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- PDB-4o2b: Tubulin-Colchicine complex -

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Basic information

Entry
Database: PDB / ID: 4o2b
TitleTubulin-Colchicine 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 / COLCHICINE / 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 / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / microtubule-based process / regulation of microtubule polymerization or depolymerization / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / microtubule cytoskeleton / neuron projection development / nervous system development / mitotic cell cycle / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytoplasm / cytosol
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; / 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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / Chem-LOC / DI(HYDROXYETHYL)ETHER / 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: 2.3 Å
AuthorsProta, A.E. / Franck, D. / Bachmann, F. / Bargsten, K. / Buey, R.M. / Pohlmann, J. / Reinelt, S. / Lane, H. / Steinmetz, M.O.
CitationJournal: J.Mol.Biol. / Year: 2014
Title: The Novel Microtubule-Destabilizing Drug BAL27862 Binds to the Colchicine Site of Tubulin with Distinct Effects on Microtubule Organization.
Authors: Prota, A.E. / Danel, F. / Bachmann, F. / Bargsten, K. / Buey, R.M. / Pohlmann, J. / Reinelt, S. / Lane, H. / Steinmetz, M.O.
History
DepositionDec 17, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 5, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 16, 2014Group: Database references
Revision 1.2Sep 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 / struct_ref_seq_dif / struct_site
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 / _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)266,92240
Polymers261,6316
Non-polymers5,29134
Water11,277626
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.310, 157.010, 180.220
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsTHE BIOLOGICAL ASSEMBLY IS CONTAINED IN THE ASYMMETRIC UNIT. THE BIOLOGICALLY RELEVANT TUBULIN-TTL-COMPLEX IS FORMED BY THE CHAINS A, B AND F. BIOMT1 1 1.000000 0.000000 0.000000 0.00000 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 BIOMT3 1 0.000000 0.000000 1.000000 0.00000

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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
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 , 11 types, 660 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-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / 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-LOC / N-[(7S)-1,2,3,10-tetramethoxy-9-oxo-6,7-dihydro-5H-benzo[d]heptalen-7-yl]ethanamide / COLCHICINE


Mass: 399.437 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C22H25NO6 / Comment: medication, antiinflammatory*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-PEG / DI(HYDROXYETHYL)ETHER


Mass: 106.120 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C4H10O3
#13: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H5N2
#14: 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
#15: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 626 / 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: 2.82 Å3/Da / Density % sol: 56.39 %
Crystal growTemperature: 293 K / pH: 6.7
Details: 6% PEG 4K, 4% glycerol, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES/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
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: 2.2→62.7 Å / Num. obs: 149841 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 13.6 % / Rmerge(I) obs: 0.115 / Net I/σ(I): 21.3
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 12.6 % / Rmerge(I) obs: 1.943 / Mean I/σ(I) obs: 1.7 / % possible all: 97.9

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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: PDB ENTRY 4I4T

