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- PDB-5nfz: TUBULIN-MTC complex -

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Basic information

Entry
Database: PDB / ID: 5nfz
TitleTUBULIN-MTC 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
Chem-8WB / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.1 Å
AuthorsField, J.J. / Pera, B. / Estevez Gallego, J. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Prota, A.E. / Menchon, G. ...Field, J.J. / Pera, B. / Estevez Gallego, J. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Prota, A.E. / Menchon, G. / Miller, J.H. / Altmann, K.-H. / Diaz, J.F.
CitationJournal: J. Nat. Prod. / Year: 2018
Title: Zampanolide Binding to Tubulin Indicates Cross-Talk of Taxane Site with Colchicine and Nucleotide Sites.
Authors: Field, J.J. / Pera, B. / Gallego, J.E. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Andreu, J.M. / Prota, A.E. / Menchon, G. / Miller, J.H. / Altmann, K.H. / Diaz, J.F.
History
DepositionMar 16, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 25, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 4, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2May 2, 2018Group: Data collection / Category: reflns / Item: _reflns.pdbx_Rpim_I_all
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.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)265,24324
Polymers261,6316
Non-polymers3,61218
Water8,089449
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23110 Å2
ΔGint-149 kcal/mol
Surface area81580 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.163, 158.787, 180.376
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) / 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 (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, 467 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.: 4 / 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-8WB / 2-methoxy-5-(2,3,4-trimethoxyphenyl)cyclohepta-2,4,6-trien-1-one


Mass: 302.322 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H18O5
#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.: 449 / 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: 2.88 Å3/Da / Density % sol: 57.26 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 5% PEG 4K, 12-14% glycerol, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES/Imidazole, pH 6.7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.97976 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: May 2, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97976 Å / Relative weight: 1
ReflectionResolution: 2.1→59.782 Å / Num. obs: 175862 / % possible obs: 100 % / Redundancy: 13.5 % / CC1/2: 0.999 / Rmerge(I) obs: 0.135 / Rpim(I) all: 0.042 / Net I/σ(I): 16.2
Reflection shellResolution: 2.1→2.15 Å / Redundancy: 10.6 % / Rmerge(I) obs: 2.89 / Mean I/σ(I) obs: 0.92 / Num. unique obs: 12854 / CC1/2: 0.452 / Rpim(I) all: 0.879 / % possible all: 99.8

