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- PDB-6gf3: Tubulin-Jerantinine B acetate complex -

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Basic information

Entry
Database: PDB / ID: 6gf3
TitleTubulin-Jerantinine B acetate complex
Components
  • (Tubulin beta-2B ...) x 2
  • Stathmin-4
  • Tubulin alpha-1B 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
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 ...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. / 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 / 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 / Jerantinine B / 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: 2.4 Å
AuthorsSmedley, C.J. / Stanley, P.A. / Qazzaz, M.E. / Prota, A.E. / Olieric, N. / Collins, H. / Eastman, H. / Barrow, A.S. / Lim, K.-H. / Kam, T.-S. ...Smedley, C.J. / Stanley, P.A. / Qazzaz, M.E. / Prota, A.E. / Olieric, N. / Collins, H. / Eastman, H. / Barrow, A.S. / Lim, K.-H. / Kam, T.-S. / Smith, B.J. / Duivenvoorden, H.M. / Parker, B.S. / Bradshaw, T.D. / Steinmetz, M.O. / Moses, J.E.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
CitationJournal: Sci Rep / Year: 2018
Title: Sustainable Syntheses of (-)-Jerantinines A & E and Structural Characterisation of the Jerantinine-Tubulin Complex at the Colchicine Binding Site.
Authors: Smedley, C.J. / Stanley, P.A. / Qazzaz, M.E. / Prota, A.E. / Olieric, N. / Collins, H. / Eastman, H. / Barrow, A.S. / Lim, K.H. / Kam, T.S. / Smith, B.J. / Duivenvoorden, H.M. / Parker, B.S. ...Authors: Smedley, C.J. / Stanley, P.A. / Qazzaz, M.E. / Prota, A.E. / Olieric, N. / Collins, H. / Eastman, H. / Barrow, A.S. / Lim, K.H. / Kam, T.S. / Smith, B.J. / Duivenvoorden, H.M. / Parker, B.S. / Bradshaw, T.D. / Steinmetz, M.O. / Moses, J.E.
History
DepositionApr 29, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 8, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 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)265,12621
Polymers261,6176
Non-polymers3,50815
Water2,756153
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)104.720, 158.150, 180.950
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 , 3 types, 4 molecules ACEF

#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
#4: 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
#5: 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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Tubulin beta-2B ... , 2 types, 2 molecules BD

#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Tissue: brain / References: UniProt: Q6B856
#3: Protein Tubulin beta-2B chain


Mass: 49985.859 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / Tissue: brain / References: UniProt: Q6B856

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Non-polymers , 9 types, 168 molecules

#6: 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
#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Ca
#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.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-EX5 / Jerantinine B


Mass: 440.489 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C24H28N2O6
#12: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#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.: 153 / 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: 2.86 Å3/Da / Density % sol: 57.05 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 10% PEG 4K, 12% GLYCEROL, 30 MM REMARK 280 MGCL2, 30 MM CACL2, 100 MM MES/IMIDAZOLE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.99999 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 13, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99999 Å / Relative weight: 1
ReflectionResolution: 2.4→48 Å / Num. obs: 117441 / % possible obs: 99.7 % / Redundancy: 12.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.152 / Rrim(I) all: 0.159 / Net I/σ(I): 12.5
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 12.8 % / Rmerge(I) obs: 3.936 / Num. unique obs: 8572 / CC1/2: 0.204 / Rrim(I) all: 4.101 / % possible all: 99.6

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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: 4O2B

