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- PDB-4tuy: Tubulin-Rhizoxin complex -

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Basic information

Entry
Database: PDB / ID: 4tuy
TitleTubulin-Rhizoxin complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine Ligase
KeywordsCELL CYCLE / CYTOSKELETON / TUBULIN FOLD / RHIZOXIN
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / neuron projection development / mitotic cell cycle / nervous system development / growth cone / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / microtubule / neuron projection / protein heterodimerization activity / GTPase activity / nucleotide binding / 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, A domain / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 60s Ribosomal Protein L30; Chain: A; / Alpha tubulin / Tubulin-beta mRNA autoregulation signal. / 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 / Dna Ligase; domain 1 / 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
Chem-36L / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / 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: 2.1 Å
AuthorsProta, A.E. / Bargsten, K. / Diaz, J.F. / Marsh, M. / Cuevas, C. / Liniger, M. / Neuhaus, C. / Andreu, J.M. / Altmann, K.H. / Steinmetz, M.O.
Funding support Switzerland, Spain, 5items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_138659 Switzerland
Ministero de Economia y CompetitividadBIO2010-16351 Spain
Ministero de Economia y CompetitividadBFU2011-23416 Spain
Comunidad Autonoma de MadridS201/BMD-2457 Spain
Comunidad Autonoma de MadridS2010/BMD-2353 Spain
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs.
Authors: Prota, A.E. / Bargsten, K. / Diaz, J.F. / Marsh, M. / Cuevas, C. / Liniger, M. / Neuhaus, C. / Andreu, J.M. / Altmann, K.H. / Steinmetz, M.O.
History
DepositionJun 25, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Aug 27, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2014Group: Database references
Revision 1.2Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.pdbx_dist_value / _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

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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)265,07620
Polymers261,6316
Non-polymers3,44514
Water21,4201189
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22400 Å2
ΔGint-141 kcal/mol
Surface area79720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.310, 156.920, 181.120
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 / Tubulin alpha chain


Mass: 50204.445 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / 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) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1 / Fragment: STATHMIN-LIKE DOMAIN, Residues 49-189
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


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 , 8 types, 1203 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.: 2 / 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-36L / (1R,2R,3E,5R,7R,8S,10S,13E,16R)-8-hydroxy-10-[(2S,3R,4E,6E,8E)-3-methoxy-4,8-dimethyl-9-(2-methyl-1,3-oxazol-4-yl)nona-4,6,8-trien-2-yl]-2,7-dimethyl-6,11,19-trioxatricyclo[14.3.1.0~5,7~]icosa-3,13-diene-12,18-dione / Rhizoxin


