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- PDB-5m8d: Tubulin MTD265-R1 complex -

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Basic information

Entry
Database: PDB / ID: 5m8d
TitleTubulin MTD265-R1 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 / 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 / Dna Ligase; domain 1 / 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-UGI / 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: 2.25 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 28, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 22, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Jan 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)265,07324
Polymers261,6316
Non-polymers3,44218
Water9,602533
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22720 Å2
ΔGint-165 kcal/mol
Surface area80700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.180, 157.020, 179.980
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 , 9 types, 551 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.: 5 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#9: Chemical ChemComp-UGI / 5-(6-morpholin-4-yl-2-pyrrolidin-1-yl-pyrimidin-4-yl)-4-(trifluoromethyl)pyridin-2-amine


Mass: 394.394 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H21F3N6O
#10: 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
#11: 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
#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.: 533 / 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: 2.81 Å3/Da / Density % sol: 56.28 %
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: 1.00003 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Jul 8, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2.25→68.101 Å / Num. obs: 139439 / % possible obs: 99.5 % / Redundancy: 13.4 % / CC1/2: 0.999 / Rmerge(I) obs: 0.117 / Net I/σ(I): 17
Reflection shellResolution: 2.25→2.31 Å / Redundancy: 11.6 % / Rmerge(I) obs: 1.844 / Mean I/σ(I) obs: 1.4 / Num. measured obs: 9900 / CC1/2: 0.539 / % possible all: 96

