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- PDB-4o4h: Tubulin-Laulimalide complex -

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Basic information

Entry
Database: PDB / ID: 4o4h
TitleTubulin-Laulimalide complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligase
KeywordsCELL CYCLE/INHIBITOR / ALPHA-TUBULIN / BETA-TUBULIN / LIGASE / GTPASE / MICROTUBULE / STATHMIN / LAULIMALIDE / CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / CELL CYCLE-INHIBITOR complex
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 / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Laulimalide / 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 / Difference Fourier / Resolution: 2.1 Å
AuthorsProta, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Structural basis of microtubule stabilization by laulimalide and peloruside a.
Authors: Prota, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
History
DepositionDec 18, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 5, 2014Provider: repository / Type: Initial release
Revision 1.1Mar 12, 2014Group: Data collection
Revision 1.2Sep 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 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _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 / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_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)265,01022
Polymers261,6316
Non-polymers3,37916
Water11,818656
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.693, 156.868, 180.451
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 / Details: BRAIN / 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 / Details: BRAIN / 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) / 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) / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 672 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.: 3 / Source method: obtained synthetically / Formula: Ca
#8: 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
#9: Chemical ChemComp-LLM / Laulimalide / (1R,3S,7S,8S,10S,12S,15Z,18R)-7-hydroxy-12-{(1S,2E)-1-hydroxy-3-[(2S)-4-methyl-3,6-dihydro-2H-pyran-2-yl]prop-2-en-1-yl }-3-methyl-5-methylidene-9,13,22-trioxatricyclo[16.3.1.0~8,10~]docosa-15,19-dien-14-one


Mass: 514.650 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C30H42O7
#10: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#11: 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
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 656 / 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: 2.83 Å3/Da / Density % sol: 56.56 %
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, pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: PSI PILATUS 2M / Detector: PIXEL / Date: Mar 3, 2013
RadiationMonochromator: vertically collimating mirror (M1, focus at infinity), followed by a Bartels Monochromator with dual channel cut crystals (DCCM) in (+--+) geometry, and a toroidal mirror (M2) to ...Monochromator: vertically collimating mirror (M1, focus at infinity), followed by a Bartels Monochromator with dual channel cut crystals (DCCM) in (+--+) geometry, and a toroidal mirror (M2) to vertically and horizontally focus the beam at the sample position (with 2:1 horizontal demagnification)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→71.9 Å / Num. all: 173149 / Num. obs: 172824 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 13.6 % / Rmerge(I) obs: 0.181 / Net I/σ(I): 14.3
Reflection shellResolution: 2.1→2.15 Å / Redundancy: 12.7 % / Rmerge(I) obs: 2.89 / Mean I/σ(I) obs: 1 / % possible all: 99.6

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Processing

Software
NameVersionClassification
DA+data collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: Difference Fourier
Starting model: 4I4T

