Tubulin—tyrosine ligase


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 9 types, 472 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine triphosphate


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#9: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#10: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#11: Chemical ChemComp-5IS / (1S,2R,3S,5S,6S,16E,18E,20R)-11-chloro-6-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-4,24-dioxa-9,22-diazatetracyclo[19.3.1.1~10,14~.0~3,5~]hexacosa-10(26),11,13,16,18,21-hexaene-8,23-dione


Mass: 547.040 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C28H35ClN2O7 / Feature type: SUBJECT OF INVESTIGATION
#12: Chemical ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C11H18N5O12P3 / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#13: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 456 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.8 Å3/Da / Density % sol: 56.6 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 3% PEG 4K, 4% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00003 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Feb 23, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2.3→49.66 Å / Num. obs: 133463 / % possible obs: 100 % / Redundancy: 13.738 % / Biso Wilson estimate: 50.05 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.189 / Rrim(I) all: 0.196 / Χ2: 0.765 / Net I/σ(I): 10.9 / Num. measured all: 1833232
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.3-2.3613.9562.8640.93136575979097860.3892.973100
2.36-2.4214.262.3661.16136226955695530.4952.454100
2.42-2.4914.2021.8451.51131753928092770.6151.914100
2.49-2.5714.1151.5581.82126616897189700.6821.616100
2.57-2.6613.951.2192.35121825873687330.7771.266100
2.66-2.7513.8061.0132.82116837846484630.8371.052100
2.75-2.8513.3440.7593.7108689814681450.8990.789100
2.85-2.9712.6690.5924.699804787878780.9290.617100
2.97-3.114.0330.4276.66105979755275520.9670.443100
3.1-3.2513.6750.3168.7199146725072500.9810.328100
3.25-3.4312.810.22811.4588159688268820.9890.237100
3.43-3.6414.1870.16615.8592927655065500.9950.172100
3.64-3.8914.20.12320.7386961612461240.9970.128100
3.89-4.213.9830.09625.0280642576857670.9980.1100
4.2-4.613.6780.07929.372192527852780.9980.082100
4.6-5.1412.950.07330.6162367481648160.9980.076100
5.14-5.9413.0750.08128.3355763426542650.9980.084100
5.94-7.2712.8990.07629.8147249366336630.9980.079100
7.27-10.2913.9790.05542.0939798284728470.9990.057100
10.29-49.6612.6650.0545.220872166916480.9980.05298.7

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Processing

Software
NameVersionClassificationNB
PHENIX1.19.1_4122refinement
XSCALEdata scaling
PDB_EXTRACT3.28data extraction
XDSdata reduction
PHENIX1.19.1_4122phasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 5LXT

