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- PDB-6qtn: Tubulin-cyclostreptin complex -

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Basic information

Entry
Database: PDB / ID: 6qtn
TitleTubulin-cyclostreptin 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
Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family ...Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / 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. / 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 non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Cyclostreptin / 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 / FOURIER SYNTHESIS / Resolution: 1.9 Å
AuthorsBalaguer, F.d.A. / Muehlethaler, T. / Estevez-Gallego, J. / Calvo, E. / Gimenez-Abian, J.F. / Risinger, A.L. / Sorensen, E.J. / Vanderwal, C.D. / Altmann, K.-H. / Mooberry, S.L. ...Balaguer, F.d.A. / Muehlethaler, T. / Estevez-Gallego, J. / Calvo, E. / Gimenez-Abian, J.F. / Risinger, A.L. / Sorensen, E.J. / Vanderwal, C.D. / Altmann, K.-H. / Mooberry, S.L. / Steinmetz, M.O. / Oliva, M.A. / Prota, A.E. / Diaz, J.F.
Funding support Spain, Switzerland, United States, 4items
OrganizationGrant numberCountry
Spanish Ministry of Economy and CompetitivenessBFU2016-75319-R Spain
Spanish Ministry of Science, Innovation, and UniversitiesRYC-2011-07900 Spain
Swiss National Science Foundation31003A_166608 Switzerland
National Institutes of Health/National Cancer Institute (NIH/NCI)R01CA121138 United States
CitationJournal: Int J Mol Sci / Year: 2019
Title: Crystal Structure of the Cyclostreptin-Tubulin Adduct: Implications for Tubulin Activation by Taxane-Site Ligands.
Authors: Balaguer, F.A. / Muhlethaler, T. / Estevez-Gallego, J. / Calvo, E. / Gimenez-Abian, J.F. / Risinger, A.L. / Sorensen, E.J. / Vanderwal, C.D. / Altmann, K.H. / Mooberry, S.L. / Steinmetz, M.O. ...Authors: Balaguer, F.A. / Muhlethaler, T. / Estevez-Gallego, J. / Calvo, E. / Gimenez-Abian, J.F. / Risinger, A.L. / Sorensen, E.J. / Vanderwal, C.D. / Altmann, K.H. / Mooberry, S.L. / Steinmetz, M.O. / Oliva, M.A. / Prota, A.E. / Diaz, J.F.
History
DepositionFeb 25, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 3, 2019Provider: repository / Type: Initial release
Revision 1.1Mar 30, 2022Group: Author supporting evidence / Database references / Derived calculations
Category: database_2 / pdbx_audit_support ...database_2 / pdbx_audit_support / pdbx_struct_conn_angle / struct_conn / struct_conn_type
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn_type.id
Revision 1.2Jan 24, 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-Tyrosine Ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,67226
Polymers261,6316
Non-polymers4,04020
Water12,268681
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23720 Å2
ΔGint-152 kcal/mol
Surface area80130 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.585, 158.361, 179.946
Angle α, β, γ (deg.)90.00, 90.00, 90.00
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 , 10 types, 701 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.: 2 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H6O2
#9: 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
#10: 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
#11: Chemical ChemComp-JHH / Cyclostreptin


Mass: 402.524 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C24H34O5
#12: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#13: 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
#14: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 681 / Source method: isolated from a natural source / Formula: H2O

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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: 2.85 Å3/Da / Density % sol: 56.81 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 6% glycerol, 3% PEG4000, 0.1 M Mes/0.1 M imidazole pH 6.7, 30 mM CaCl2, 30 mM MgCl2

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Sep 27, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→49.7 Å / Num. obs: 234346 / % possible obs: 100 % / Redundancy: 26.8 % / CC1/2: 1 / Rmerge(I) obs: 0.102 / Rpim(I) all: 0.025 / Rrim(I) all: 0.104 / Net I/σ(I): 22.7
Reflection shellResolution: 1.9→1.95 Å / Redundancy: 27 % / Rmerge(I) obs: 4.485 / Mean I/σ(I) obs: 0.9 / Num. unique obs: 17147 / CC1/2: 0.322 / Rpim(I) all: 0.843 / Rrim(I) all: 4.572 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5LXT

