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- PDB-4tv8: Tubulin-Maytansine complex -

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Basic information

Entry
Database: PDB / ID: 4tv8
TitleTubulin-Maytansine complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine LigaseTubulin—tyrosine ligase
KeywordsCELL CYCLE / CYTOSKELETON / TUBULIN FOLD / MICROTUBULE
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / double-stranded RNA binding / mitotic cell cycle / nervous system development / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase 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-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / 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-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / 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; / Tubulin-beta mRNA autoregulation signal. / Alpha tubulin / 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 / Dna Ligase; domain 1 / 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
(3beta,4beta,5beta,10beta,11E,13E)-maytansine / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.103 Å
AuthorsProta, A.E. / Bargsten, K. / Diaz, J.F. / Marsh, M. / Cuevas, C. / Liniger, M. / Neuhaus, C. / Andreu, J.M. / Altmann, K.H. / Steinmetz, M.O.
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2014
Title: A new tubulin-binding site and pharmacophore for microtubule-destabilizing anticancer drugs.
Authors: Prota, A.E. / Bargsten, K. / Diaz, J.F. / Marsh, M. / Cuevas, C. / Liniger, M. / Neuhaus, C. / Andreu, J.M. / Altmann, K.H. / Steinmetz, M.O.
History
DepositionJun 26, 2014Deposition site: RCSB / Processing site: PDBE
Revision 1.0Aug 27, 2014Provider: repository / Type: Initial release
Revision 1.1Oct 1, 2014Group: Database references
Revision 1.2Dec 20, 2023Group: 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)265,39823
Polymers261,6316
Non-polymers3,76717
Water12,088671
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23910 Å2
ΔGint-151 kcal/mol
Surface area79630 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.860, 155.570, 180.620
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 / tubulin alpha chain


Mass: 50204.445 Da / Num. of mol.: 2 / Fragment: STATHMIN-LIKE DOMAIN / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain / Tubulin beta chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1 / Fragment: UNP Residues 49-189
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 / 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, 688 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine 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.: 4 / 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 / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#9: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine 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 / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-3GT / (3beta,4beta,5beta,10beta,11E,13E)-maytansine / Maitansine


Mass: 692.196 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C34H46ClN3O10
#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 / Water


Mass: 18.015 Da / Num. of mol.: 671 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.79 Å3/Da / Density % sol: 55.89 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 6% PEG, 16% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 5, 2013
RadiationMonochromator: LN2 cooled fixed-exit Si(III) Monochromator, sagittally-horizontally focussed
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→62.5 Å / Num. all: 169576 / Num. obs: 169427 / % possible obs: 99.6 % / Redundancy: 13.4 % / Rmerge(I) obs: 0.139 / Net I/σ(I): 14.2
Reflection shellResolution: 2.1→2.16 Å / Redundancy: 12.1 % / Mean I/σ(I) obs: 0.6 / % possible all: 94.5

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Processing

Software
NameVersionClassification
PHENIX(phenix.refine: 1.9_1692)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4i4t