Mass: 609.750 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C35H47NO8 / Comment: antitumor*YM
#11: 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
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1189 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.83 Å3/Da / Density % sol: 56.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 6% PEG, 16% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Mar 3, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→68.4 Å / Num. obs: 173215 / % possible obs: 100 % / Redundancy: 13.6 % / Rmerge(I) obs: 0.165 / Net I/σ(I): 16.9
Reflection shellResolution: 2.1→2.15 Å / Redundancy: 14.3 % / Mean I/σ(I) obs: 1.3 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.9_1692)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.1→62.7 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 23.22 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.217 8659 5 %
Rwork0.184 --
obs0.186 173178 100 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.1→62.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17256 0 214 1189 18659
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218026
X-RAY DIFFRACTIONf_angle_d0.65824500
X-RAY DIFFRACTIONf_dihedral_angle_d12.5316744
X-RAY DIFFRACTIONf_chiral_restr0.0262689
X-RAY DIFFRACTIONf_plane_restr0.0033172
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12390.34042870.3135448X-RAY DIFFRACTION100
2.1239-2.14890.29872830.29995381X-RAY DIFFRACTION100
2.1489-2.17510.31892890.29595496X-RAY DIFFRACTION100
2.1751-2.20260.29172830.28265383X-RAY DIFFRACTION100
2.2026-2.23160.31062870.27185459X-RAY DIFFRACTION100
2.2316-2.26220.29892850.26895415X-RAY DIFFRACTION100
2.2622-2.29450.27642860.25675424X-RAY DIFFRACTION100
2.2945-2.32870.2892870.25465460X-RAY DIFFRACTION100
2.3287-2.36510.31072850.24945408X-RAY DIFFRACTION100
2.3651-2.40390.28582870.24145464X-RAY DIFFRACTION100
2.4039-2.44530.27472890.22665478X-RAY DIFFRACTION100
2.4453-2.48980.23842870.21945452X-RAY DIFFRACTION100
2.4898-2.53770.27382850.21155423X-RAY DIFFRACTION100
2.5377-2.58950.22812860.20195435X-RAY DIFFRACTION100
2.5895-2.64580.24582880.2035469X-RAY DIFFRACTION100
2.6458-2.70740.25342870.2075445X-RAY DIFFRACTION100
2.7074-2.77510.26792870.20545461X-RAY DIFFRACTION100
2.7751-2.85010.24672880.19575475X-RAY DIFFRACTION100
2.8501-2.9340.23432880.19065466X-RAY DIFFRACTION100
2.934-3.02870.20842890.18235491X-RAY DIFFRACTION100
3.0287-3.13690.22112880.17625470X-RAY DIFFRACTION100
3.1369-3.26250.23362900.18435509X-RAY DIFFRACTION100
3.2625-3.4110.20632890.17835486X-RAY DIFFRACTION100
3.411-3.59080.19852900.16825514X-RAY DIFFRACTION100
3.5908-3.81570.17522890.15635497X-RAY DIFFRACTION100
3.8157-4.11030.18642910.14975521X-RAY DIFFRACTION100
4.1103-4.52380.16232930.13825576X-RAY DIFFRACTION100
4.5238-5.17820.17392930.13915556X-RAY DIFFRACTION100
5.1782-6.52280.19652970.17475652X-RAY DIFFRACTION100
6.5228-62.73020.19083060.16755805X-RAY DIFFRACTION99
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)
11.2116-0.1568-0.07973.01911.12182.10140.00050.1120.1792-0.43560.2899-0.3095-0.6680.4206-0.21750.5023-0.14040.11360.3943-0.12830.348131.680887.942351.895
20.999-0.337-0.10752.35611.13742.76270.03960.0355-0.00620.1876-0.00360.1558-0.155-0.0407-0.04540.3098-0.00090.04980.2512-0.0630.286319.205381.870265.8778
30.8089-0.25610.07763.5121.36141.94730.0003-0.08440.07660.4254-0.00570.1131-0.0926-0.01240.00070.4075-0.00240.07990.3369-0.05160.320518.743282.962373.4377
40.78340.056-0.13112.36871.70263.30570.0258-0.0204-0.1860.45650.358-0.37470.47640.7828-0.3730.32910.0833-0.06250.3407-0.12390.382732.641361.505860.5479
53.99220.0829-0.52150.66922.21287.76850.0048-0.30960.30790.2825-0.13650.1504-0.6870.10380.09371.38580.08920.10710.8491-0.08590.684124.260265.562784.7669
63.2721-0.8229-0.33743.13510.78952.92290.18110.2570.602-0.2458-0.09970.0608-0.7092-0.1651-0.06080.3940.03930.04270.3044-0.00310.413116.35469.959719.4068
71.9991-0.499-0.70713.17340.38761.80670.110.359-0.0148-0.30260.0588-0.2603-0.37250.3712-0.15260.3018-0.05940.02860.4861-0.07110.280429.072856.088614.5026
