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- PDB-8bdg: Tubulin-taxane-2b complex -

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Basic information

Entry
Database: PDB / ID: 8bdg
TitleTubulin-taxane-2b complex
Components
  • (Tubulin beta-2B ...) x 2
  • Stathmin-4
  • Tubulin alpha-1B chain
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 / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / microtubule cytoskeleton / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / cilium / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. ...Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / Stathmin family / Stathmin, conserved site / Stathmin superfamily / Stathmin family / Stathmin family signature 1. / Stathmin family signature 2. / Stathmin-like (SLD) domain profile. / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / 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 / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-R3T / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.35 Å
AuthorsProta, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muehlethaler, T. ...Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muehlethaler, T. / Gago, F. / Oliva, M.A. / Steinmetz, M.O. / Fang, W.S. / Diaz, J.F.
Funding support Switzerland, Spain, European Union, 4items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
Spanish Ministry of Science, Innovation, and Universities2019-104545RB-I00 Spain
Spanish Ministry of Science, Innovation, and UniversitiesCOV20/01007 Spain
H2020 Marie Curie Actions of the European Commission2019 860070European Union
CitationJournal: Elife / Year: 2023
Title: Structural insight into the stabilization of microtubules by taxanes.
Authors: Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Josa-Prado, F. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muhlethaler, T. / Gago, F. / Oliva, M.A. ...Authors: Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Josa-Prado, F. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muhlethaler, T. / Gago, F. / Oliva, M.A. / Steinmetz, M.O. / Fang, W.S. / Diaz, J.F.
History
DepositionOct 19, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 22, 2023Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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 beta-2B chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,57819
Polymers261,6316
Non-polymers3,94713
Water2,990166
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22020 Å2
ΔGint-140 kcal/mol
Surface area78790 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.250, 158.640, 179.190
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 , 2 types, 3 molecules ACE

#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 (domestic cattle) / Organ: Brain / References: UniProt: P81947
#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

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Tubulin beta-2B ... , 2 types, 3 molecules BDF

#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 (domestic cattle) / Organ: Brain / References: UniProt: Q6B856
#4: Protein Tubulin beta-2B chain


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 , 7 types, 179 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-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.: 1 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-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


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#10: Chemical ChemComp-R3T / [(1~{S},2~{S},3~{R},4~{S},7~{R},9~{S},10~{S},12~{R},15~{S})-4-acetyloxy-15-[(2~{R},3~{S})-3-(2-bromanylethanoylamino)-2-oxidanyl-3-phenyl-propanoyl]oxy-10,14,16,16-tetramethyl-1,9,12-tris(oxidanyl)-11-oxidanylidene-6-oxatetracyclo[11.3.1.0^{3,10}.0^{4,7}]heptadec-13-en-2-yl] benzoate


Mass: 828.696 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C40H46BrNO13 / Feature type: SUBJECT OF INVESTIGATION
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 166 / 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: 3.05 Å3/Da / Density % sol: 59.69 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 2-4% PEG 4K, 2-10% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.91501 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: May 25, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91501 Å / Relative weight: 1
ReflectionResolution: 2.35→49.368 Å / Num. obs: 125172 / % possible obs: 100 % / Redundancy: 54.879 % / Biso Wilson estimate: 56.92 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.176 / Rrim(I) all: 0.178 / Χ2: 0.994 / Net I/σ(I): 27.8 / Num. measured all: 6869262 / Scaling rejects: 1348
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
2.35-2.4155.2354.0691.24505791916191570.6324.107100
2.41-2.4857.2983.0561.72512247894289400.7663.083100
2.48-2.5556.9792.5432.11494579868386800.8132.566100
2.55-2.6356.7271.9152.88479404845184510.8841.932100
2.63-2.7155.9751.5993.5459612821282110.9061.613100
2.71-2.8155.391.2214.6439241793479300.9471.23299.9
2.81-2.9154.0130.8876.35413095765076480.9690.895100
2.91-3.0350.5620.6498.5373858739673940.9830.656100
3.03-3.1755.7120.45612.61395113709470920.9920.46100
3.17-3.3255.2030.33617.04373721677067700.9960.339100
3.32-3.551.8260.23423.35336402649164910.9980.236100
3.5-3.7255.4180.17632.37338219610561030.9990.178100
3.72-3.9756.8840.11946.88329017578557840.9990.12100
3.97-4.2956.0290.08364.163002045358535810.084100
4.29-4.754.6920.0683.482717124968496810.061100
4.7-5.2552.430.05785.622380314540454010.058100
5.25-6.0751.4270.06478.052055553997399710.064100
6.07-7.4352.0750.05389.761784613427342710.054100
7.43-10.5154.7870.03144.081478162698269810.03100
10.51-49.36850.3480.024165.08771841557153310.02598.5