5lxt


Resolution: 1.9→49.655 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.29
RfactorNum. reflection% reflection
Rfree0.2133 11838 5.05 %
Rwork0.1866 --
obs0.188 234314 99.98 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.9→49.655 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17274 0 254 681 18209
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00418007
X-RAY DIFFRACTIONf_angle_d0.65224456
X-RAY DIFFRACTIONf_dihedral_angle_d15.49710787
X-RAY DIFFRACTIONf_chiral_restr0.0452662
X-RAY DIFFRACTIONf_plane_restr0.0043157
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9-1.92160.40253920.38357284X-RAY DIFFRACTION100
1.9216-1.94420.41284270.39697354X-RAY DIFFRACTION100
1.9442-1.96790.3933620.37987347X-RAY DIFFRACTION100
1.9679-1.99280.32963830.33927341X-RAY DIFFRACTION100
1.9928-2.0190.34073750.30867403X-RAY DIFFRACTION100
2.019-2.04670.29643830.29667371X-RAY DIFFRACTION100
2.0467-2.07590.30323970.28587325X-RAY DIFFRACTION100
2.0759-2.10690.31053990.27537371X-RAY DIFFRACTION100
2.1069-2.13990.26473810.2537408X-RAY DIFFRACTION100
2.1399-2.17490.25233590.24077357X-RAY DIFFRACTION100
2.1749-2.21240.28683980.23957354X-RAY DIFFRACTION100
2.2124-2.25270.2614080.22887342X-RAY DIFFRACTION100
2.2527-2.2960.23584040.21487389X-RAY DIFFRACTION100
2.296-2.34290.25453860.2127386X-RAY DIFFRACTION100
2.3429-2.39380.22723840.20237393X-RAY DIFFRACTION100
2.3938-2.44950.22043970.19637365X-RAY DIFFRACTION100
2.4495-2.51070.2154150.19667383X-RAY DIFFRACTION100
2.5107-2.57860.22643990.19587368X-RAY DIFFRACTION100
2.5786-2.65450.2483980.20237409X-RAY DIFFRACTION100
2.6545-2.74020.24933940.20517402X-RAY DIFFRACTION100
2.7402-2.83810.26174130.20247404X-RAY DIFFRACTION100
2.8381-2.95170.23543870.20347424X-RAY DIFFRACTION100
2.9517-3.0860.23833920.19827450X-RAY DIFFRACTION100
3.086-3.24870.23923750.19237454X-RAY DIFFRACTION100
3.2487-3.45220.21023860.18787481X-RAY DIFFRACTION100
3.4522-3.71870.19774120.17167443X-RAY DIFFRACTION100
3.7187-4.09270.19554230.15157470X-RAY DIFFRACTION100
4.0927-4.68460.16364170.13857523X-RAY DIFFRACTION100
4.6846-5.90060.17484020.15527600X-RAY DIFFRACTION100
5.9006-49.67230.17383900.16847875X-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)
10.86570.14070.04013.57121.46272.626-0.02520.17220.1053-0.44090.3489-0.4222-0.72360.4946-0.27110.5303-0.14640.10630.5241-0.19330.453931.638786.458952.8742
21.82230.19620.27733.32331.61613.99220.0625-0.08190.10520.4207-0.0860.298-0.2116-0.11290.01010.447-0.00320.10390.3523-0.13060.40816.835786.976970.5059
31.51620.3559-0.54974.18282.49464.56240.0867-0.1143-0.20830.86180.2217-0.30190.85820.3651-0.2430.460.1268-0.08920.4111-0.14860.454529.182262.407961.6733
41.9224-0.2633-0.02752.85591.22422.71470.00580.12060.3376-0.28540.0189-0.009-0.52550.0723-0.03430.3066-0.01610.01920.3372-0.09030.383121.399660.999321.2276
51.5275-0.26590.50191.39010.86233.0596-0.134-0.22590.06510.0916-0.15490.312-0.0835-0.82140.22550.34810.02940.04570.602-0.23280.52486.669159.918338.2838