4o2b


Resolution: 2.4→47.958 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.4
RfactorNum. reflection% reflection
Rfree0.2507 5877 5.01 %
Rwork0.1983 --
obs0.2009 117393 99.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.4→47.958 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16810 0 217 153 17180
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00317556
X-RAY DIFFRACTIONf_angle_d0.55223853
X-RAY DIFFRACTIONf_dihedral_angle_d11.71610544
X-RAY DIFFRACTIONf_chiral_restr0.0422605
X-RAY DIFFRACTIONf_plane_restr0.0043085
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.42730.4112010.38983628X-RAY DIFFRACTION98
2.4273-2.45580.36921850.36283670X-RAY DIFFRACTION100
2.4558-2.48580.40471780.35733691X-RAY DIFFRACTION100
2.4858-2.51720.37522020.35073671X-RAY DIFFRACTION100
2.5172-2.55040.36731910.34583716X-RAY DIFFRACTION100
2.5504-2.58530.34922060.3193652X-RAY DIFFRACTION100
2.5853-2.62220.35382040.30263681X-RAY DIFFRACTION100
2.6222-2.66140.32852010.31043642X-RAY DIFFRACTION100
2.6614-2.7030.39291960.30893727X-RAY DIFFRACTION100
2.703-2.74730.32661970.30413705X-RAY DIFFRACTION100
2.7473-2.79460.34491980.29273656X-RAY DIFFRACTION100
2.7946-2.84540.31811970.27763687X-RAY DIFFRACTION100
2.8454-2.90020.32631980.26993691X-RAY DIFFRACTION100
2.9002-2.95940.30941830.283689X-RAY DIFFRACTION100
2.9594-3.02370.31891940.25373703X-RAY DIFFRACTION100
3.0237-3.0940.30192210.23523708X-RAY DIFFRACTION100
3.094-3.17140.25461890.22033729X-RAY DIFFRACTION100
3.1714-3.25710.28451930.22413691X-RAY DIFFRACTION100
3.2571-3.35290.28371940.21873718X-RAY DIFFRACTION100
3.3529-3.46110.27671990.20693715X-RAY DIFFRACTION100
3.4611-3.58480.26331960.20163735X-RAY DIFFRACTION100
3.5848-3.72830.23971890.18443740X-RAY DIFFRACTION100
3.7283-3.89790.20441920.17063731X-RAY DIFFRACTION100
3.8979-4.10330.22731750.16663748X-RAY DIFFRACTION100
4.1033-4.36020.22681960.15933758X-RAY DIFFRACTION99
4.3602-4.69660.16672140.14083731X-RAY DIFFRACTION100
4.6966-5.16870.21381790.14793775X-RAY DIFFRACTION100
5.1687-5.91550.2321910.1763805X-RAY DIFFRACTION100
5.9155-7.44840.22972210.18443797X-RAY DIFFRACTION99
7.4484-47.96710.21951970.16613926X-RAY DIFFRACTION98
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)
11.8613-0.2757-0.57794.34961.23823.2905-0.00740.2850.1439-0.80480.3725-0.5772-0.82970.5251-0.34830.7274-0.16050.17260.7033-0.21120.657332.027288.819251.9892
21.9446-0.4382-0.06964.9381.99865.46210.0126-0.05840.06290.28380.04160.1803-0.1771-0.1006-0.05420.45570.00380.05490.4741-0.07820.546719.626982.807466.0294
31.8338-0.2064-0.01575.49431.52283.2329-0.1285-0.21870.16051.00960.20880.2169-0.07820.1246-0.06970.6280.01740.11470.586-0.13990.582619.469983.817773.5743
43.9662-0.5923-0.04825.66963.44267.2918-0.2349-0.1421-0.45850.8790.4699-0.75261.42491.6165-0.24440.66050.139-0.11070.7157-0.2090.844432.975262.362660.2565
55.2128-1.7701-0.62344.64771.42494.74530.2610.25691.0322-0.6525-0.24750.2967-1.2194-0.4134-0.020.78870.08490.06410.4933-0.01790.74515.563570.089618.9016