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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: 2.1→59.782 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 24.61
RfactorNum. reflection% reflection
Rfree0.2176 8794 5 %
Rwork0.1821 --
obs0.1839 175862 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.1→59.782 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17419 0 222 449 18090
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00718071
X-RAY DIFFRACTIONf_angle_d0.85624506
X-RAY DIFFRACTIONf_dihedral_angle_d15.49810776
X-RAY DIFFRACTIONf_chiral_restr0.0522662
X-RAY DIFFRACTIONf_plane_restr0.0053176
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12390.3812880.35315470X-RAY DIFFRACTION100
2.1239-2.14890.39792920.34865553X-RAY DIFFRACTION100
2.1489-2.17510.37192900.32555485X-RAY DIFFRACTION100
2.1751-2.20260.352910.31165526X-RAY DIFFRACTION100
2.2026-2.23160.31952890.2985498X-RAY DIFFRACTION100
2.2316-2.26210.29412890.27235491X-RAY DIFFRACTION100
2.2621-2.29450.30882930.26465568X-RAY DIFFRACTION100
2.2945-2.32870.30542890.26425490X-RAY DIFFRACTION100
2.3287-2.36510.30192900.25155513X-RAY DIFFRACTION100
2.3651-2.40390.28592930.24325565X-RAY DIFFRACTION100
2.4039-2.44530.28172910.23825520X-RAY DIFFRACTION100
2.4453-2.48980.25572890.22225503X-RAY DIFFRACTION100
2.4898-2.53770.27792930.22075559X-RAY DIFFRACTION100
2.5377-2.58950.25222900.20715512X-RAY DIFFRACTION100
2.5895-2.64580.25032930.19985573X-RAY DIFFRACTION100
2.6458-2.70730.25782910.20625528X-RAY DIFFRACTION100
2.7073-2.7750.27322940.2055574X-RAY DIFFRACTION100
2.775-2.85010.23072920.19195555X-RAY DIFFRACTION100
2.8501-2.93390.21882920.19265547X-RAY DIFFRACTION100
2.9339-3.02860.25212920.1915548X-RAY DIFFRACTION100
3.0286-3.13690.22722930.1875559X-RAY DIFFRACTION100
3.1369-3.26250.21162940.18415598X-RAY DIFFRACTION100
3.2625-3.41090.21942940.18455574X-RAY DIFFRACTION100
3.4109-3.59070.22132950.17565611X-RAY DIFFRACTION100
3.5907-3.81570.21322940.16265588X-RAY DIFFRACTION100
3.8157-4.11020.17042950.14655595X-RAY DIFFRACTION100
4.1102-4.52370.15622980.12935669X-RAY DIFFRACTION100
4.5237-5.1780.15612970.12885640X-RAY DIFFRACTION100
5.178-6.52250.20143020.16655732X-RAY DIFFRACTION100
6.5225-59.80660.16863110.15535924X-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)
10.9633-0.0331-0.26024.19981.27762.8760.01840.14550.1441-0.4490.3245-0.3801-0.69880.4444-0.30760.5275-0.12350.11470.5016-0.15550.429631.810488.584251.8737
21.3112-0.191-0.16332.95051.28493.22570.08580.02030.00480.351-0.0020.1572-0.0725-0.0232-0.08250.3863-0.00660.05970.3167-0.07430.340819.094582.934165.7681
30.6968-0.12540.30034.62011.5542.7248-0.0066-0.14920.09260.79250.04830.181-0.0512-0.0641-0.07060.4871-0.01790.11620.3894-0.07220.351118.850983.828473.3911
41.991-0.2025-1.1824.6544.60827.7067-0.0606-0.2199-0.11820.93810.4514-0.43330.92090.9254-0.370.47520.1436-0.11820.4085-0.12680.452432.621762.234460.8336
55.6337-1.6205-0.77596.80321.51863.82480.1990.2630.6101-0.5765-0.18510.1457-0.9693-0.23480.01380.49530.05160.01510.3561-0.01440.347616.103570.184919.231
62.0366-0.6773-0.7768.9478-0.03343.23370.17860.3930.0113-0.32530.0049-0.5462-0.43160.3077-0.17090.3099-0.0390.04560.539-0.09260.335429.141856.536814.6244
72.88582.64880.40767.39522.44584.015-0.0063-0.09520.1159-0.03880.0305-0.139-0.18690.1748-0.04410.19810.03170.02130.3512-0.10230.315124.399253.443326.1598
87.6004-0.11821.39110.8708-0.92492.3589-0.1366-0.4236-0.25950.1008-0.23640.52740.4163-0.85130.33470.3468-0.05730.10.6322-0.30850.53045.43551.165328.3092
91.8178-0.8523-0.17541.76070.94022.6734-0.0322-0.12250.10390.0296-0.13870.2285-0.3166-0.48350.08430.33040.02560.02690.4306-0.15420.41519.876662.224935.8893
103.7937-1.08030.93712.9178-0.57863.2016-0.2942-0.32150.12910.39520.03640.2949-0.1831-0.98220.16630.44920.0570.0960.6599-0.1910.46546.371760.973644.8804
111.1567-3.1863-2.2248.92846.78525.4558-0.0251-0.1013-0.08870.5767-0.21780.58170.6435-0.21830.30430.3018-0.07060.03950.3696-0.08780.342615.442142.335534.1694
121.6168-1.6893-1.2055.63124.87696.8643-0.1193-0.3061-0.17690.96870.1429-0.20371.11130.7253-0.00920.3937-0.0268-0.07040.4187-0.03540.372525.657138.296131.0224
131.2432-0.32640.10232.75690.16871.8515-0.04410.19780.1021-0.30510.0792-0.0661-0.16760.1441-0.02450.2657-0.06180.0370.3439-0.03650.28620.327933.4482-12.1481
140.9183-0.49890.03561.57030.87391.4216-0.016-0.00910.01120.0834-0.08650.18830.0935-0.23810.08680.2317-0.05950.03860.2886-0.03890.30997.79626.33853.0097
155.6653-3.1985-0.88637.29931.78993.87330.03660.91380.1377-0.83930.0170.1363-0.1292-0.2275-0.07210.7023-0.13160.0320.7979-0.020.284917.329910.201-44.4519
161.8259-0.0358-0.47121.70110.35222.1098-0.11210.5412-0.1858-0.51010.1591-0.16010.2343-0.0935-0.07010.6114-0.06340.06750.5886-0.18970.403620.4917-1.758-34.0619
171.6880.0212-0.73832.04860.70873.0754-0.17280.3595-0.32180.00850.10620.22050.3423-0.49910.11650.4464-0.08610.01290.4489-0.12050.39219.0809-3.4656-21.61
182.927-2.03-2.62124.16332.8986.6776-0.4720.0672-0.86730.09890.1713-0.35760.92710.6293-0.17450.67790.06280.03450.5126-0.27610.743930.5076-15.9146-24.5657
192.9739-1.59880.30715.05430.08142.30450.027-0.26280.21951.4390.4269-0.36-0.20970.5198-0.39490.9342-0.0951-0.02890.5926-0.1850.50828.490692.336181.3073
200.2901-0.1616-0.25530.79370.97521.6842-0.0772-0.0142-0.04770.26450.4627-0.45230.40560.6513-0.49460.3970.05980.0490.6815-0.26020.654843.118127.6473.5728
213.76963.36830.07126.5961.83722.7184-0.56390.5474-0.8396-0.2329-0.0355-0.25291.3374-0.54160.31991.0079-0.16530.23050.6234-0.18680.62266.02955.341170.115
222.09590.1968-0.00772.9304-1.49063.7688-0.0218-0.8949-0.6670.6152-0.5489-0.87290.2841.79270.57430.87980.1918-0.03661.28050.33070.836214.887358.2591105.489
233.2880.6519-2.37961.9419-0.1952.6447-0.6548-0.1328-0.91860.19820.2122-0.12741.03160.08310.01270.9560.06130.17870.42090.07680.6792-1.52454.366594.1296
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 379)

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