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- PDB-5osk: Tubulin-7j complex -

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Basic information

Entry
Database: PDB / ID: 5osk
TitleTubulin-7j complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine Ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE QUINAZOLINONES
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 / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / neuron projection development / 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 / cytoplasm / cytosol
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 / Tubulin/FtsZ, GTPase domain / Tubulin/FtsZ, GTPase domain superfamily / Dna Ligase; domain 1 / 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-A9Q / 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 / FOURIER SYNTHESIS / Resolution: 2.11 Å
AuthorsMenchon, G. / Prota, A.E. / Steinmetz, M.O. / Potter, B.V.L.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
CitationJournal: J. Med. Chem. / Year: 2018
Title: Quinazolinone-Based Anticancer Agents: Synthesis, Antiproliferative SAR, Antitubulin Activity, and Tubulin Co-crystal Structure.
Authors: Dohle, W. / Jourdan, F.L. / Menchon, G. / Prota, A.E. / Foster, P.A. / Mannion, P. / Hamel, E. / Thomas, M.P. / Kasprzyk, P.G. / Ferrandis, E. / Steinmetz, M.O. / Leese, M.P. / Potter, B.V.L.
History
DepositionAug 17, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 20, 2017Provider: repository / Type: Initial release
Revision 1.1Jan 17, 2018Group: Database references / Category: citation / Item: _citation.title / _citation.year
Revision 1.2Feb 21, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 17, 2024Group: 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)265,63228
Polymers261,6316
Non-polymers4,00122
Water15,205844
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24430 Å2
ΔGint-135 kcal/mol
Surface area81680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.670, 159.920, 181.010
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) / Tissue: 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) / Tissue: 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


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, 866 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-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C3H8O3
#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-A9Q / 3-(2,5-Dimethoxybenzyl)-7-sulfamoyloxy-6-methoxy-3,4-dihydroquinazolin-2(1H)-one


Mass: 423.440 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H21N3O7S
#11: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Ca
#12: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H5N2
#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


Mass: 18.015 Da / Num. of mol.: 844 / 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: 2.92 Å3/Da / Density % sol: 57.92 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 10% PEG 4K, 16% glycerol, 30 mM MgCl2, 30 mM CaCl2, and 100 mM MES/Imidazole (pH 6.7)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jun 9, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→49.8 Å / Num. obs: 172614 / % possible obs: 99.9 % / Redundancy: 6.7 % / CC1/2: 1 / Rsym value: 0.06 / Net I/σ(I): 19.5
Reflection shellResolution: 2.1→2.16 Å / Redundancy: 6.6 % / Mean I/σ(I) obs: 1.02 / Num. unique obs: 12620 / CC1/2: 0.394 / Rsym value: 2.003 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5LXT