63.4466-0.7988-0.81366.09310.46914.08710.4090.02510.293-0.4069-0.207-0.6995-1.00870.1758-0.170.7007-0.02090.14860.6539-0.03260.664228.677956.642514.4136
71.7492-0.14050.1934.93531.84144.40470.0979-0.24490.1074-0.0446-0.0146-0.2579-0.20060.1688-0.07670.2827-0.00050.0380.4012-0.10.447924.128153.650225.8801
86.8027-1.949-0.83742.6174-1.94733.2609-0.0094-0.318-0.4121-0.0674-0.08010.80410.4079-1.00650.16620.5008-0.02170.0350.7703-0.28650.65255.161451.067928.3088
92.7919-1.0147-0.08732.38230.48082.66510.09440.03190.2007-0.0736-0.15150.2352-0.3936-0.30940.04340.46420.06510.03470.5119-0.18530.589810.729262.219335.8366
104.06-1.82080.1943.0645-0.25122.9153-0.2245-0.21860.03840.4410.10190.2268-0.192-0.54860.10840.5350.04050.06780.7356-0.20210.59786.092561.077744.5562
111.4615-1.9939-1.40183.91423.35353.3866-0.0187-0.0274-0.17140.5626-0.26330.29180.5777-0.14370.36440.5501-0.0661-0.00630.6393-0.08460.561515.366942.538234.145
121.66950.16460.2025.39443.7582.5845-0.1067-0.1428-0.08120.88740.1657-0.26071.08210.8789-0.12640.50120.0411-0.06710.5356-0.01910.480525.709538.580531.0256
132.0155-1.05020.02524.4425-0.07542.3383-0.04290.35190.1101-0.45210.05570.0181-0.23750.107-0.00360.415-0.12470.02350.5103-0.03750.424719.856433.0996-11.8482
141.7212-0.48030.01591.98620.83882.1395-0.0521-0.02570.06410.0509-0.00970.14780.0005-0.21310.05860.3214-0.08050.02570.3908-0.03660.4087.521426.13383.3225
154.415-1.16910.12994.3309-0.19583.1905-0.24771.07220.3544-0.51280.4301-0.13650.1739-0.3783-0.13530.8965-0.299-0.01171.2155-0.01940.569716.97139.353-43.9494
161.92070.11540.25211.9595-0.11172.709-0.25330.784-0.3888-0.55550.2227-0.21680.4833-0.0255-0.00220.8493-0.18530.10470.898-0.25840.610821.0979-2.3656-33.3182
173.306-0.27150.83852.5794-0.69533.5522-0.24470.4538-0.1721-0.05670.18280.0740.474-0.55270.10390.6707-0.21470.05410.7414-0.14530.5588.8823-4.0113-20.9676
184.2465-1.5136-2.77293.02760.60645.9476-0.4305-0.0599-0.80740.31220.3077-0.14121.34120.7498-0.02291.12080.01540.07350.7051-0.30031.030430.3798-16.2638-23.7871
193.5803-0.489-0.33184.9959-0.28812.48550.0395-0.25820.08841.14330.0875-0.4959-0.68790.716-0.22731.216-0.108-0.08611.0577-0.21691.007828.44392.732682.1729
200.4276-0.5964-0.89790.25170.29540.7361-0.1436-0.10440.10290.4230.3392-0.15110.51430.6075-0.24170.6070.05530.01850.899-0.24420.786142.793329.10685.0293
214.24041.3583-2.22525.033-0.29765.0644-0.44260.7704-0.68410.13630.157-0.01961.5987-0.9650.26991.2497-0.1070.18491.092-0.24340.86276.30755.154269.6506
224.16771.0953-0.75563.8315-0.45836.4566-0.181-1.1006-0.38530.5509-0.1003-0.66950.28671.71360.27030.96930.2791-0.04471.23180.12080.8812.178859.5845102.9239
233.502-0.229-1.5411.83510.02862.3047-0.53190.188-0.95640.16470.37070.02941.3396-0.35780.04171.31210.00810.16280.73440.05680.9423-3.10655.782391.9668
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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