4i4t


Resolution: 2.1→71.9 Å / SU ML: 0.27 / σ(F): 1.99 / Phase error: 23.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2239 8659 5.01 %RANDOM
Rwork0.1924 ---
obs0.194 172789 99.79 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.1→71.9 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17432 0 208 656 18296
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00618345
X-RAY DIFFRACTIONf_angle_d1.15924973
X-RAY DIFFRACTIONf_dihedral_angle_d15.4536902
X-RAY DIFFRACTIONf_chiral_restr0.0772751
X-RAY DIFFRACTIONf_plane_restr0.0043244
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1-2.12390.3722610.32925426X-RAY DIFFRACTION100
2.1239-2.14890.3612740.31625394X-RAY DIFFRACTION99
2.1489-2.17510.34322870.30395462X-RAY DIFFRACTION100
2.1751-2.20260.33922900.29095337X-RAY DIFFRACTION99
2.2026-2.23160.31682700.28315422X-RAY DIFFRACTION99
2.2316-2.26220.31572740.2765413X-RAY DIFFRACTION100
2.2622-2.29450.32363190.26535378X-RAY DIFFRACTION99
2.2945-2.32870.2943060.25195418X-RAY DIFFRACTION99
2.3287-2.36510.26892960.24445410X-RAY DIFFRACTION100
2.3651-2.40390.28823080.23955381X-RAY DIFFRACTION100
2.4039-2.44540.26512900.22925481X-RAY DIFFRACTION100
2.4454-2.48980.25492740.21935443X-RAY DIFFRACTION100
2.4898-2.53770.26732800.21995404X-RAY DIFFRACTION100
2.5377-2.58950.24483030.21345426X-RAY DIFFRACTION100
2.5895-2.64580.27313020.21275429X-RAY DIFFRACTION100
2.6458-2.70740.28322760.21155454X-RAY DIFFRACTION100
2.7074-2.77510.27062640.21395479X-RAY DIFFRACTION100
2.7751-2.85010.24452720.20715493X-RAY DIFFRACTION100
2.8501-2.9340.23723050.20135423X-RAY DIFFRACTION100
2.934-3.02870.22442690.18995513X-RAY DIFFRACTION100
3.0287-3.1370.22962940.18585458X-RAY DIFFRACTION100
3.137-3.26260.22062960.19295510X-RAY DIFFRACTION100
3.2626-3.4110.22953100.19215453X-RAY DIFFRACTION100
3.411-3.59090.20842840.17525504X-RAY DIFFRACTION100
3.5909-3.81590.21262770.16225515X-RAY DIFFRACTION100
3.8159-4.11050.17272940.15255523X-RAY DIFFRACTION100
4.1105-4.52410.14623090.14255555X-RAY DIFFRACTION100
4.5241-5.17860.18032800.14165578X-RAY DIFFRACTION100
5.1786-6.5240.19523040.18245642X-RAY DIFFRACTION100
6.524-78.26560.18132910.17195806X-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)
11.05630.015-0.28732.08540.86871.89130.02460.03640.2034-0.38220.2351-0.2596-0.61570.3187-0.1680.465-0.12020.09360.3547-0.10930.356831.84587.976851.6834
20.9034-0.0838-0.16422.13440.45331.94410.0749-0.02010.08320.14520.00340.0931-0.1760.0886-0.06490.3031-0.00630.04090.2718-0.07360.2919.507381.928565.8314
30.39680.2030.39862.08740.57451.27990.0072-0.08570.03270.4256-0.03340.1742-0.0888-0.04140.03140.43560.00810.08130.3579-0.06540.351519.184582.927773.3328
40.58880.1895-0.14141.40380.80072.0646-0.02730.0036-0.16940.31850.2039-0.2410.27370.527-0.11480.33430.0865-0.04350.3738-0.11390.380933.006861.520460.3443
52.2268-0.1139-2.73330.04620.07453.4603-0.0802-0.2497-0.59850.11290.05350.26360.6069-0.3279-0.05031.33530.08830.27451.11920.20521.099324.526364.08785.3239
62.3646-0.5417-0.68892.4865-0.01651.90230.15140.22780.4977-0.2396-0.09270.1748-0.5926-0.1052-0.04410.42470.00690.02350.2879-0.01220.398516.181769.897219.3479
71.118-0.2868-0.25971.22470.15561.30130.11090.31390.0268-0.2032-0.0297-0.1789-0.31390.3029-0.08180.307-0.04730.03770.4393-0.04270.296829.138656.134914.3195
81.07980.1078-0.22781.55980.71441.6854-0.0128-0.0642-0.0062-0.09150.0788-0.0787-0.16030.1626-0.06520.21650.00790.00660.3235-0.09030.289724.374553.133325.9925
93.3974-0.44960.47741.0794-0.44691.8364-0.1284-0.35340.19370.0296-0.16920.44340.1021-0.58050.23280.2794-0.02220.0160.4748-0.18770.40755.438550.628428.1325
100.4226-0.497-0.3170.95360.41741.33710.00850.0832-0.0299-0.0413-0.01970.2016-0.2497-0.26830.0340.3040.01990.01880.3632-0.09150.393310.15161.675435.4942