60.7278-0.37070.65554.38162.8745.06540.0332-0.1193-0.15370.7985-0.0497-0.03060.76130.1106-0.03630.3494-0.012-0.0250.3282-0.05850.300222.787937.542230.8768
71.52980.0081-0.01672.27240.54442.0423-0.07460.2270.1406-0.31130.1423-0.0899-0.2430.1929-0.05640.2647-0.08630.03890.3511-0.05220.311820.045833.107-11.4955
81.2643-0.14410.48681.50541.09562.4609-0.0358-0.03460.11060.0085-0.18640.28430.0596-0.42650.18210.2112-0.05770.04950.3103-0.08430.35812.43131.38513.5679
91.8332-0.654-1.4283.26992.59154.32910.01860.0695-0.13880.3940.1323-0.1620.54730.2001-0.19380.35610.0488-0.02830.2826-0.0570.360122.293211.16952.0241
102.3711-0.27080.08062.46540.1842.2941-0.18880.6465-0.0931-0.63470.2769-0.31080.17690.129-0.08930.6708-0.12530.13480.7494-0.20950.402823.95513.0686-40.0235
111.40240.0882-0.31461.93660.71552.8442-0.1520.4-0.2275-0.24310.12780.20830.2746-0.54540.0210.4417-0.09610.00080.5374-0.14170.39537.6545-0.2159-24.8127
121.6515-1.422-2.03142.13681.47093.7146-0.3110.157-0.8779-0.0040.2164-0.47330.77890.68810.12630.8210.04550.08970.6094-0.31620.799628.7136-17.9512-26.8811
132.9818-2.19910.08168.5591-1.14022.096-0.44-0.42710.391.25820.4808-0.8137-0.21640.5573-0.12881.1668-0.10220.02550.5904-0.19140.519525.063995.368683.983
141.87343.60583.55726.24266.77947.09640.1751-0.43980.3550.3790.3897-0.47020.24480.6497-0.63870.43970.0025-0.00050.9672-0.42740.725643.480355.238834.6313
150.3352-1.6431-1.58768.33696.87417.1026-0.1416-0.2136-0.07410.45110.3631-0.43870.81460.8074-0.24830.46780.07390.14830.784-0.3160.754942.86776.2271-20.6206
163.34711.1946-1.64494.04280.47864.8434-0.44050.2793-0.6847-0.09630.0669-0.14661.0982-0.31030.31870.8626-0.07870.11550.5536-0.14830.57716.035855.170869.8355
172.76190.38590.31032.1099-0.63583.3375-0.1145-1.011-0.48950.5129-0.3875-0.76570.19241.59470.42350.81020.1564-0.11491.16020.21340.79614.407858.8458105.6912
182.10960.4897-1.57871.37690.07562.3769-0.40110.0238-0.75130.25390.2173-0.01630.9932-0.092-0.02730.92740.02650.12650.43910.06290.6696-2.316154.718793.053
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 205)
2X-RAY DIFFRACTION2chain 'A' and (resid 206 through 381)
3X-RAY DIFFRACTION3chain 'A' and (resid 382 through 436)
4X-RAY DIFFRACTION4chain 'B' and (resid 2 through 205)
5X-RAY DIFFRACTION5chain 'B' and (resid 206 through 381)
6X-RAY DIFFRACTION6chain 'B' and (resid 382 through 436)
7X-RAY DIFFRACTION7chain 'C' and (resid 1 through 205)
8X-RAY DIFFRACTION8chain 'C' and (resid 206 through 381)
9X-RAY DIFFRACTION9chain 'C' and (resid 382 through 440)
10X-RAY DIFFRACTION10chain 'D' and (resid 2 through 205)
11X-RAY DIFFRACTION11chain 'D' and (resid 206 through 381)
12X-RAY DIFFRACTION12chain 'D' and (resid 382 through 436)
13X-RAY DIFFRACTION13chain 'E' and (resid 7 through 28)
14X-RAY DIFFRACTION14chain 'E' and (resid 45 through 89)
15X-RAY DIFFRACTION15chain 'E' and (resid 90 through 144)
16X-RAY DIFFRACTION16chain 'F' and (resid 1 through 66)
17X-RAY DIFFRACTION17chain 'F' and (resid 67 through 198)
18X-RAY DIFFRACTION18chain 'F' and (resid 199 through 384)

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