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- PDB-4tv9: Tubulin-PM060184 complex -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 4tv9
TitleTubulin-PM060184 complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Uncharacterized protein
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
Chem-3H4 / 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 / FOURIER SYNTHESIS / Resolution: 2 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.
Funding support Switzerland, Spain, 5items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_138659 Switzerland
Ministero de Economia y CompetitividadBIO2010-16351 Spain
Ministero de Economia y CompetitividadBFU2011-23416 Spain
Comunidad Autonoma de MadridS2010/BMD-2457 Spain
Comunidad Autonoma de MadridS2010/BMD-2353 Spain
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 20, 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 / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _chem_comp.name / _database_2.pdbx_DOI ..._chem_comp.name / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _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: Uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,22222
Polymers261,6316
Non-polymers3,59116
Water13,439746
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23340 Å2
ΔGint-160 kcal/mol
Surface area79500 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.200, 157.290, 180.220
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) / 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) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1 / Fragment: STATHMIN-LIKE DOMAIN, 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 Uncharacterized protein


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, 762 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.: 2 / 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-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.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-3H4 / (1Z,4S,6Z)-1-[(N-{(2Z,4Z,6E,8S)-8-[(2S)-5-methoxy-6-oxo-3,6-dihydro-2H-pyran-2-yl]-6-methylnona-2,4,6-trienoyl}-3-methy l-L-valyl)amino]octa-1,6-dien-4-yl carbamate / PM060184


Mass: 571.705 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C31H45N3O7
#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.: 746 / 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: 2.82 Å3/Da / Density % sol: 56.42 %
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: Mar 3, 2013
RadiationMonochromator: LN2 cooled fixed-exit SI(111) 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→52.05 Å / Num. obs: 199377 / % possible obs: 99.9 % / Redundancy: 37.6 % / Rmerge(I) obs: 0.104 / Net I/σ(I): 23.7
Reflection shellResolution: 2→2.05 Å / Redundancy: 20.1 % / Mean I/σ(I) obs: 1.1 / % possible all: 99.1