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Processing

Software
NameVersionClassification
PHENIX1.13_2998refinement
XSCALEdata scaling
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5lxt

5lxt


Resolution: 2.35→49.368 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 23.83 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2139 6170 4.93 %
Rwork0.1829 118998 -
obs0.1845 125168 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 374.86 Å2 / Biso mean: 76.1165 Å2 / Biso min: 29.76 Å2
Refinement stepCycle: final / Resolution: 2.35→49.368 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17193 0 248 166 17607
Biso mean--95.88 59.43 -
Num. residues----2172
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
2.35-2.37670.36231950.32323946
2.3767-2.40470.32922290.2993897
2.4047-2.4340.34231990.27813895
2.434-2.46480.2882210.2683915
2.4648-2.49720.32042000.25813925
2.4972-2.53140.29282000.2553924
2.5314-2.56760.29092240.23683959
2.5676-2.60590.25821890.23463910
2.6059-2.64660.27181840.22883957
2.6466-2.690.27112030.2383959
2.69-2.73640.25841770.23183931
2.7364-2.78620.26422290.22053919
2.7862-2.83980.25122020.21643955
2.8398-2.89770.28371790.223960
2.8977-2.96070.26322360.21723888
2.9607-3.02960.27121920.21013964
3.0296-3.10530.27172120.2113973
3.1053-3.18930.24452050.21233946
3.1893-3.28310.25652120.21693935
3.2831-3.3890.24731880.20423983
3.389-3.51010.20661930.18733979
3.5101-3.65060.22042150.183942
3.6506-3.81670.19531780.17353996
3.8167-4.01790.20812170.16293990
4.0179-4.26950.19012230.15663973
4.2695-4.59890.16042160.13433994
4.5989-5.06130.1722080.13714022
5.0613-5.79270.1722120.16374049
5.7927-7.29440.20852090.17864076
7.2944-49.3680.1682230.1634236
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)
11.153-0.3803-0.31042.4732-0.17621.80930.11450.15360.2537-0.3530.047-0.1947-0.83080.0613-0.1540.786-0.05360.09730.5655-0.14680.526128.966997.805953.4035
20.61210.12030.94243.41930.42551.4481-0.20330.26180.1263-1.17380.2563-0.1095-0.81030.0318-0.11640.9657-0.11530.05840.5789-0.11390.570828.099987.357642.1152
30.7226-0.0999-0.34982.49830.87222.0719-0.04170.0306-0.0702-0.02840.2358-0.4279-0.04250.4445-0.20960.4902-0.00630.03240.5681-0.2140.552935.176278.638954.7614
42.8104-1.0551-0.16522.8680.14752.57830.23580.2932-0.23970.1459-0.12490.67570.1773-0.8092-0.06930.48560.01690.03620.5961-0.15810.681911.763779.543759.5952
50.8360.31990.21792.80461.03033.43940.131-0.11330.0740.4954-0.110.1471-0.2127-0.042-0.05550.53420.00970.08350.4536-0.13790.545718.782987.342368.0326
61.62750.3770.37082.18380.74781.64710.0808-0.22170.03370.5112-0.05950.30840.1111-0.1054-0.02050.69670.00180.13970.5169-0.17180.538617.567488.825976.2933
70.51940.0651-0.13481.31341.22672.26610.17160.06730.00540.50430.1455-0.14980.42780.1195-0.29950.61290.06270.00350.5196-0.15090.535527.56161.61857.5353
81.97280.99320.10032.5237-1.07490.68380.1761-0.1711-0.53760.9737-0.2046-0.20390.07610.29270.0020.8620.1631-0.07210.6359-0.14040.660229.610262.636471.1477