5lxt


Resolution: 2.11→49.792 Å / SU ML: 0.28 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 26.88 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.232 8557 4.96 %RANDOM
Rwork0.1951 ---
obs0.1969 172604 97.93 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.11→49.792 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17080 0 250 844 18174
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717837
X-RAY DIFFRACTIONf_angle_d0.85824186
X-RAY DIFFRACTIONf_dihedral_angle_d11.22310677
X-RAY DIFFRACTIONf_chiral_restr0.0532626
X-RAY DIFFRACTIONf_plane_restr0.0063129
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1095-2.13350.39121240.36372125X-RAY DIFFRACTION39
2.1335-2.15860.37372680.32445527X-RAY DIFFRACTION99
2.1586-2.18490.33623040.32255488X-RAY DIFFRACTION100
2.1849-2.21260.34612870.31735531X-RAY DIFFRACTION100
2.2126-2.24170.32682780.29895509X-RAY DIFFRACTION100
2.2417-2.27240.32952810.29015528X-RAY DIFFRACTION100
2.2724-2.30490.33172530.28085618X-RAY DIFFRACTION100
2.3049-2.33930.32643020.2755527X-RAY DIFFRACTION100
2.3393-2.37580.3082700.26185531X-RAY DIFFRACTION100
2.3758-2.41480.28182690.26775577X-RAY DIFFRACTION100
2.4148-2.45640.29932770.25515550X-RAY DIFFRACTION100
2.4564-2.50110.29122850.24085540X-RAY DIFFRACTION100
2.5011-2.54920.2932840.23885568X-RAY DIFFRACTION100
2.5492-2.60120.2672810.23195536X-RAY DIFFRACTION100
2.6012-2.65780.26913370.22235542X-RAY DIFFRACTION100
2.6578-2.71960.262980.22685536X-RAY DIFFRACTION100
2.7196-2.78760.28453110.22715550X-RAY DIFFRACTION100
2.7876-2.8630.28222720.22775588X-RAY DIFFRACTION100
2.863-2.94720.25823220.22485536X-RAY DIFFRACTION100
2.9472-3.04230.26432710.22685575X-RAY DIFFRACTION100
3.0423-3.1510.27843150.21285546X-RAY DIFFRACTION100
3.151-3.27720.25762910.20885606X-RAY DIFFRACTION100
3.2772-3.42630.24793210.19735569X-RAY DIFFRACTION100
3.4263-3.60690.22913100.18865567X-RAY DIFFRACTION100
3.6069-3.83280.19652770.17335638X-RAY DIFFRACTION100
3.8328-4.12860.1952830.15595628X-RAY DIFFRACTION100
4.1286-4.54380.18332930.14385667X-RAY DIFFRACTION100
4.5438-5.20070.18212840.14185677X-RAY DIFFRACTION100
5.2007-6.550.21613030.18315733X-RAY DIFFRACTION100
6.55-49.80610.19553060.18395934X-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)
11.5188-0.4194-0.54854.08851.44653.2083-0.02170.20260.2044-0.62480.4336-0.529-0.93030.5158-0.36910.6473-0.17770.14080.5927-0.1950.499532.141689.594652.1164
21.768-0.0236-0.25934.381.80974.28740.09790.05820.07430.33490.00090.255-0.2071-0.0431-0.12520.41920.03250.060.3704-0.09570.416319.726183.330866.1919
31.2075-0.1130.21215.7272.53754.215-0.0716-0.15510.12821.00220.0570.3984-0.0476-0.0795-0.02350.5082-0.01510.13240.4856-0.11060.47919.613184.508373.9233
41.8178-0.7065-0.12265.30513.02837.0579-0.13080.0082-0.11860.81440.4305-0.47340.89411.1958-0.30970.46090.1671-0.09090.5148-0.15850.587733.390862.725260.6496
55.882-2.2047-0.59548.33531.43374.72960.22270.23340.814-0.5503-0.13850.1886-1.0167-0.2179-0.03770.51740.0520.03970.38430.01590.479916.00770.924219.2126
62.0475-0.7131-1.26495.58240.88563.17960.26890.31740.1391-0.5253-0.0308-0.3798-0.4510.2862-0.23470.3958-0.00290.07080.5622-0.07350.427329.269257.120214.5453
71.99280.7497-0.0515.95271.99753.53560.0349-0.23740.1747-0.01550.0317-0.1926-0.13930.2205-0.04820.23440.02120.03830.3522-0.11860.343724.597653.939326.0373
86.5094-1.91640.10652.4966-1.57033.46480.0128-0.2576-0.57090.0066-0.13790.79260.6107-1.28980.12690.4005-0.08950.08930.767-0.28860.58865.463651.304128.4701
92.2244-0.74510.04782.17480.89043.60670.0455-0.07320.2099-0.0453-0.03810.1631-0.355-0.4672-0.00370.38560.04590.07410.4447-0.15160.472810.570362.76135.938
