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- PDB-5m7e: Tubulin-BKM120 complex -

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Basic information

Entry
Database: PDB / ID: 5m7e
TitleTubulin-BKM120 complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-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 / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / 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 / cellular response to interleukin-4 / tubulin binding / 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 / cytoplasm / cytosol
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Helix hairpin bin / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site / Stathmin superfamily ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Helix hairpin bin / 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 / 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; / 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. / Dna Ligase; domain 1 / 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 / Chem-SD5 / 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: 2.046 Å
AuthorsBohnacker, T. / Prota, A.E. / Steinmetz, M.O. / Wymann, M.P.
Funding support Switzerland, Spain, United Kingdom, 6items
OrganizationGrant numberCountry
Swiss Commission for Technology and Innovation (CTI)14032.1 ; 15811.2 ; 17241.1 Switzerland
Stiftung fuer Krebsbekaempfung341 Switzerland
Swiss National Science Foundation310030_153211 ; 316030_133860 ; 310030B_138659; 31003A_166608 ; Switzerland
Spanish Ministry of Economy and CompetitivenessBIO2013-42984-R Spain
Comunidad Autonoma de MadridS2010/BMD-2457 BIPEDD2 Spain
Medical Research Council (United Kingdom)U105184308 United Kingdom
CitationJournal: Nat Commun / Year: 2017
Title: Deconvolution of Buparlisib's mechanism of action defines specific PI3K and tubulin inhibitors for therapeutic intervention.
Authors: Bohnacker, T. / Prota, A.E. / Beaufils, F. / Burke, J.E. / Melone, A. / Inglis, A.J. / Rageot, D. / Sele, A.M. / Cmiljanovic, V. / Cmiljanovic, N. / Bargsten, K. / Aher, A. / Akhmanova, A. / ...Authors: Bohnacker, T. / Prota, A.E. / Beaufils, F. / Burke, J.E. / Melone, A. / Inglis, A.J. / Rageot, D. / Sele, A.M. / Cmiljanovic, V. / Cmiljanovic, N. / Bargsten, K. / Aher, A. / Akhmanova, A. / Diaz, J.F. / Fabbro, D. / Zvelebil, M. / Williams, R.L. / Steinmetz, M.O. / Wymann, M.P.
History
DepositionOct 27, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 22, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 22, 2017Group: Database references / Structure summary
Revision 1.2Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
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.ptnr3_symmetry / _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 / _struct_conn.ptnr2_symmetry

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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)265,19324
Polymers261,6316
Non-polymers3,56218
Water12,268681
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23040 Å2
ΔGint-146 kcal/mol
Surface area80280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.593, 157.985, 179.728
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 (domestic 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 (domestic 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


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, 699 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.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#9: 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
#10: 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
#11: Chemical ChemComp-SD5 / 5-[2,6-di(morpholin-4-yl)pyrimidin-4-yl]-4-(trifluoromethyl)pyridin-2-amine


Mass: 410.394 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H21F3N6O2
#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


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: 2.84 Å3/Da / Density % sol: 56.66 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 3% PEG 4000, 4-6% GLYCEROL, 30 MM MAGNESIUM CHLORIDE, 30 MM CALCIUM CHLORIDE, 100 MM MES/IMIDAZOLE

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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: Feb 20, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.046→44.932 Å / Num. obs: 187079 / % possible obs: 99.8 % / Redundancy: 7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.109 / Net I/σ(I): 12.5
Reflection shellResolution: 2.05→2.1 Å / Redundancy: 7 % / Rmerge(I) obs: 1.821 / Mean I/σ(I) obs: 12.5 / CC1/2: 0.359 / % possible all: 98.7