92.1857-0.3637-0.20722.0739-0.15122.1490.04540.22620.37-0.2545-0.15080.1984-0.7004-0.10650.09320.64440.0578-0.03910.4579-0.06260.618816.43970.156619.208
101.21060.0178-0.04052.31381.28712.417-0.03370.14030.1067-0.17220.1083-0.0508-0.21290.2394-0.08210.33970.0130.01130.4637-0.11310.421926.254754.451721.8571
111.2379-0.0821-0.07871.12810.48642.8857-0.0012-0.08460.3270.0892-0.21430.3754-0.1952-0.47930.21940.42260.050.06580.5488-0.20820.60112.024557.946332.5592
121.2328-0.91870.02823.21940.13720.6477-0.1315-0.2381-0.2935-0.0295-0.16880.92460.0854-1.02750.41230.60310.02980.03331.0566-0.33510.8498-0.4757.068438.2062
133.0877-1.9686-0.87171.68810.68070.8401-0.6408-0.750.12910.72340.27640.4936-0.6168-1.42550.42690.77390.27670.00291.0564-0.31230.78074.817665.447646.9645
140.8464-0.3120.41960.8311.23672.7333-0.0777-0.05590.16380.3942-0.2060.24040.1918-0.48840.32490.4687-0.05270.09240.5289-0.11850.493812.281652.426339.1814
151.0316-0.260.5312.86081.68664.40060.0438-0.0931-0.27910.6971-0.0244-0.19530.71630.4117-0.03080.5046-0.038-0.05040.4513-0.04260.464525.884738.142630.8264
161.2438-0.41660.04162.43080.02591.5961-0.08570.24880.0749-0.25470.1176-0.0514-0.09690.1694-0.03550.3025-0.08480.03490.3984-0.05770.359420.289933.4048-11.9285
171.3824-0.42360.4521.27271.05482.39190.0124-0.0690.06740.0216-0.12730.21150.0809-0.34640.11070.3141-0.05780.06260.4017-0.050.42012.763231.2533.1809
180.7704-0.4580.00651.93690.91821.6032-0.05830.0585-0.10320.31480.1337-0.1020.38630.182-0.10580.34130.00340.01120.349-0.06490.405820.170213.72872.4399
192.3164-0.65650.07731.71890.3421.7642-0.19240.6771-0.091-0.62690.1499-0.1430.06270.11150.02870.8261-0.16210.09110.9508-0.17310.523722.53977.2236-44.29
201.22350.23750.04680.9465-0.22261.6676-0.13860.3691-0.2881-0.35570.2127-0.15770.3210.0949-0.08710.6078-0.07380.06190.6853-0.25110.564320.3865-2.2342-32.0738
210.2516-0.4083-0.08850.91370.20321.4211-0.12350.3692-0.4121-0.14240.01920.39070.3997-0.51570.08760.7632-0.18010.00780.868-0.19020.70252.9943-5.7083-25.2285
221.3771-0.0623-0.05441.8260.85782.5236-0.12430.2086-0.2329-0.17120.12960.00840.2807-0.32940.02330.5711-0.13050.05940.535-0.12830.48869.3309-2.2443-21.4764
232.9362-0.0474-1.57592.00020.48853.3907-0.35370.0475-0.85840.1620.1935-0.31161.07510.62330.13380.87270.07780.04550.7426-0.29970.843830.4456-15.9704-24.643
242.3097-1.6560.75474.311-0.21250.3650.0632-0.11560.17380.69270.1924-0.1202-0.55780.3868-0.17490.9756-0.12680.03730.7534-0.23070.646727.521793.665881.2245
250.1982-0.0821-0.33670.67071.06891.567-0.0974-0.0188-0.08680.39890.464-0.42520.54070.6716-0.38830.59850.08350.02760.8145-0.24820.737243.005829.07714.8223
262.27120.3774-1.40952.24510.53222.6969-0.32260.2706-0.5066-0.10850.0655-0.02110.8948-0.21160.23951.0467-0.07280.1330.7336-0.1560.73766.221155.282669.6852
272.87171.00220.13992.258-2.6433.8022-0.224-0.52640.24420.59920.0811-0.29510.14521.20380.16930.88990.0331-0.03031.01030.00030.71311.072466.689297.1714