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Processing

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

4i4t


Resolution: 2→52.044 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 22.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2077 9967 5 %
Rwork0.1801 --
obs0.1815 199355 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2→52.044 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17275 0 223 746 18244
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00318169
X-RAY DIFFRACTIONf_angle_d0.70924721
X-RAY DIFFRACTIONf_dihedral_angle_d12.0976826
X-RAY DIFFRACTIONf_chiral_restr0.0282719
X-RAY DIFFRACTIONf_plane_restr0.0033201
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.02270.39833240.38686153X-RAY DIFFRACTION98
2.0227-2.04650.3523300.33186280X-RAY DIFFRACTION100
2.0465-2.07150.35653310.31256288X-RAY DIFFRACTION100
2.0715-2.09770.34523270.29546209X-RAY DIFFRACTION100
2.0977-2.12530.29723290.26096263X-RAY DIFFRACTION100
2.1253-2.15440.26073290.23446243X-RAY DIFFRACTION100
2.1544-2.18520.23113310.21866284X-RAY DIFFRACTION100
2.1852-2.21780.25783300.20936271X-RAY DIFFRACTION100
2.2178-2.25250.22773270.20236222X-RAY DIFFRACTION100
2.2525-2.28940.24083310.19736289X-RAY DIFFRACTION100
2.2894-2.32890.24313310.20016285X-RAY DIFFRACTION100
2.3289-2.37130.23463310.19736294X-RAY DIFFRACTION100
2.3713-2.41690.22883310.19386291X-RAY DIFFRACTION100
2.4169-2.46620.24393290.19236246X-RAY DIFFRACTION100
2.4662-2.51980.2273300.19566262X-RAY DIFFRACTION100
2.5198-2.57840.2153310.18816300X-RAY DIFFRACTION100
2.5784-2.64290.21793310.19016289X-RAY DIFFRACTION100
2.6429-2.71440.2253330.19316322X-RAY DIFFRACTION100
2.7144-2.79420.23243290.19686250X-RAY DIFFRACTION100
2.7942-2.88440.24013340.1986342X-RAY DIFFRACTION100
2.8844-2.98750.22273320.19686318X-RAY DIFFRACTION100
2.9875-3.10710.19933330.18746326X-RAY DIFFRACTION100
3.1071-3.24850.22783320.19486309X-RAY DIFFRACTION100
3.2485-3.41970.22413350.1896347X-RAY DIFFRACTION100
3.4197-3.63390.20733330.17636344X-RAY DIFFRACTION100
3.6339-3.91440.1813360.16276370X-RAY DIFFRACTION100
3.9144-4.30820.16963360.15236382X-RAY DIFFRACTION100
4.3082-4.93120.16683380.13666427X-RAY DIFFRACTION100
4.9312-6.21110.19153410.16796478X-RAY DIFFRACTION100
6.2111-52.06130.1923520.16526704X-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)
11.1341-0.1733-0.01083.78161.26152.2635-0.00550.0850.1893-0.46050.2814-0.3672-0.71790.4006-0.24460.5689-0.14750.13020.4533-0.14160.421431.67888.048451.791
21.1887-0.4867-0.49093.22041.21332.95550.0580.00770.10180.26870.00990.1281-0.24160.0082-0.06380.3869-0.00080.04710.3276-0.08050.34519.211482.108165.7207
30.6846-0.22740.00674.84931.82912.6372-0.0179-0.13430.12560.60720.07210.1755-0.14280.0017-0.05560.4754-0.01730.10210.4209-0.07370.406818.832483.068573.3473
41.4314-0.3264-0.96383.52133.46338.0906-0.0642-0.1738-0.12490.70980.4345-0.41130.69481.0024-0.32940.48520.1401-0.08350.4678-0.14470.496832.9661.588660.5539
52.1955-0.2749-1.03332.9149-2.53973.15760.2143-2.0146-0.9282.40310.38991.05740.6992-0.6054-0.56611.71390.09120.23921.2370.07661.403324.063264.264285.5069
64.7072-1.8944-0.87077.61881.41714.28750.22680.22830.6972-0.4263-0.17810.1375-0.9867-0.21160.00880.46020.04240.01830.35340.00760.422816.093469.74919.3531
72.1784-0.2274-0.84565.9970.80712.67420.13750.36520.0481-0.413-0.0223-0.4353-0.44290.3297-0.12350.3092-0.03480.03080.5361-0.05990.322429.042755.908314.3955
82.04271.19490.16345.1411.81443.45750.0125-0.11940.08290.03590.0408-0.1088-0.1490.1506-0.05390.20930.0150.02920.3515-0.10970.335324.434752.911326.0463
91.1883-1.11011.03511.1445-1.24141.6254-0.1665-0.5703-0.14210.0061-0.18610.66940.2438-0.97510.34020.3591-0.06960.07450.7966-0.32730.61135.374750.675128.2215
100.6952-0.6134-0.0081.43660.91342.7251-0.0413-0.08610.1356-0.0737-0.02280.1183-0.383-0.36790.05220.35690.02410.03360.4366-0.12510.438210.481261.655635.7447
112.8403-0.52190.37182.359-0.5573.84-0.2229-0.14950.01050.3462-0.00540.4075-0.1448-0.99330.22530.440.06640.06840.6596-0.17650.46526.54460.606244.8264
121.9256-2.6462-1.28075.43484.01133.6277-0.0235-0.1097-0.2130.2381-0.16020.70340.443-0.21260.20730.3135-0.03410.04980.2969-0.06170.334315.40341.896334.043
131.4977-0.9401-1.40893.74962.94592.8337-0.0755-0.2277-0.1650.60540.1537-0.12430.65310.7149-0.11090.36170.0047-0.03460.4156-0.0380.389625.665537.839230.9121
141.1852-0.2149-0.06712.62760.27771.8729-0.02070.12170.1721-0.25250.0852-0.0436-0.18480.1293-0.05760.2507-0.06420.03210.3307-0.030.293720.325332.7303-12.0021
150.8692-0.2243-0.03391.36390.91561.65310.00140.0010.08370.0925-0.09120.12790.0763-0.22370.07950.2197-0.06020.03930.2943-0.03340.2877.718525.80763.0354
164.5084-2.235-0.12525.66731.17523.1199-0.04310.65590.0784-0.76960.04760.1339-0.0266-0.1838-0.00220.6226-0.11930.03060.7243-0.0150.306417.44719.4678-44.0851
171.33940.0186-0.20361.49990.51882.2269-0.10620.361-0.1394-0.33450.1315-0.17990.33890.1165-0.02950.5507-0.03580.07280.5141-0.16060.362521.0973-2.5541-33.6963
182.2735-0.6038-0.26131.31650.59182.1646-0.19830.2658-0.2564-0.02870.07910.17720.3567-0.2160.13970.5212-0.1240.04820.4189-0.11550.39129.0829-4.092-21.3546
193.1259-0.5919-1.01212.59151.26013.2953-0.37240.0709-0.65140.07810.0967-0.23010.76840.43770.11150.74990.08940.08030.4175-0.14950.550830.3857-16.6712-24.2389
203.4082-2.7805-0.73165.68041.55641.8238-0.1184-0.21850.29910.7280.6501-0.5303-0.04030.7713-0.52110.9468-0.0908-0.03370.7536-0.23940.625727.290393.065781.5789
210.1835-0.1902-0.40760.84771.14561.838-0.1039-0.0342-0.02570.39580.6635-0.54250.55160.9635-0.58730.44180.09610.01420.7242-0.25250.636642.955728.13924.4575
221.54921.7102-0.42275.1351.17822.9951-0.57330.4838-0.6599-0.40650.2408-0.18771.3858-0.55210.16670.9949-0.17210.17140.577-0.1680.56686.46254.256569.8923
233.20550.13150.03453.0037-0.8993.8216-0.1024-0.7773-0.55490.597-0.3217-0.83670.24971.46810.4020.72010.1266-0.09231.03210.22940.70615.731657.5924104.2504
242.37230.8641-1.93331.626-0.49752.3407-0.4336-0.0207-0.66070.14690.251-0.13270.8574-0.033-0.05590.90140.03410.11620.39220.03720.6096-1.360853.12993.8235
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 47:142)
22X-RAY DIFFRACTION22chain 'F' and (resseq 1:66)
23X-RAY DIFFRACTION23chain 'F' and (resseq 67:198)
24X-RAY DIFFRACTION24chain 'F' and (resseq 199:378)

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