111.5945-0.33120.00750.81770.30971.5724-0.1589-0.142-0.02680.2007-0.01140.2765-0.1318-0.59280.16770.39080.04540.03320.4796-0.12340.42156.651160.661144.6258
120.7039-0.33210.28680.71950.70491.36470.0284-0.0444-0.08080.0113-0.08180.26850.1175-0.11210.07430.2925-0.01610.04590.2774-0.05220.300415.471341.9633.958
130.1635-0.21420.26331.63731.27463.3991-0.0061-0.0234-0.03840.32040.1029-0.09750.37170.3276-0.09620.24390.0164-0.04940.2572-0.01760.269425.683738.093631.2249
140.00640.0045-0.00640.0031-0.00450.00630.0332-0.0346-0.0327-0.01920.00290.2179-0.0651-0.0816-0.00140.97180.28510.27851.28890.13941.2738-0.838153.214246.593
150.7494-0.1041-0.10761.61380.30471.4358-0.03240.10060.0949-0.18650.0881-0.0262-0.12650.0929-0.04140.1703-0.04950.02350.2225-0.0250.210920.195332.5043-12.0374
160.6405-0.298-0.08641.02640.58771.3292-0.01970.02430.03450.0508-0.03760.09070.0518-0.17260.0520.1899-0.03690.02620.2426-0.03020.25187.820325.73073.1731
172.4905-0.49950.11162.06780.10381.6708-0.11930.52740.0752-0.41610.13050.11450.0371-0.1641-0.02270.443-0.08820.01670.5586-0.03160.302317.2199.1658-43.941
180.84570.0355-0.2140.85620.0551.6578-0.07890.282-0.1276-0.24860.0768-0.10250.23940.0243-0.01230.4007-0.04070.05240.4051-0.13540.31520.3092-2.7775-33.6524
191.46380.0984-0.40960.82120.46551.6033-0.16650.2139-0.17780.04140.04370.06770.2899-0.23320.12650.3924-0.08850.04480.3588-0.08640.30978.92-4.2053-21.1408
202.3021-0.2299-1.37191.27670.12392.598-0.1347-0.0454-0.39440.01410.0182-0.11620.45340.3924-0.00850.59120.07820.05050.432-0.12850.527130.1806-16.8316-23.9629
211.44060.04470.08480.48820.24040.5102-0.1861-0.15540.25940.5290.19-0.49840.33860.52540.02060.88030.02580.04230.6277-0.12590.488827.778392.866981.5402
220.1577-0.0831-0.23521.63781.37681.1391-0.061-0.01960.03570.35370.3153-0.26920.45110.4595-0.18690.3410.06390.03260.5175-0.16640.494842.932827.36573.7727
231.22640.9608-0.73342.8119-0.2480.9338-0.47610.3806-0.4946-0.30990.0870.02631.3395-0.5790.25361.0303-0.20170.1780.5858-0.13520.55236.71354.149769.8402
241.5397-0.002-0.23051.5287-0.46732.075-0.0627-0.738-0.37840.4755-0.3601-0.74210.21.1910.30870.66630.0819-0.04780.87390.22340.694615.880357.4568105.2438
251.72160.7288-1.58761.327-0.4531.6414-0.4120.0517-0.4722-0.03940.2393-0.00920.7398-0.1439-0.0420.7515-0.00940.11910.35370.04690.5061-1.357453.057193.5885
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 1:180 )A1 - 180
2X-RAY DIFFRACTION2( CHAIN A AND RESID 181:311 )A181 - 311
3X-RAY DIFFRACTION3( CHAIN A AND RESID 312:401 )A312 - 401
4X-RAY DIFFRACTION4( CHAIN A AND RESID 402:436 )A402 - 436
5X-RAY DIFFRACTION5( CHAIN A AND RESID 437:439 )A437 - 439
6X-RAY DIFFRACTION6( CHAIN B AND RESID 1:88 )B1 - 88
7X-RAY DIFFRACTION7( CHAIN B AND RESID 89:127 )B89 - 127
8X-RAY DIFFRACTION8( CHAIN B AND RESID 128:197 )B128 - 197
9X-RAY DIFFRACTION9( CHAIN B AND RESID 198:223 )B198 - 223
10X-RAY DIFFRACTION10( CHAIN B AND RESID 224:295 )B224 - 295
11X-RAY DIFFRACTION11( CHAIN B AND RESID 296:373 )B296 - 373
12X-RAY DIFFRACTION12( CHAIN B AND RESID 374:401 )B374 - 401
13X-RAY DIFFRACTION13( CHAIN B AND RESID 402:438 )B402 - 438
14X-RAY DIFFRACTION14( CHAIN B AND RESID 503:503 )B503
15X-RAY DIFFRACTION15( CHAIN C AND RESID 1:197 )C1 - 197
16X-RAY DIFFRACTION16( CHAIN C AND RESID 198:440 )C198 - 440
17X-RAY DIFFRACTION17( CHAIN D AND RESID 1:88 )D1 - 88
18X-RAY DIFFRACTION18( CHAIN D AND RESID 89:295 )D89 - 295
19X-RAY DIFFRACTION19( CHAIN D AND RESID 296:401 )D296 - 401
20X-RAY DIFFRACTION20( CHAIN D AND RESID 402:441 )D402 - 441
21X-RAY DIFFRACTION21( CHAIN E AND RESID 6:46 )E6 - 46
22X-RAY DIFFRACTION22( CHAIN E AND RESID 47:143 )E47 - 143
23X-RAY DIFFRACTION23( CHAIN F AND RESID 1:66 )F1 - 66
24X-RAY DIFFRACTION24( CHAIN F AND RESID 67:198 )F67 - 198
25X-RAY DIFFRACTION25( CHAIN F AND RESID 199:380 )F199 - 380

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