5lxt


Resolution: 2.3→49.66 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.92 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2299 6673 5 %
Rwork0.1932 126778 -
obs0.195 133451 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 188.08 Å2 / Biso mean: 65.7256 Å2 / Biso min: 31.55 Å2
Refinement stepCycle: final / Resolution: 2.3→49.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17329 0 219 456 18004
Biso mean--65.42 55.75 -
Num. residues----2189
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.3-2.330.33822230.317342254448
2.33-2.350.35112190.304241634382
2.35-2.380.29652210.299241994420
2.38-2.410.35942180.311541464364
2.41-2.440.33072190.299741654384
2.44-2.480.30472200.279441814401
2.48-2.510.31962210.280741924413
2.51-2.550.33092220.270742174439
2.55-2.590.28552210.249941934414
2.59-2.630.27732190.241741694388
2.63-2.680.28092220.241142184440
2.68-2.730.29032190.237441664385
2.73-2.780.32322210.235441894410
2.78-2.840.26222210.23542064427
2.84-2.90.27312200.242441844404
2.9-2.970.29132230.253142324455
2.97-3.040.27032220.2342064428
3.04-3.120.26672210.216441984419
3.12-3.210.24842210.209242054426
3.21-3.320.25262230.204742414464
3.32-3.440.25482220.199742214443
3.44-3.570.22852220.189442094431
3.57-3.740.21452230.180442514474
3.74-3.930.21182240.159642424466
3.93-4.180.19312240.157642524476
4.18-4.50.19092240.144742654489
4.5-4.950.15972260.135142844510
4.95-5.670.18562260.16142944520
5.67-7.140.19662280.184743434571
7.14-49.660.19722380.168745224760
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)
10.6844-0.563-0.55231.2101-0.18490.98990.00780.12780.2752-0.47990.1734-0.0169-0.84050.26400.9183-0.15990.13350.5769-0.12930.608328.647696.423552.6878
21.383-0.18240.15412.70111.6123.0731-0.00970.05750.0226-0.05340.2757-0.2554-0.32850.43820.00180.4652-0.0530.05280.4982-0.12890.518928.887181.824757.4625
30.94110.6039-0.15151.11030.66561.24040.1039-0.041-0.12220.3546-0.28890.6534-0.1361-0.545500.63070.01820.12920.5581-0.14920.64969.167484.576871.7612
40.693-0.06490.02752.7861.76852.9102-0.023-0.1257-0.0190.64370.16140.03910.23510.22970.00010.4989-0.01790.03480.5061-0.08870.513523.057976.653469.905
50.5677-0.2896-0.38840.5695-0.19540.6336-0.09590.15110.3934-0.32980.1930.1726-0.5384-0.18040.00010.49970.0470.03350.4794-0.06230.629815.620564.47121.7041
60.4626-0.0326-0.12830.2820.08930.05840.14020.2460.9314-0.2143-0.2508-0.0527-0.76340.0163-0.00010.92240.09590.00820.5848-0.0180.836915.296478.565322.2757
70.7405-0.6564-0.28571.00230.24121.31930.20370.46180.2218-0.5662-0.0833-0.1603-0.53370.1505-00.58920.00010.04250.6688-0.04080.588324.609858.824213.2551
81.1717-0.0386-0.2082.95561.41323.1328-0.00170.04610.0482-0.034-0.08460.1122-0.0492-0.147-0.0160.30690.02280.01710.4436-0.10580.469217.273753.444926.4191
90.5204-0.4692-0.26711.32870.04262.3988-0.02910.05640.1599-0.0312-0.12050.0855-0.2631-0.358300.48220.04990.0050.5349-0.1930.553910.91362.931638.2844
100.9901-0.61810.43260.94480.74481.9733-0.1413-0.18030.10310.4059-0.16910.27850.0658-0.594300.48830.0030.07550.6318-0.12950.59118.908555.69741.6158
110.1802-0.1652-0.01850.98390.13860.86820.0072-0.1073-0.19830.70390.1161-0.24440.75870.60150.0060.569-0.0172-0.02810.5801-0.07780.544725.573737.96930.5175
121.0946-0.21110.06662.50110.28271.9219-0.04550.21280.0825-0.31350.0811-0.0367-0.1590.137300.3809-0.0840.02590.4666-0.03080.433320.133233.0275-11.9131
130.9082-0.46220.00331.81461.05141.748-0.0239-0.00850.03950.0687-0.07840.14070.1084-0.205800.356-0.07430.03910.4165-0.02810.45237.531925.91443.0954
141.5820.00870.31060.5668-0.39380.7964-0.22140.56660.2703-0.41090.3150.0494-0.0948-0.23450.00010.8103-0.1156-0.00130.9529-0.05830.545214.850211.1696-40.8333
152.63580.06820.2390.13160.01560.02350.02921.53930.3933-0.9851-0.0156-0.25670.2564-0.53780.00771.1003-0.19320.11651.2321-0.11190.575721.04596.1275-49.2057
161.7994-0.1817-0.15861.65930.00992.2632-0.22490.5915-0.2457-0.57410.2289-0.2080.41840.1155-0.00030.8327-0.0810.12380.7761-0.23140.581123.9935-4.4816-36.5714
170.7071-0.621-0.1691.2650.81021.29490.0310.2926-0.0897-0.4753-0.04570.19220.0913-0.315100.6334-0.0679-0.01560.6795-0.09320.550710.03712.5095-25.0848