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.046→44.932 Å / SU ML: 0.24 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 21.09
RfactorNum. reflection% reflection
Rfree0.2028 9355 5 %
Rwork0.1734 --
obs0.1749 187079 99.82 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.046→44.932 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17163 0 218 681 18062
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717789
X-RAY DIFFRACTIONf_angle_d0.8824120
X-RAY DIFFRACTIONf_dihedral_angle_d16.2910651
X-RAY DIFFRACTIONf_chiral_restr0.0522629
X-RAY DIFFRACTIONf_plane_restr0.0053115
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0461-2.06940.3242940.30975578X-RAY DIFFRACTION95
2.0694-2.09370.30863100.28015883X-RAY DIFFRACTION100
2.0937-2.11930.28973090.2665887X-RAY DIFFRACTION100
2.1193-2.14610.29693080.25275842X-RAY DIFFRACTION100
2.1461-2.17430.28233110.24735918X-RAY DIFFRACTION100
2.1743-2.20410.28963090.23855868X-RAY DIFFRACTION100
2.2041-2.23560.25193090.22795869X-RAY DIFFRACTION100
2.2356-2.2690.26083100.22155884X-RAY DIFFRACTION100
2.269-2.30440.25693100.21415903X-RAY DIFFRACTION100
2.3044-2.34220.26873100.21375889X-RAY DIFFRACTION100
2.3422-2.38260.23643090.19835873X-RAY DIFFRACTION100
2.3826-2.42590.233120.19595927X-RAY DIFFRACTION100
2.4259-2.47260.2313100.18525887X-RAY DIFFRACTION100
2.4726-2.5230.23163100.19545884X-RAY DIFFRACTION100
2.523-2.57790.23233110.1885913X-RAY DIFFRACTION100
2.5779-2.63780.23923130.18315935X-RAY DIFFRACTION100
2.6378-2.70380.23463100.18565891X-RAY DIFFRACTION100
2.7038-2.77690.21753110.19025913X-RAY DIFFRACTION100
2.7769-2.85860.2473110.1925909X-RAY DIFFRACTION100
2.8586-2.95080.22493120.19275935X-RAY DIFFRACTION100
2.9508-3.05630.22023130.18135945X-RAY DIFFRACTION100
3.0563-3.17860.21863130.17425936X-RAY DIFFRACTION100
3.1786-3.32320.20923120.17765947X-RAY DIFFRACTION100
3.3232-3.49840.21513140.1715956X-RAY DIFFRACTION100
3.4984-3.71750.17363130.15835945X-RAY DIFFRACTION100
3.7175-4.00430.16983150.14715995X-RAY DIFFRACTION100
4.0043-4.4070.15653170.13666014X-RAY DIFFRACTION100
4.407-5.0440.14413170.12896025X-RAY DIFFRACTION100
5.044-6.3520.20293200.17146085X-RAY DIFFRACTION100
6.352-44.94280.1773320.16226288X-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)
11.5885-0.2506-0.24244.57191.49223.04090.02770.15150.2532-0.43650.2712-0.4481-0.73690.4365-0.27110.4881-0.13240.11650.43-0.13110.375331.646788.203251.6803
21.5621-0.4739-0.41673.4871.22943.40440.0356-0.05580.04580.3807-0.04110.2854-0.1633-0.1015-0.00510.3812-0.02140.0610.295-0.08380.34919.126282.367765.7314
30.924-0.84030.10535.74841.94042.8888-0.0575-0.22870.09640.84690.04910.2057-0.1218-0.09240.01410.4516-0.05410.12180.3931-0.07150.374718.872983.293273.3164
41.5560.3117-0.2823.55723.55329.1682-0.0222-0.0496-0.25570.65280.3096-0.41110.62820.9299-0.27040.42340.1224-0.06260.4012-0.13520.45332.878861.869560.6432
55.6994-2.7763-0.97649.55712.65784.75860.19150.32210.6228-0.6452-0.25950.2739-1.0024-0.26270.08510.44760.01470.01540.3637-0.00530.402416.050869.764719.3046