282.07630.98920.66662.5148-0.87110.9186-0.1318-0.8555-0.16680.8276-0.217-1.22820.2510.70750.3631.05080.1511-0.13191.82930.27561.049220.428357.6569108.1839
292.247-0.0697-1.01670.7512-0.19772.6811-0.6105-0.0986-0.94460.0362-0.1308-0.30431.01860.08710.84631.11110.03670.24650.63890.12970.8689-2.165254.15196.7781
301.2699-0.98170.02081.30971.44693.8651-0.56180.2209-1.037-0.1098-0.3617-0.67910.68010.77371.0372.13420.33180.16551.06760.33541.55722.279940.8343103.4693
312.1379-0.3681-1.72090.55580.96232.8679-0.3293-0.0058-0.42740.26660.30870.12480.5228-0.0176-0.03251.00880.0250.16570.60050.05870.6773-2.278558.831794.8525
322.68930.2922-0.41742.2259-0.09284.1133-0.21870.7925-0.9135-0.1341-0.05210.40821.2342-0.88640.28390.8948-0.20330.15060.9573-0.19520.856-7.524155.875678.8328
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 71 )A1 - 71
2X-RAY DIFFRACTION2chain 'A' and (resid 72 through 102 )A72 - 102
3X-RAY DIFFRACTION3chain 'A' and (resid 103 through 199 )A103 - 199
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 223 )A200 - 223
5X-RAY DIFFRACTION5chain 'A' and (resid 224 through 306 )A224 - 306
6X-RAY DIFFRACTION6chain 'A' and (resid 307 through 381 )A307 - 381
7X-RAY DIFFRACTION7chain 'A' and (resid 382 through 414 )A382 - 414
8X-RAY DIFFRACTION8chain 'A' and (resid 415 through 450 )A415 - 450
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 88 )B1 - 88
10X-RAY DIFFRACTION10chain 'B' and (resid 89 through 197 )B89 - 197
11X-RAY DIFFRACTION11chain 'B' and (resid 198 through 273 )B198 - 273
12X-RAY DIFFRACTION12chain 'B' and (resid 274 through 311 )B274 - 311
13X-RAY DIFFRACTION13chain 'B' and (resid 312 through 338 )B312 - 338
14X-RAY DIFFRACTION14chain 'B' and (resid 339 through 401 )B339 - 401
15X-RAY DIFFRACTION15chain 'B' and (resid 402 through 438 )B402 - 438
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 199 )C1 - 199
17X-RAY DIFFRACTION17chain 'C' and (resid 200 through 372 )C200 - 372
18X-RAY DIFFRACTION18chain 'C' and (resid 373 through 440 )C373 - 440
19X-RAY DIFFRACTION19chain 'D' and (resid 1 through 127 )D1 - 127
20X-RAY DIFFRACTION20chain 'D' and (resid 128 through 268 )D128 - 268
21X-RAY DIFFRACTION21chain 'D' and (resid 269 through 311 )D269 - 311
22X-RAY DIFFRACTION22chain 'D' and (resid 312 through 401 )D312 - 401
23X-RAY DIFFRACTION23chain 'D' and (resid 402 through 441 )D402 - 441
24X-RAY DIFFRACTION24chain 'E' and (resid 6 through 46 )E6 - 46
25X-RAY DIFFRACTION25chain 'E' and (resid 47 through 141 )E47 - 141
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 66 )F1 - 66
27X-RAY DIFFRACTION27chain 'F' and (resid 67 through 96 )F67 - 96
28X-RAY DIFFRACTION28chain 'F' and (resid 97 through 184 )F97 - 184
29X-RAY DIFFRACTION29chain 'F' and (resid 185 through 223 )F185 - 223
30X-RAY DIFFRACTION30chain 'F' and (resid 224 through 257 )F224 - 257
31X-RAY DIFFRACTION31chain 'F' and (resid 258 through 339 )F258 - 339
32X-RAY DIFFRACTION32chain 'F' and (resid 340 through 378 )F340 - 378

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