181.8192-0.5074-0.41451.04790.39352.7023-0.22790.3144-0.2774-0.14290.07920.23510.4113-0.36100.6646-0.15490.0320.6137-0.1110.55028.2549-3.298-20.7878
191.40420.17010.44751.2277-0.55170.5009-0.45150.2675-0.75330.01280.1023-0.08761.03410.1824-0.01341.01450.0290.17730.684-0.24450.828930.1619-17.4799-24.3921
200.50470.18410.27810.45610.51340.5896-0.1298-0.04490.09720.63160.1472-0.50050.22830.6371-0.00011.0758-0.08650.04760.7665-0.17030.727127.510492.486682.2748
210.4765-0.2391-0.50190.13540.17960.6346-0.0077-0.021-0.01210.38470.283-0.4210.53970.45620.01450.54590.08210.02810.8172-0.21820.737742.854327.52154.0592
221.33570.304-1.21651.0060.36591.5454-0.33770.3426-0.4622-0.05460.0215-0.16881.1139-0.342301.0824-0.12050.13210.7074-0.13440.75726.106454.801669.7872
230.3480.10430.1650.228-0.07130.15190.1717-0.3870.12950.3912-0.1079-0.5749-0.32590.8961-0.00010.86990.0099-0.00141.00260.04710.774511.303165.740997.4733
240.0204-0.03-0.0050.12580.03160.00830.2491-0.5114-0.01540.3308-0.4482-0.8638-00.625801.1234-0.1115-0.35871.8210.23121.245222.267661.8084109.2817
250.14030.17240.10150.21160.12470.07310.2118-0.8327-0.40440.67240.2516-1.10190.18260.8085-0.00041.17290.2757-0.00181.85950.39811.285719.387152.9499107.8639
261.90410.4169-1.19060.77050.29691.198-0.4301-0.2677-0.65240.08870.0141-0.15741.08780.106-0.00031.09990.06760.22780.61590.11920.792-1.869153.224896.9072
270.51550.15740.12770.0617-0.02450.3214-0.40730.4028-1.0016-0.3933-0.3655-0.94590.69640.91370.00081.82310.2310.41960.88150.30311.67074.811338.8428104.0327
280.57110.22270.60760.70620.57190.8279-0.44780.1607-0.6536-0.38350.2214-0.221.1719-0.3301-0.07991.3977-0.00660.35520.52930.13260.9166-11.157649.6028102.3597
291.70460.1992-0.39670.43190.41130.9951-0.2037-0.159-0.28160.11260.2398-0.16760.32640.12930.00010.9630.09640.09080.55760.02370.63752.332161.930991.6016
300.7253-0.2034-0.28020.0570.08770.5946-0.11090.5066-0.13050.29170.26390.35220.4216-0.7333-0.00010.9242-0.16510.12580.7689-0.04910.8415-6.928857.87780.2449
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 79 )A1 - 79
2X-RAY DIFFRACTION2chain 'A' and (resid 80 through 273 )A80 - 273
3X-RAY DIFFRACTION3chain 'A' and (resid 274 through 311 )A274 - 311
4X-RAY DIFFRACTION4chain 'A' and (resid 312 through 438 )A312 - 438
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 27 )B2 - 27
6X-RAY DIFFRACTION6chain 'B' and (resid 28 through 64 )B28 - 64
7X-RAY DIFFRACTION7chain 'B' and (resid 65 through 127 )B65 - 127
8X-RAY DIFFRACTION8chain 'B' and (resid 128 through 238 )B128 - 238
9X-RAY DIFFRACTION9chain 'B' and (resid 239 through 295 )B239 - 295
10X-RAY DIFFRACTION10chain 'B' and (resid 296 through 401 )B296 - 401
11X-RAY DIFFRACTION11chain 'B' and (resid 402 through 437 )B402 - 437
12X-RAY DIFFRACTION12chain 'C' and (resid 1 through 199 )C1 - 199
13X-RAY DIFFRACTION13chain 'C' and (resid 200 through 440 )C200 - 440
14X-RAY DIFFRACTION14chain 'D' and (resid 1 through 56 )D1 - 56
15X-RAY DIFFRACTION15chain 'D' and (resid 57 through 88 )D57 - 88
16X-RAY DIFFRACTION16chain 'D' and (resid 89 through 238 )D89 - 238
17X-RAY DIFFRACTION17chain 'D' and (resid 239 through 295 )D239 - 295
18X-RAY DIFFRACTION18chain 'D' and (resid 296 through 399 )D296 - 399
19X-RAY DIFFRACTION19chain 'D' and (resid 400 through 441 )D400 - 441
20X-RAY DIFFRACTION20chain 'E' and (resid 6 through 46 )E6 - 46
21X-RAY DIFFRACTION21chain 'E' and (resid 47 through 143 )E47 - 143
22X-RAY DIFFRACTION22chain 'F' and (resid 1 through 66 )F1 - 66
23X-RAY DIFFRACTION23chain 'F' and (resid 67 through 96 )F67 - 96
24X-RAY DIFFRACTION24chain 'F' and (resid 97 through 140 )F97 - 140
25X-RAY DIFFRACTION25chain 'F' and (resid 141 through 184 )F141 - 184
26X-RAY DIFFRACTION26chain 'F' and (resid 185 through 223 )F185 - 223
27X-RAY DIFFRACTION27chain 'F' and (resid 224 through 257 )F224 - 257
28X-RAY DIFFRACTION28chain 'F' and (resid 258 through 283 )F258 - 283
29X-RAY DIFFRACTION29chain 'F' and (resid 284 through 339 )F284 - 339
30X-RAY DIFFRACTION30chain 'F' and (resid 340 through 382 )F340 - 382

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