4i4t


Resolution: 2.3→62.7 Å / SU ML: 0.27 / σ(F): 1.35 / Phase error: 23.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.213 1790 1.36 %
Rwork0.182 --
obs0.183 131603 100 %
all-150282 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.3→62.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17107 0 336 626 18069
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218074
X-RAY DIFFRACTIONf_angle_d0.65124550
X-RAY DIFFRACTIONf_dihedral_angle_d13.3426787
X-RAY DIFFRACTIONf_chiral_restr0.0442679
X-RAY DIFFRACTIONf_plane_restr0.0033175
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.36220.34751360.27149854X-RAY DIFFRACTION100
2.3622-2.43170.291370.25319902X-RAY DIFFRACTION100
2.4317-2.51020.26611350.23479884X-RAY DIFFRACTION100
2.5102-2.59990.28071370.22569914X-RAY DIFFRACTION100
2.5999-2.7040.28491360.22859878X-RAY DIFFRACTION100
2.704-2.82710.29761380.21389940X-RAY DIFFRACTION100
2.8271-2.97610.22281360.20189927X-RAY DIFFRACTION100
2.9761-3.16260.23471380.19349952X-RAY DIFFRACTION100
3.1626-3.40680.19011380.18699982X-RAY DIFFRACTION100
3.4068-3.74960.18721370.16999985X-RAY DIFFRACTION100
3.7496-4.2920.19971390.154810052X-RAY DIFFRACTION100
4.292-5.4070.17461390.145610132X-RAY DIFFRACTION100
5.407-62.74860.18841440.176810411X-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)
10.9713-0.1387-0.2392.54470.73952.30730.08040.08160.1637-0.34960.2169-0.3688-0.5790.3584-0.1940.4508-0.10180.11220.3949-0.16630.412631.526787.831351.8331
20.6957-0.3358-0.10561.95410.62292.16050.0385-0.05630.03380.30660.02680.0943-0.1849-0.0073-0.09320.40950.00970.05060.3672-0.13920.406719.12481.886966.0081
30.8188-0.14410.1712.32290.71211.6711-0.0416-0.14780.0750.68780.02040.3152-0.0990.07050.00570.53180.00480.1050.3697-0.10140.389618.920482.991373.5058
40.82120.2408-0.10121.32470.67561.7544-0.03340.0081-0.10850.36510.4078-0.42360.37110.8656-0.14170.36090.1311-0.07590.3857-0.17490.431832.868761.388760.5184
51.7741-0.25150.29590.72110.63541.38160.0106-0.1175-0.00060.21820.03950.0693-0.106-0.0738-0.03311.61280.29960.64951.10410.26651.117324.647763.871285.6124
61.9987-0.9245-0.60742.6348-0.2571.76690.16140.18170.3292-0.228-0.0276-0.0007-0.6798-0.0886-0.08880.40.02250.03580.3127-0.02260.347915.903369.681119.2592
70.6214-0.128-0.56441.38230.44870.98980.14150.2983-0.0406-0.4889-0.0182-0.164-0.3080.27-0.11850.3461-0.03220.05310.4757-0.12740.353528.879955.841514.4301
81.33390.0564-0.33072.25140.69282.2233-0.0534-0.06310.0231-0.10170.1196-0.1569-0.11610.2132-0.05440.18930.00970.02890.3077-0.1370.331224.220652.9225.9445
91.9041-0.5297-0.05640.7308-0.66691.0451-0.1135-0.2902-0.2085-0.01-0.14150.40980.2137-0.66740.13950.2572-0.08170.08150.5632-0.25730.45515.303750.489928.1961
101.0316-0.2884-0.25290.94190.99252.2940.0270.01420.1936-0.125-0.04650.0628-0.3566-0.2482-0.01460.28060.03230.03570.2953-0.12240.359710.431961.661835.844
111.8627-0.17360.34921.20370.24271.8072-0.0584-0.19270.14560.2601-0.04570.1449-0.112-0.5870.06190.3420.04270.07220.5071-0.17130.41176.291460.256544.7656
120.6352-0.9872-0.43151.41.47272.023-0.03370.0609-0.20210.6076-0.32940.73110.5961-0.32110.08130.3182-0.02330.07110.3038-0.10320.364315.396441.757834.0399
130.2710.1206-0.02682.03721.23842.6175-0.069-0.1418-0.16170.55710.164-0.06590.66980.7176-0.0510.30750.029-0.02780.3505-0.06370.346425.816537.918131.2318
