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- PDB-5m7g: Tubulin-MTD147 complex -

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Basic information

Entry
Database: PDB / ID: 5m7g
TitleTubulin-MTD147 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 / 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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / Chem-FB7 / 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: 2.248 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
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.ptnr1_symmetry / _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.ptnr1_symmetry / _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)265,58926
Polymers261,6316
Non-polymers3,95820
Water7,584421
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22860 Å2
ΔGint-177 kcal/mol
Surface area79560 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.083, 156.864, 179.684
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


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, 441 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.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#9: Chemical ChemComp-FB7 / 5-(2,6-dimorpholin-4-ylpyridin-4-yl)-4-(trifluoromethyl)pyridin-2-amine / MBT147


Mass: 409.405 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H22F3N5O2
#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.: 421 / 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: 2.8 Å3/Da / Density % sol: 56.12 %
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: 2.248→46.723 Å / Num. obs: 138844 / % possible obs: 99.1 % / Redundancy: 6.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.105 / Net I/σ(I): 15.8
Reflection shellResolution: 2.25→2.38 Å / Redundancy: 6.5 % / Rmerge(I) obs: 1.803 / Mean I/σ(I) obs: 1 / CC1/2: 0.335 / % possible all: 96.5

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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: 2.248→46.723 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 23.74
RfactorNum. reflection% reflection
Rfree0.2168 6942 5 %
Rwork0.1723 --
obs0.1745 138844 99.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.248→46.723 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17116 0 243 421 17780
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00817731
X-RAY DIFFRACTIONf_angle_d0.9124036
X-RAY DIFFRACTIONf_dihedral_angle_d16.42310592
X-RAY DIFFRACTIONf_chiral_restr0.0522615
X-RAY DIFFRACTIONf_plane_restr0.0053099
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2476-2.27310.35591990.34153782X-RAY DIFFRACTION86
2.2731-2.29990.35992310.30594378X-RAY DIFFRACTION100
2.2999-2.32790.33042290.29544358X-RAY DIFFRACTION99
2.3279-2.35740.32142290.28724351X-RAY DIFFRACTION99
2.3574-2.38840.30562300.27674362X-RAY DIFFRACTION99
2.3884-2.42110.28482270.26674321X-RAY DIFFRACTION99
2.4211-2.45570.31962320.26044403X-RAY DIFFRACTION100
2.4557-2.49230.30082280.26064339X-RAY DIFFRACTION99
2.4923-2.53130.31062330.24224419X-RAY DIFFRACTION99
2.5313-2.57280.24442280.22744342X-RAY DIFFRACTION99
2.5728-2.61710.292300.22774365X-RAY DIFFRACTION99
2.6171-2.66470.28642310.23074396X-RAY DIFFRACTION100
2.6647-2.7160.28682290.22424353X-RAY DIFFRACTION100
2.716-2.77140.25722330.20844417X-RAY DIFFRACTION99
2.7714-2.83170.24452300.19584367X-RAY DIFFRACTION99
2.8317-2.89750.26742330.18844423X-RAY DIFFRACTION100
2.8975-2.970.22132300.1844377X-RAY DIFFRACTION100
2.97-3.05030.23292330.17724428X-RAY DIFFRACTION100
3.0503-3.140.23372330.17754434X-RAY DIFFRACTION100
3.14-3.24130.2322310.18344389X-RAY DIFFRACTION100
3.2413-3.35710.22482340.17534436X-RAY DIFFRACTION100
3.3571-3.49150.23452320.1684414X-RAY DIFFRACTION100
3.4915-3.65040.22262330.16194433X-RAY DIFFRACTION100
3.6504-3.84270.1982360.154470X-RAY DIFFRACTION100
3.8427-4.08340.18272330.14114439X-RAY DIFFRACTION100
4.0834-4.39840.17222360.12964474X-RAY DIFFRACTION100
4.3984-4.84060.14952360.11864481X-RAY DIFFRACTION100