81.51990.7018-0.41182.93230.97152.21760.0312-0.1029-0.0639-0.02230.0586-0.201-0.09480.2275-0.07070.16810.0010.02760.3144-0.09610.291824.350852.921625.987
93.1786-1.10260.69510.6189-0.51480.4797-0.1678-0.4282-0.03440.0339-0.24410.65540.1388-0.82390.1630.2469-0.07230.05240.6722-0.29620.52845.28650.806428.0964
100.4317-0.5171-0.20491.46850.66021.73570.0068-0.0832-0.0091-0.0047-0.06970.2043-0.2792-0.35740.05510.28440.01370.02640.398-0.12280.405810.076961.731135.6185
112.1131-0.47110.70381.44050.25162.1295-0.1436-0.15950.03960.2343-0.10440.2331-0.0794-0.70170.19420.36070.03940.04720.553-0.1570.41116.510860.658844.7281
121.1554-1.068-0.20132.57172.07892.2764-0.0368-0.0461-0.11750.3154-0.04450.36590.4329-0.17140.10390.3155-0.03810.04280.3058-0.05140.30815.225541.970934.0359
130.5194-0.25690.15582.71571.99416.0755-0.0401-0.1256-0.12760.58480.0715-0.1150.67660.5925-0.02930.28350.0177-0.02740.2993-0.04550.31825.45738.02331.3487
140.9699-0.1594-0.04452.33150.15381.5363-0.03270.12670.1218-0.25790.0653-0.0841-0.10930.1022-0.02430.2173-0.04730.0320.2879-0.01760.242920.23732.6249-12.1009
150.8306-0.2509-0.08071.43390.82221.698-0.0090.00950.0630.0614-0.08960.11930.1004-0.19520.07630.1693-0.06060.02930.2389-0.02770.24717.690225.78083.1309
163.386-1.04160.60892.85040.2442.3629-0.05080.55310.1142-0.68020.03030.08320.0537-0.17360.03260.6525-0.09480.03220.6673-0.04620.324217.35789.3157-43.9826
170.8776-0.1153-0.21311.5560.50011.7415-0.08220.3841-0.1349-0.430.0737-0.16770.32780.0519-0.03350.5979-0.03430.0870.4973-0.14730.357320.9234-2.6494-33.5145
181.7544-0.5085-0.34371.21980.32691.8897-0.1510.2686-0.2067-0.12260.00910.20780.3561-0.19460.17930.4794-0.11210.03670.3813-0.10380.32728.7853-4.1757-21.2438
192.7314-0.8568-1.36181.64441.2942.0815-0.16470.0768-0.4459-0.0390.1234-0.27340.69430.3233-0.12070.80530.11030.1130.4287-0.15450.571230.131-16.7838-24.1616
201.6103-0.2331-0.12362.09330.20241.56390.0919-0.1240.05990.87690.2114-0.1357-0.00590.5867-0.27220.8162-0.0359-0.08170.5916-0.16050.515527.387792.164882.1177
210.16920.0552-0.15171.25811.47542.07-0.0384-0.0369-0.00150.42830.5389-0.56940.59970.7355-0.490.36940.09110.0250.6461-0.20160.567442.645129.0575.7594
221.72511.2233-0.97863.24230.21651.1155-0.51260.5277-0.5549-0.3740.1036-0.04711.1141-0.55190.21480.981-0.17860.16990.5199-0.14780.5576.252654.263769.873
230.9574-0.29770.10211.8877-0.64182.5878-0.182-0.9238-0.56740.6835-0.4175-0.94480.11151.56090.44280.77930.0574-0.1241.05270.30390.758614.845257.8816106.0501
242.17880.706-1.88311.3955-0.40431.681-0.4413-0.0571-0.67250.09720.1352-0.06550.879-0.0294-0.04070.8430.03370.1560.3430.05420.5688-1.188452.881793.8378
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN 'A' AND (RESSEQ 1:180)
2X-RAY DIFFRACTION2CHAIN 'A' AND (RESSEQ 181:311)
3X-RAY DIFFRACTION3CHAIN 'A' AND (RESSEQ 312:401)
4X-RAY DIFFRACTION4CHAIN 'A' AND (RESSEQ 402:436)
5X-RAY DIFFRACTION5CHAIN 'A' AND (RESSEQ 437:438)
6X-RAY DIFFRACTION6CHAIN 'B' AND (RESSEQ 1:88)
7X-RAY DIFFRACTION7CHAIN 'B' AND (RESSEQ 89:127)
8X-RAY DIFFRACTION8CHAIN 'B' AND (RESSEQ 128:197)
9X-RAY DIFFRACTION9CHAIN 'B' AND (RESSEQ 198:223)
10X-RAY DIFFRACTION10CHAIN 'B' AND (RESSEQ 224:295)
11X-RAY DIFFRACTION11CHAIN 'B' AND (RESSEQ 296:373)
12X-RAY DIFFRACTION12CHAIN 'B' AND (RESSEQ 374:401)
13X-RAY DIFFRACTION13CHAIN 'B' AND (RESSEQ 402:438)
14X-RAY DIFFRACTION14CHAIN 'C' AND (RESSEQ 1:197)
15X-RAY DIFFRACTION15CHAIN 'C' AND (RESSEQ 198:440)
16X-RAY DIFFRACTION16CHAIN 'D' AND (RESSEQ 1:88)
17X-RAY DIFFRACTION17CHAIN 'D' AND (RESSEQ 89:295)
18X-RAY DIFFRACTION18CHAIN 'D' AND (RESSEQ 296:401)
19X-RAY DIFFRACTION19CHAIN 'D' AND (RESSEQ 402:441)
20X-RAY DIFFRACTION20CHAIN 'E' AND (RESSEQ 6:46)
21X-RAY DIFFRACTION21CHAIN 'E' AND (RESSEQ 47:140)
22X-RAY DIFFRACTION22CHAIN 'F' AND (RESSEQ 1:66)
23X-RAY DIFFRACTION23CHAIN 'F' AND (RESSEQ 67:198)
24X-RAY DIFFRACTION24CHAIN 'F' AND (RESSEQ 199:362)

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