140.51540.38020.01392.16720.56470.1612-0.3413-0.1857-0.1718-0.3058-0.2926-0.1414-0.1891-0.07130.05140.26450.03420.03270.3937-0.16750.488216.978265.984543.403
151.3268-0.3593-0.13492.11120.18291.82820.00510.15780.1498-0.23680.0685-0.0741-0.17170.1006-0.0580.2317-0.06240.03860.3021-0.03130.255220.315532.6553-12.0475
160.84-0.4227-0.07021.40950.99221.6115-0.0155-0.03610.08210.1062-0.07840.10820.0865-0.22490.06690.2268-0.06730.04750.2687-0.03710.28977.72625.79283.0776
172.3634-0.161-0.22031.3961-0.10541.3999-0.07510.97970.2427-0.43360.18540.12080.0628-0.452-0.08310.5807-0.12770.0480.8593-0.01050.316717.2099.3848-44.3045
181.6490.1794-0.56461.6520.16182.4308-0.18680.558-0.1584-0.36430.2094-0.22850.3553-0.0065-0.11910.4868-0.07460.06660.5134-0.19270.339221.1714-2.3677-33.7389
191.6340.0295-0.70081.34660.10712.4113-0.19060.3123-0.25450.02760.19170.15760.4407-0.3580.06110.4297-0.1080.04210.3829-0.1130.3159.1722-4.2645-21.3534
201.7784-0.1378-1.00391.27890.34011.6363-0.0712-0.0495-0.60590.04790.0696-0.2370.47510.457-0.27480.69360.09650.08820.5055-0.2520.591130.5865-16.5238-24.1263
211.3314-0.00970.26022.13210.49110.24410.14110.08110.32370.07950.0917-0.22070.0625-0.0021-0.02020.4322-0.04730.03230.292-0.12260.387913.64618.646-19.9579
221.8988-0.6578-0.10091.08710.38930.62570.0367-0.30840.16770.7470.2388-0.63010.22641.0692-0.12711.1186-0.0517-0.00590.656-0.18480.556827.712492.180982.0169
230.3514-0.1637-0.37880.08690.05170.335-0.0988-0.02930.00850.34560.4265-0.3610.55280.69330.06150.36950.09010.02570.6327-0.26490.583542.742228.5834.7647
241.66190.6648-0.88842.0986-0.15350.8007-0.42440.7037-0.5521-0.09240.025-0.16851.4112-0.49690.19711.1134-0.20490.18640.6788-0.16590.58866.230354.076969.7951
251.02710.0782-0.21131.38770.10892.0489-0.0948-0.8668-0.6790.4015-0.2711-0.76120.46731.44140.11690.72770.2021-0.0571.0470.25680.714314.014258.077104.7039
262.32040.5246-2.0640.91410.06131.95-0.48350.0634-0.61850.04980.2339-0.05161.0589-0.0371-0.08040.95760.02260.15760.40740.05690.5641-2.014353.251293.2293
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1:180 )
2X-RAY DIFFRACTION2(CHAIN A AND RESID 181:311 )
3X-RAY DIFFRACTION3(CHAIN A AND RESID 312:401 )
4X-RAY DIFFRACTION4(CHAIN A AND RESID 402:436 )
5X-RAY DIFFRACTION5(CHAIN A AND RESID 437:439 )
6X-RAY DIFFRACTION6(CHAIN B AND RESID 1:88 )
7X-RAY DIFFRACTION7(CHAIN B AND RESID 89:127 )
8X-RAY DIFFRACTION8(CHAIN B AND RESID 128:197 )
9X-RAY DIFFRACTION9(CHAIN B AND RESID 198:223 )
10X-RAY DIFFRACTION10(CHAIN B AND RESID 224:295 )
11X-RAY DIFFRACTION11(CHAIN B AND RESID 296:373 )
12X-RAY DIFFRACTION12(CHAIN B AND RESID 374:401 )
13X-RAY DIFFRACTION13(CHAIN B AND RESID 402:438 )
14X-RAY DIFFRACTION14(CHAIN B AND RESID 503:503 )
15X-RAY DIFFRACTION15(CHAIN C AND RESID 1:197 )
16X-RAY DIFFRACTION16(CHAIN C AND RESID 198:440 )
17X-RAY DIFFRACTION17(CHAIN D AND RESID 1:88 )
18X-RAY DIFFRACTION18(CHAIN D AND RESID 89:295 )
19X-RAY DIFFRACTION19(CHAIN D AND RESID 296:401 )
20X-RAY DIFFRACTION20(CHAIN D AND RESID 402:441 )
21X-RAY DIFFRACTION21(CHAIN D AND RESID 503:503 )
22X-RAY DIFFRACTION22(CHAIN E AND RESID 6:46 )
23X-RAY DIFFRACTION23(CHAIN E AND RESID 47:141 )
24X-RAY DIFFRACTION24(CHAIN F AND RESID 1:66 )
25X-RAY DIFFRACTION25(CHAIN F AND RESID 67:198 )
26X-RAY DIFFRACTION26(CHAIN F AND RESID 199:378 )

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