4.8406-5.54010.19542370.14434517X-RAY DIFFRACTION100
5.5401-6.97620.2032400.17014541X-RAY DIFFRACTION100
6.9762-46.73350.17822460.15284693X-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)
11.5-0.4317-0.53724.65911.41373.07370.03390.070.2795-0.41360.2904-0.4694-0.72220.4414-0.28730.544-0.14560.10920.4936-0.16010.455931.494787.62951.7155
21.2694-0.3793-0.12883.36621.06183.17430.0883-0.01210.01430.3565-0.06980.325-0.1907-0.0954-0.02070.4511-0.00690.07990.3754-0.10360.45119.06981.711265.7864
31.075-0.89510.0255.77112.16252.9421-0.1143-0.24890.1120.97420.15910.1943-0.07090.0059-0.03870.5387-0.00940.15860.446-0.09060.459818.831982.559373.3761
42.2368-0.2385-0.81153.41012.75176.9367-0.0161-0.0442-0.19760.60110.3547-0.32070.39120.917-0.38290.45810.1096-0.06680.4256-0.13780.516332.84761.34260.546
56.0442-2.5622-1.31245.05631.52184.93590.23890.33850.6021-0.5244-0.23940.1599-0.935-0.33190.06340.4580.02630.00010.3750.00560.428615.934269.416219.2539
62.2406-0.6494-1.03887.32820.38882.92690.1530.44420.0964-0.4703-0.0958-0.3501-0.38850.2565-0.10320.3629-0.05860.04290.5965-0.06950.383129.034755.904114.5744
72.43432.21320.35447.52132.47094.0611-0.0127-0.16290.1316-0.00680.0762-0.1448-0.19630.1719-0.05430.23460.02490.03710.3832-0.12410.362224.483452.750626.1019
81.4825-1.23480.52951.9478-1.7942.2424-0.0584-0.5294-0.3477-0.0934-0.11670.55230.3226-1.23170.20190.4059-0.09360.09750.9093-0.32620.59745.435850.308228.2632
92.5574-1.22330.07012.24280.77923.288-0.0214-0.23740.15630.0365-0.12740.3372-0.2892-0.73970.10340.35790.00520.05750.5456-0.16590.491910.339661.49635.9341
103.9131-0.26191.08532.0557-1.5193.4769-0.3054-0.31660.11530.29630.18190.3715-0.2961-1.12230.1320.47440.04960.09770.7793-0.20010.5436.211659.860944.7689
111.6276-2.5643-2.83924.78465.87437.1495-0.1438-0.1842-0.00381.0082-0.1750.53210.8769-0.17260.34360.3317-0.09370.04240.4213-0.08620.396815.637741.457934.1338
122.3431-1.1956-1.42526.55035.18016.8258-0.0483-0.3685-0.22611.01610.2079-0.18811.1820.5276-0.19240.4082-0.0154-0.09260.42930.00280.416625.872537.52730.9066
131.3257-0.7832-0.16353.32910.21371.5657-0.0210.12790.1974-0.26770.1158-0.1613-0.23710.1303-0.09330.3005-0.08410.03570.3754-0.04450.32520.35332.721-12.0641
141.1266-0.46350.02491.70261.11161.7804-0.026-0.02180.05270.1152-0.06640.15960.0853-0.250.08890.2687-0.08120.04710.3189-0.04430.33048.035825.60753.069
156.1752-3.1683-1.00946.52231.42162.70240.20321.08040.164-0.8722-0.09350.0833-0.1308-0.2906-0.10910.6096-0.12420.05920.8012-0.02150.320717.42039.3913-44.3556
162.0488-0.1083-0.31931.74280.20942.6403-0.13680.4987-0.2283-0.36130.1937-0.21070.34140.0069-0.04630.5688-0.05540.07970.6315-0.21360.436221.3633-2.6856-33.9886
172.6032-0.1119-0.5891.7123-0.19423.6834-0.18590.4072-0.459-0.15720.21830.21440.3033-0.53620.00280.4575-0.10380.03730.4668-0.12970.44279.2569-4.2177-21.3502
184.6494-1.629-3.48643.44121.90095.4599-0.31780.0473-0.66050.2040.3059-0.43041.23690.7382-0.11660.7140.07550.0650.6039-0.29450.770530.6735-16.5463-24.2289
193.3709-2.45140.62936.98550.78840.5316-0.1375-0.2820.31131.57030.2328-0.5361-0.1530.3381-0.13981.1136-0.0982-0.00710.7064-0.25920.698627.406792.116181.8781
200.3932-0.2732-0.39680.12230.22340.7253-0.0739-0.0376-0.03740.2120.4748-0.43860.39160.6838-0.53890.46330.05380.03760.737-0.25180.691143.214127.67914.0333
213.92091.9104-1.06246.0210.89524.1875-0.60550.4392-0.9251-0.24780.121-0.13271.7447-0.27440.32631.0376-0.12710.25470.5479-0.14240.60486.267254.003869.7725
223.18290.222-0.14692.4386-0.6154.0884-0.2821-1.0294-0.86440.4089-0.3567-0.74350.54861.68590.58840.81590.26320.03021.22890.33540.815214.169856.904103.7718
233.16990.6481-2.24791.0533-0.3913.4007-0.5713-0.1415-0.86870.09620.1984-0.08131.277-0.05870.1360.95840.04340.18760.43470.08490.6896-2.22853.73792.8239
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 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 379)

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