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- PDB-5lxt: Tubulin-Discodermolide complex -

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Basic information

Entry
Database: PDB / ID: 5lxt
TitleTubulin-Discodermolide complex
Components
  • Stathmin-4
  • TUBULIN-TYROSINE LIGASE
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE / DISCODERMOLIDE
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
(+)-Discodermolide / 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: 1.9 Å
AuthorsProta, A.E. / Steinmetz, M.O.
Funding support Switzerland, Spain, United States, 4items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_138659 and 31003A_166608 Switzerland
Spanish Ministry of Economy and CompetitivenessBIO2013-42984-R and S2010/BMD-2457 BIPEDD2 Spain
National Institutes of Health/National Cancer Institute (NIH/NCI)CA077263 United States
Breast Cancer Research Foundation United States
CitationJournal: Chembiochem / Year: 2017
Title: Structural Basis of Microtubule Stabilization by Discodermolide.
Authors: Prota, A.E. / Bargsten, K. / Redondo-Horcajo, M. / Smith, A.B. / Yang, C.H. / McDaid, H.M. / Paterson, I. / Horwitz, S.B. / Fernando Diaz, J. / Steinmetz, M.O.
History
DepositionSep 22, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 1, 2017Provider: repository / Type: Initial release
Revision 1.1Jun 7, 2017Group: Database references
Revision 1.2Sep 13, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Mar 30, 2022Group: Author supporting evidence / Database references / Derived calculations
Category: database_2 / pdbx_audit_support ...database_2 / pdbx_audit_support / 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_audit_support.funding_organization / _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
Revision 1.4Jan 17, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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)265,73423
Polymers261,6316
Non-polymers4,10317
Water28,2301567
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23020 Å2
ΔGint-152 kcal/mol
Surface area80950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.500, 157.790, 180.230
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) / 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) / 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 , 8 types, 1584 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-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-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#10: Chemical ChemComp-7AK / (+)-Discodermolide