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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: 2.25→68.101 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 22.31
RfactorNum. reflection% reflection
Rfree0.2099 6885 4.94 %
Rwork0.1695 --
obs0.1715 139439 99.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.25→68.101 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17363 0 207 533 18103
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00717947
X-RAY DIFFRACTIONf_angle_d0.89624327
X-RAY DIFFRACTIONf_dihedral_angle_d16.81710734
X-RAY DIFFRACTIONf_chiral_restr0.0522643
X-RAY DIFFRACTIONf_plane_restr0.0053151
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.25-2.27560.332460.29824150X-RAY DIFFRACTION95
2.2756-2.30230.30512180.26874251X-RAY DIFFRACTION97
2.3023-2.33040.28862230.25894318X-RAY DIFFRACTION98
2.3304-2.35990.30282290.264259X-RAY DIFFRACTION98
2.3599-2.3910.29812410.24974378X-RAY DIFFRACTION99
2.391-2.42370.30372150.24644371X-RAY DIFFRACTION99
2.4237-2.45840.28222220.22494419X-RAY DIFFRACTION100
2.4584-2.49510.30792010.2294385X-RAY DIFFRACTION99
2.4951-2.5340.26232260.22744452X-RAY DIFFRACTION100
2.534-2.57560.27182080.21624374X-RAY DIFFRACTION100
2.5756-2.620.2642390.21124385X-RAY DIFFRACTION100
2.62-2.66760.27612260.20844412X-RAY DIFFRACTION100
2.6676-2.7190.25042130.20014396X-RAY DIFFRACTION100
2.719-2.77450.26262520.19834395X-RAY DIFFRACTION100
2.7745-2.83480.23622430.18334382X-RAY DIFFRACTION100
2.8348-2.90070.24082460.18514434X-RAY DIFFRACTION100
2.9007-2.97330.23942350.18854380X-RAY DIFFRACTION100
2.9733-3.05370.22082320.18294422X-RAY DIFFRACTION100
3.0537-3.14350.21082130.16814483X-RAY DIFFRACTION100
3.1435-3.2450.23742270.17634406X-RAY DIFFRACTION100
3.245-3.3610.21762380.17354452X-RAY DIFFRACTION100
3.361-3.49550.20162210.16164432X-RAY DIFFRACTION100
3.4955-3.65460.19232180.15764462X-RAY DIFFRACTION100
3.6546-3.84730.18722050.15044508X-RAY DIFFRACTION100
3.8473-4.08830.18172420.14364448X-RAY DIFFRACTION100
4.0883-4.40390.18212380.13344479X-RAY DIFFRACTION100
4.4039-4.84690.15112470.12254481X-RAY DIFFRACTION100
4.8469-5.5480.16432450.14344526X-RAY DIFFRACTION100
5.548-6.98880.22462250.17284574X-RAY DIFFRACTION100
6.9888-68.13240.18292510.15664740X-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)
11.4348-0.4374-0.42244.38291.49632.99430.03320.13080.2308-0.47270.2959-0.4555-0.74520.4376-0.30260.5292-0.14040.11290.4937-0.15450.432931.624587.853851.7486
21.7449-0.0573-0.04613.48771.16623.47030.01920.00050.09070.36490.00470.2241-0.212-0.0433-0.05240.39770.01040.07020.3293-0.09720.371619.180981.928165.7957
30.8177-0.47620.18855.21842.05483.5618-0.0806-0.22520.13770.88420.08190.1794-0.1589-0.0502-0.01970.472-0.02370.12540.4215-0.0960.417718.92282.733773.3699
41.2892-0.2221-0.44363.83672.77472.1661-0.0787-0.0024-0.21370.66960.4095-0.40970.62240.9508-0.40030.44380.1301-0.08150.4571-0.17140.488732.814261.502760.466
55.9449-2.8298-1.17728.41992.27184.42680.26860.31730.7058-0.6477-0.24550.199-1.0184-0.26950.05070.48670.04470.0040.3911-0.0180.444615.98769.557719.1495
62.7821-0.8852-1.40767.80590.48553.75590.16250.41630.1232-0.53480.0015-0.4192-0.51820.2846-0.18780.36-0.05220.04660.5533-0.08880.354428.997956.005914.479
72.35711.71930.57886.17162.54283.6835-0.0553-0.16510.18890.00260.0493-0.0229-0.23040.1643-0.00550.24870.02240.03480.379-0.1270.366424.385552.895526.0261
84.0596-1.71970.90341.89-1.76722.18140.0053-0.4836-0.1930.139-0.21040.74410.4326-1.11310.24350.3668-0.09960.08880.7765-0.3140.56495.4150.476328.2315
91.7826-0.81630.14991.50810.85393.4903-0.0399-0.15430.119-0.061-0.05910.2604-0.3424-0.56770.10530.35630.0320.03270.448-0.14960.47869.928361.609235.6791
103.7327-0.67361.16481.2561-0.96472.3533-0.3711-0.30880.13090.39820.09190.2776-0.3876-1.13940.24520.51060.12040.06080.7209-0.20560.51936.325860.23944.6504
110.8985-2.3005-1.11586.34184.67174.6702-0.0554-0.0697-0.08870.6004-0.05040.42370.6347-0.2450.18710.3252-0.05450.05790.3838-0.10670.374515.453441.749634.0408
122.1292-1.0433-1.31815.26943.91573.4388-0.2034-0.3728-0.30360.96960.1718-0.0831.32340.7989-0.06890.40980.0044-0.06660.4437-0.02440.393425.696337.804630.9186
131.4109-0.44910.01922.78440.19831.7115-0.02930.16270.1331-0.28590.0894-0.0935-0.19230.1317-0.05120.2922-0.07750.04080.3601-0.04120.295220.191732.7698-12.0794
140.9988-0.43520.05571.62170.99331.7984-0.0089-0.05120.05610.0963-0.08740.16670.0832-0.27340.09320.2495-0.06420.03750.3029-0.03730.32027.914625.67623.1192
155.1442-2.1894-0.99375.36291.76623.9357-0.00941.04960.1922-0.89380.0923-0.0137-0.1571-0.2324-0.03820.6116-0.14370.05210.8045-0.03250.315317.28919.2419-44.2753
161.91540.1978-0.69951.48510.29442.7858-0.12310.506-0.2029-0.3690.156-0.14820.2854-0.0584-0.0560.5668-0.05770.05980.5713-0.19990.408720.375-2.5577-33.816
172.6203-0.3586-0.57632.27270.68062.8552-0.25590.3808-0.34670.06750.15230.24170.4469-0.37350.11020.4964-0.11510.04690.4759-0.11960.35329.1264-4.1465-21.2959
184.4088-0.7087-2.04163.49570.62343.8807-0.39610.0858-0.71150.19450.1498-0.24331.04010.67810.05910.72860.09150.03040.5327-0.24230.666230.482-16.617-24.1689
193.8385-2.842-0.16976.09951.02040.4748-0.114-0.4840.19251.41080.5938-0.69620.07580.5526-0.40121.0951-0.0762-0.07950.7068-0.21520.613527.501392.190681.949
200.43650.1027-0.00050.79560.80831.3567-0.0425-0.0343-0.01110.29620.561-0.54710.47640.7748-0.76970.41270.06110.02650.7055-0.24420.642143.044327.76214.0704
213.3041.4682-1.67846.09171.35583.719-0.62980.5566-0.762-0.3090.2378-0.20571.3631-0.39340.23771.0408-0.12680.18690.5673-0.14810.58146.288454.222569.6874
223.35960.5187-0.10093.0858-1.35154.012-0.0653-1.0014-0.7490.471-0.516-0.85180.64211.88550.50180.90550.2819-0.03151.28040.29970.806514.969656.9329104.8595
232.97450.6675-2.40271.3866-0.12633.2305-0.5429-0.16-0.77210.17710.2713-0.09681.088-0.01690.02040.97050.07190.16010.4060.08910.6643-1.585753.873493.2391
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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