4i4t


Resolution: 2.103→62.423 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 26.8 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2185 8415 4.97 %
Rwork0.1894 --
obs0.1909 169427 99.78 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.103→62.423 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17257 0 231 671 18159
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218049
X-RAY DIFFRACTIONf_angle_d0.66424516
X-RAY DIFFRACTIONf_dihedral_angle_d12.8276733
X-RAY DIFFRACTIONf_chiral_restr0.0272684
X-RAY DIFFRACTIONf_plane_restr0.0033178
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.103-2.12690.42282690.43645030X-RAY DIFFRACTION94
2.1269-2.15190.40062570.37185306X-RAY DIFFRACTION100
2.1519-2.17820.35392800.36095303X-RAY DIFFRACTION100
2.1782-2.20570.35542760.34175335X-RAY DIFFRACTION100
2.2057-2.23480.34652570.33115358X-RAY DIFFRACTION100
2.2348-2.26540.35182730.32225307X-RAY DIFFRACTION100
2.2654-2.29780.34392660.30565352X-RAY DIFFRACTION100
2.2978-2.33210.28652700.28735325X-RAY DIFFRACTION100
2.3321-2.36850.30293040.28315367X-RAY DIFFRACTION100
2.3685-2.40730.34112680.27585330X-RAY DIFFRACTION100
2.4073-2.44880.32472780.26215316X-RAY DIFFRACTION100
2.4488-2.49340.29182970.25765319X-RAY DIFFRACTION100
2.4934-2.54130.30862820.24925361X-RAY DIFFRACTION100
2.5413-2.59320.25572710.22685379X-RAY DIFFRACTION100
2.5932-2.64960.28272910.22525307X-RAY DIFFRACTION100
2.6496-2.71120.24312710.21985375X-RAY DIFFRACTION100
2.7112-2.7790.24172880.21265336X-RAY DIFFRACTION100
2.779-2.85420.25652880.20625352X-RAY DIFFRACTION100
2.8542-2.93810.25942860.19875352X-RAY DIFFRACTION100
2.9381-3.0330.23732700.19485370X-RAY DIFFRACTION100
3.033-3.14140.23122900.18645361X-RAY DIFFRACTION100
3.1414-3.26720.1992860.18015376X-RAY DIFFRACTION100
3.2672-3.41580.21422810.17485411X-RAY DIFFRACTION100
3.4158-3.59590.21252830.17085409X-RAY DIFFRACTION100
3.5959-3.82120.17532790.16165407X-RAY DIFFRACTION100
3.8212-4.11620.1852900.15325424X-RAY DIFFRACTION100
4.1162-4.53030.17562860.14665427X-RAY DIFFRACTION100
4.5303-5.18550.17392890.1435491X-RAY DIFFRACTION100
5.1855-6.53210.19782880.17755505X-RAY DIFFRACTION100
6.5321-62.45020.18253010.16845721X-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)
11.4829-0.1327-0.34153.51951.39232.54090.00430.11280.2238-0.53610.2878-0.3-0.77320.3912-0.25710.6504-0.14260.11280.5469-0.14050.472131.599487.208552.0158
21.2776-0.2978-0.65012.8380.78072.70810.0638-0.01850.05920.32950.01850.1373-0.15190.0922-0.06410.45560.00760.04290.4248-0.10130.430820.016380.666366.0051
30.6745-0.3860.28064.44372.05983.0389-0.0473-0.10560.12840.57520.0240.157-0.11520.03030.01530.5311-0.02710.12340.4435-0.08590.464618.932481.855873.533
41.4275-0.00480.81362.44611.79553.8551-0.04990.0516-0.19310.49520.4291-0.37170.58230.7333-0.34930.50.1353-0.06830.5406-0.15410.558232.942560.710460.5178
51.92850.9891.42772.84022.94383.18280.0827-0.916-0.23380.7175-0.13140.2129-0.3171-0.03730.0321.5763-0.00880.16471.1039-0.13781.359924.632963.323685.5997
63.3892-1.7638-0.78215.28040.69523.4190.14520.15120.6108-0.4228-0.15750.1685-0.8167-0.20030.05470.58660.0635-0.01130.5063-0.02020.584716.212769.330319.4682
71.4610.0372-0.89663.96890.86152.1026-0.00530.2657-0.0317-0.55740.1547-0.2106-0.41210.2606-0.15140.4189-0.05920.01130.5605-0.08040.381429.071455.664714.4991
82.18240.715-0.00253.49491.3462.8166-0.0036-0.1159-0.0554-0.04640.0456-0.1697-0.12830.1614-0.01060.25720.01570.01690.4002-0.10810.375724.417952.397925.967
95.5459-1.28720.33532.1174-0.78032.7493-0.1986-0.52650.1302-0.0586-0.21020.71810.3166-1.04190.35790.4077-0.08290.06050.7127-0.26090.5795.399250.066928.1471