103.3071-0.86760.82812.7749-0.5693.9106-0.1461-0.2110.12080.51810.06410.4433-0.3724-0.9040.0440.57410.06740.14530.7238-0.18260.58046.486661.542545.0123
110.2274-1.3576-0.87166.31664.38953.813-0.0648-0.15330.02160.49640.02680.46740.4171-0.10290.01020.3958-0.01780.08610.4437-0.09930.401515.914741.912834.0016
121.8509-0.52250.13694.09721.94544.7062-0.0131-0.394-0.04610.73710.1058-0.03680.58910.285-0.07730.3794-0.04710.00540.4732-0.04860.39424.249842.202730.378
131.8073-0.7197-0.11873.36570.25872.3401-0.02610.24110.1125-0.34380.0676-0.0163-0.19250.1013-0.03250.3056-0.09060.0310.3778-0.03230.316420.358833.3907-11.9248
141.173-0.45970.11951.9080.93341.8402-0.0553-0.02020.09030.0846-0.04310.16150.0293-0.25540.09040.2474-0.06520.03360.311-0.03020.33557.887226.19883.282
154.6347-0.9143-0.8174.46361.42384.1646-0.27331.21910.2615-0.81210.4270.1154-0.0082-0.3074-0.08980.6865-0.2724-0.00051.0612-0.01340.409617.47389.4282-44.3571
161.94410.0041-0.04192.15020.18033.1484-0.20430.6925-0.3064-0.42020.2744-0.20.5034-0.0586-0.08950.6393-0.12470.07670.7331-0.25380.482721.4706-2.563-33.7055
173.1689-0.18290.28323.3487-0.46523.5242-0.20840.4685-0.3471-0.05910.32990.17620.4003-0.5215-0.06770.4904-0.18240.04480.5986-0.12470.42679.2154-4.2449-21.3539
185.3269-0.9607-2.38184.07150.29774.5723-0.2860.039-0.9450.16430.2263-0.53681.03240.7862-0.21110.88740.01790.04550.6281-0.28870.80430.9408-16.8621-24.2145
193.3752-1.4898-1.23938.206-0.94163.3156-0.0097-0.40230.02661.72460.27050.187-1.26951.3252-0.36340.9022-0.125-0.05510.9319-0.24230.603528.42793.891282.4553
200.522-0.6513-0.74971.41711.3061.9899-0.04860.0074-0.01120.15270.5527-0.49990.3210.7645-0.63980.44070.05450.04130.8102-0.25590.721943.531328.39534.1251
215.95292.6925-1.71148.00611.2486.9276-0.60510.8962-1.0449-0.08750.2552-0.23891.9172-0.71760.19571.1341-0.18840.19220.8012-0.18440.67486.366255.366570.0567
223.7360.14780.60023.9018-1.35525.3635-0.0524-1.1968-0.67350.6313-0.527-0.81620.25461.92890.53470.98290.2752-0.07721.40180.20120.876613.612959.8943105.949
233.68530.7144-2.5472.1473-0.57312.9914-0.56290.0144-0.95940.1640.2969-0.021.2068-0.17480.08471.11560.01620.16160.56330.04740.7674-2.331454.992193.2256
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 180)
2X-RAY DIFFRACTION2chain 'A' and (resid 181 through 311)
3X-RAY DIFFRACTION3chain 'A' and (resid 312 through 401)
4X-RAY DIFFRACTION4chain 'A' and (resid 402 through 436)
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 88)
6X-RAY DIFFRACTION6chain 'B' and (resid 89 through 127)
7X-RAY DIFFRACTION7chain 'B' and (resid 128 through 197)
8X-RAY DIFFRACTION8chain 'B' and (resid 198 through 223)
9X-RAY DIFFRACTION9chain 'B' and (resid 224 through 295)
10X-RAY DIFFRACTION10chain 'B' and (resid 296 through 373)
11X-RAY DIFFRACTION11chain 'B' and (resid 374 through 401)
12X-RAY DIFFRACTION12chain 'B' and (resid 402 through 437)
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 197)
14X-RAY DIFFRACTION14chain 'C' and (resid 198 through 440)
15X-RAY DIFFRACTION15chain 'D' and (resid 2 through 88)
16X-RAY DIFFRACTION16chain 'D' and (resid 89 through 295)
17X-RAY DIFFRACTION17chain 'D' and (resid 296 through 401)
18X-RAY DIFFRACTION18chain 'D' and (resid 402 through 441)
19X-RAY DIFFRACTION19chain 'E' and (resid 6 through 46)
20X-RAY DIFFRACTION20chain 'E' and (resid 47 through 143)
21X-RAY DIFFRACTION21chain 'F' and (resid 1 through 66)
22X-RAY DIFFRACTION22chain 'F' and (resid 67 through 198)
23X-RAY DIFFRACTION23chain 'F' and (resid 199 through 380)

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