61.9264-0.5998-0.24036.61970.57092.95050.05060.4906-0.029-0.55280.0502-0.4811-0.47290.3508-0.14370.3104-0.05850.04410.5209-0.05370.326229.11256.183714.5993
72.32161.51030.64846.42312.39774.0006-0.0113-0.13930.24510.04350.029-0.1038-0.20570.1874-0.02650.20070.01070.04170.3522-0.11670.310324.514853.06426.1627
87.0799-0.57971.97740.8972-1.07161.70380.0382-0.5983-0.21560.1791-0.2040.58390.2476-1.00480.25370.3539-0.07990.08940.7206-0.27350.53755.418750.740728.3155
91.936-0.67280.4811.69060.88623.0599-0.0407-0.33320.17060.0551-0.08670.3646-0.3509-0.65340.15940.33720.01860.0640.4689-0.15950.470910.240761.875735.8743
104.264-0.93331.1832.1019-0.68183.0936-0.3627-0.30140.11590.40.06730.4579-0.2359-1.32490.3120.44580.04840.0910.7478-0.21550.48456.30360.271844.8506
111.3373-2.1586-1.58184.87524.63624.7744-0.0509-0.1129-0.04350.8245-0.18740.50030.7197-0.14350.20550.3641-0.08110.06530.4119-0.11280.354215.579841.836134.2343
122.2209-0.6726-0.61165.40964.60318.98940.0451-0.4617-0.28420.94220.0827-0.23670.97160.635-0.13370.3765-0.0271-0.07170.3882-0.01260.360925.897137.847530.9491
131.3921-0.53930.09273.12540.03271.6175-0.03890.16570.1422-0.28250.0867-0.1355-0.15830.1764-0.04190.254-0.06660.04380.315-0.03570.268720.383433.1002-12.0807
140.8456-0.66260.08591.81480.90581.6132-0.0247-0.0524-0.02710.1188-0.05770.21440.0992-0.27440.08820.2166-0.0650.04020.2758-0.03330.29217.993125.97323.0895
154.6381-2.1922-0.03585.85661.02252.66420.02340.85110.0594-0.99220.01520.01820.0238-0.2263-0.0450.5559-0.12210.050.7113-0.02060.293517.38019.8159-44.3766
161.5491-0.0274-0.42041.65860.30222.3644-0.110.4822-0.2182-0.39790.1336-0.13910.2798-0.051-0.03680.4809-0.05210.05250.5159-0.16410.352620.4763-2.1429-34.0084
172.1563-0.0762-0.87721.73120.38432.8178-0.15730.4506-0.3996-0.20470.09730.19110.3329-0.3340.05430.4115-0.08110.02870.4153-0.11970.33679.2021-3.8127-21.4853
184.6366-0.8898-3.22873.12151.21896.4702-0.24260.1024-0.6571-0.02360.2274-0.38650.85030.74940.08430.60480.09410.01350.4391-0.22750.631730.6349-16.2792-24.4981
193.1844-2.08350.5895.36540.45930.7179-0.09-0.47830.06621.38360.3392-0.46350.07510.4678-0.24210.9803-0.0733-0.04450.5865-0.15770.571527.353792.835281.806
200.2084-0.1265-0.20352.38592.39583.0541-0.0249-0.0244-0.04770.08010.754-0.75030.23120.9363-0.70520.31850.04290.03970.6901-0.27310.646543.161827.8283.844
213.70842.4585-0.77456.48561.72973.5144-0.56710.5765-0.8403-0.32870.1222-0.13541.5426-0.27660.40980.8868-0.12820.20870.4661-0.14440.49356.373354.600569.9
223.29140.46070.0282.8642-1.1184.1921-0.1028-1.0049-0.59680.6534-0.5017-0.79760.54321.84040.58510.73590.2307-0.02561.1130.25760.670913.995658.593104.5444
233.22910.5833-2.40751.7474-0.34584.8576-0.5112-0.0977-0.78470.13720.1792-0.05521.0619-0.09940.18170.70510.04830.13710.28720.05360.5328-2.032554.604193.0975
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 438)
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 144)
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 384)

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