100.7645-0.8993-0.98391.95741.46632.91010.0073-0.03110.0566-0.1533-0.06750.1412-0.4184-0.50120.10530.39540.03880.01650.4676-0.12250.4689.596461.033935.2121
112.3042-0.78650.5882.45940.22283.3963-0.1851-0.19820.06560.3147-0.04260.3509-0.1443-0.9570.21050.48340.06080.06180.654-0.15860.53246.49359.876944.7263
120.5377-0.8284-0.31782.29742.30542.9326-0.016-0.0633-0.15270.3876-0.20560.6350.3374-0.25420.28410.4161-0.0270.06060.4055-0.0840.475315.411641.353533.9923
130.73030.3428-0.65322.72262.3776.7460.0224-0.16-0.19660.56160.085-0.13150.72270.6141-0.15290.43320.0337-0.0550.4358-0.03490.461925.657837.301930.9128
141.2499-0.4893-0.20122.8640.08741.6753-0.03940.15290.1575-0.28010.0865-0.0807-0.16170.1324-0.05260.3386-0.07750.02960.4201-0.03180.368820.284332.2379-12.0189
150.769-0.2869-0.01681.69561.07271.833-0.0358-0.04340.11430.0946-0.04610.11690.0726-0.2290.06760.2784-0.06940.04060.3629-0.02710.3637.928225.18823.1462
163.735-1.03490.22342.77870.00172.4854-0.13320.82550.0931-0.57280.11440.02450.1614-0.24190.01010.7039-0.15630.05110.8621-0.04950.397117.39918.8311-43.9653
171.28520.1735-0.38161.29590.12971.9921-0.08890.4504-0.2472-0.36130.0867-0.17150.3210.0345-0.00420.6247-0.06030.09390.58-0.19560.430520.7286-3.0148-33.4947
182.1463-0.6015-0.23581.1340.3852.1214-0.20850.2732-0.2921-0.00120.10430.1820.3768-0.21410.11010.6652-0.1350.05690.5679-0.10920.49049.0234-4.6072-21.1921
193.5395-0.3949-1.68011.94-0.38893.7604-0.42430.0644-0.59110.1310.112-0.23391.02760.44630.12280.87350.07420.09350.5512-0.18850.756230.3231-17.2159-24.1005
203.4437-1.8173-0.32295.05511.5562.2603-0.2063-0.31540.26340.84560.4203-0.49870.02060.7904-0.25610.9069-0.0143-0.06340.7811-0.15410.520127.427791.312882.2348
210.4375-0.3371-0.55691.57891.7512.3761-0.0559-0.07790.01290.30030.3911-0.40130.45050.5801-0.45720.4870.08250.03820.7206-0.1930.702542.869228.10935.0358
223.12681.1521-2.1623.8323-0.1113.3612-0.54940.502-0.6095-0.23620.1640.03981.2084-0.58250.30971.0308-0.14030.16210.5919-0.14680.62856.209553.395669.7203
231.8187-0.3816-0.38052.4692-0.58683.3204-0.2427-0.9341-0.73010.4979-0.28-0.85230.53411.66720.39560.93440.2036-0.04351.34290.31870.94715.775356.1312105.3874
242.73870.5963-1.74341.2536-0.07932.2765-0.5416-0.0662-0.71920.10960.2519-0.040.9675-0.2069-0.03190.96880.02710.19260.45190.08020.6728-1.828152.6893.0601
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:180)
2X-RAY DIFFRACTION2chain 'A' and (resseq 181:311)
3X-RAY DIFFRACTION3chain 'A' and (resseq 312:401)
4X-RAY DIFFRACTION4chain 'A' and (resseq 402:436)
5X-RAY DIFFRACTION5chain 'A' and (resseq 437:439)
6X-RAY DIFFRACTION6chain 'B' and (resseq 1:88)
7X-RAY DIFFRACTION7chain 'B' and (resseq 89:127)
8X-RAY DIFFRACTION8chain 'B' and (resseq 128:197)
9X-RAY DIFFRACTION9chain 'B' and (resseq 198:223)
10X-RAY DIFFRACTION10chain 'B' and (resseq 224:295)
11X-RAY DIFFRACTION11chain 'B' and (resseq 296:373)
12X-RAY DIFFRACTION12chain 'B' and (resseq 374:401)
13X-RAY DIFFRACTION13chain 'B' and (resseq 402:438)
14X-RAY DIFFRACTION14chain 'C' and (resseq 1:197)
15X-RAY DIFFRACTION15chain 'C' and (resseq 198:440)
16X-RAY DIFFRACTION16chain 'D' and (resseq 1:88)
17X-RAY DIFFRACTION17chain 'D' and (resseq 89:295)
18X-RAY DIFFRACTION18chain 'D' and (resseq 296:401)
19X-RAY DIFFRACTION19chain 'D' and (resseq 402:441)
20X-RAY DIFFRACTION20chain 'E' and (resseq 6:46)
21X-RAY DIFFRACTION21chain 'E' and (resseq 47:141)
22X-RAY DIFFRACTION22chain 'F' and (resseq 1:66)
23X-RAY DIFFRACTION23chain 'F' and (resseq 67:198)
24X-RAY DIFFRACTION24chain 'F' and (resseq 199:380)

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