Mass: 593.792 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C33H55NO8
#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.: 1567 / 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: 2.9 Å3/Da / Density % sol: 57.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion
Details: 0-3% PEG, 1-6% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole
PH range: 6.7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Sep 12, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.9→52.25 Å / Num. obs: 233651 / % possible obs: 100 % / Redundancy: 13.3 % / CC1/2: 1 / Rmerge(I) obs: 0.106 / Net I/σ(I): 18.7
Reflection shellResolution: 1.9→1.95 Å / Redundancy: 12.5 % / Rmerge(I) obs: 3.209 / Mean I/σ(I) obs: 0.9 / CC1/2: 0.33 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 1.9→52.25 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 22.37
RfactorNum. reflection% reflection
Rfree0.208 11712 5.01 %
Rwork0.1729 --
obs0.1747 233651 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.9→52.25 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17497 0 256 1567 19320
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00518460
X-RAY DIFFRACTIONf_angle_d0.91225122
X-RAY DIFFRACTIONf_dihedral_angle_d14.0966902
X-RAY DIFFRACTIONf_chiral_restr0.0372769
X-RAY DIFFRACTIONf_plane_restr0.0043260
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8999-1.92150.34713680.3427292X-RAY DIFFRACTION99
1.9215-1.94410.34913890.32697308X-RAY DIFFRACTION100
1.9441-1.96790.34493640.30897389X-RAY DIFFRACTION100
1.9679-1.99280.31913960.29347281X-RAY DIFFRACTION100
1.9928-2.0190.29344030.27677337X-RAY DIFFRACTION100
2.019-2.04670.29594130.2617344X-RAY DIFFRACTION100
2.0467-2.07590.28114060.24927324X-RAY DIFFRACTION100
2.0759-2.10690.26634160.24017302X-RAY DIFFRACTION100
2.1069-2.13980.26133610.22327379X-RAY DIFFRACTION100
2.1398-2.17490.26143910.21547349X-RAY DIFFRACTION100
2.1749-2.21240.25534080.21267292X-RAY DIFFRACTION100
2.2124-2.25260.23273690.27413X-RAY DIFFRACTION100
2.2526-2.29590.22493940.19197299X-RAY DIFFRACTION100
2.2959-2.34280.22743850.19167400X-RAY DIFFRACTION100
2.3428-2.39370.22683700.1857409X-RAY DIFFRACTION100
2.3937-2.44940.22574080.17327320X-RAY DIFFRACTION100
2.4494-2.51070.22414010.17587365X-RAY DIFFRACTION100
2.5107-2.57860.23543680.17267409X-RAY DIFFRACTION100
2.5786-2.65440.22433850.17027347X-RAY DIFFRACTION100
2.6544-2.74010.21043660.17267461X-RAY DIFFRACTION100
2.7401-2.8380.21493550.16987406X-RAY DIFFRACTION100
2.838-2.95170.21844090.17087370X-RAY DIFFRACTION100
2.9517-3.0860.20683830.16497434X-RAY DIFFRACTION100
3.086-3.24870.21983880.16817433X-RAY DIFFRACTION100
3.2487-3.45220.19434080.15997426X-RAY DIFFRACTION100
3.4522-3.71860.18344090.157438X-RAY DIFFRACTION100
3.7186-4.09270.16543990.13517475X-RAY DIFFRACTION100
4.0927-4.68460.15833910.12717526X-RAY DIFFRACTION100
4.6846-5.90080.17014000.14757580X-RAY DIFFRACTION100
5.9008-52.26970.19774090.17257831X-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)
11.2182-0.5466-0.12183.64591.13912.22440.05510.14730.2148-0.35860.1243-0.3039-0.61340.2892-0.16360.4481-0.08960.10060.3566-0.09360.315931.819588.33251.7332
21.0229-0.1782-0.32642.6761.02562.64580.0884-0.00760.06490.1908-0.04780.1887-0.1896-0.1063-0.03950.31640.00020.05290.2536-0.08360.262819.235582.465865.5976
30.8702-0.3375-0.05824.03151.39352.1982-0.0204-0.1480.15520.54660.05120.1462-0.1556-0.0076-0.03650.3733-0.01710.08230.3132-0.08040.298518.722183.496373.1545
41.8297-0.2774-0.71623.53922.63054.3144-0.0175-0.1074-0.15150.57040.2618-0.28720.63550.694-0.19160.30440.0885-0.04180.2851-0.11230.355832.832161.896160.4302
54.7367-2.807-0.5771.70920.66642.35670.1714-0.3302-0.78990.11340.3970.68020.59410.7577-0.49661.891-0.02330.54240.79640.05751.106515.033755.167486.3168
64.166-1.7057-0.96286.43581.76473.59240.13390.2410.7277-0.3629-0.14360.1419-0.795-0.19330.03950.35320.040.00330.2746-0.01330.400916.260169.988219.1554
72.0315-0.07-0.62825.83450.27841.84130.00170.31190.0859-0.36940.1732-0.3976-0.29840.2058-0.16590.262-0.02480.03960.4203-0.06840.261529.056756.164714.3873
81.33430.85110.39744.07271.51752.83390.0051-0.16960.14610.02410.004-0.0642-0.16860.1431-0.01590.16340.00570.04060.2658-0.10780.257724.350253.136325.9396
91.6212-1.08371.12980.7904-0.99971.6685-0.1119-0.3329-0.097-0.0466-0.15590.4970.142-0.65770.25240.2752-0.05690.07510.5346-0.26570.50355.188451.088328.0538
101.7724-0.56580.1871.06880.72831.9871-0.0574-0.10330.1121-0.0698-0.06540.2779-0.2651-0.51170.07840.26680.02070.02590.3825-0.12860.39999.476961.957735.2227
112.7452-1.21350.82542.2656-0.40742.635-0.2478-0.3081-0.00150.3302-0.05150.4183-0.1396-1.13170.26180.41370.06860.05090.6887-0.22430.4886.489360.940344.5806
121.6182-1.8921-1.40243.86283.68184.1558-0.109-0.0889-0.09450.50660.00120.35120.592-0.11570.15170.3032-0.0460.05150.2757-0.07510.272215.398142.110534.0751
131.1842-0.8461-0.57683.88453.28342.8244-0.0686-0.211-0.1750.74390.0476-0.08730.8290.54380.00510.321-0.0199-0.03410.3267-0.03170.268525.667537.968230.8992
141.3012-0.11580.0392.11580.38261.527-0.0230.12490.1325-0.20370.105-0.039-0.19370.1621-0.07650.2072-0.06320.03590.2573-0.03930.232320.257832.9631-11.9587
150.9522-0.41490.13571.60260.84761.4673-0.0031-0.02390.03540.1357-0.06450.16060.0564-0.20350.05070.1668-0.05420.04380.2222-0.03180.23287.619126.16113.0649
163.396-1.2074-0.30474.5951.19714.0216-0.06880.83910.1784-0.62820.15410.0872-0.1439-0.1962-0.05630.3994-0.11890.01510.645-0.00860.234517.15439.8064-44.08
171.2237-0.0317-0.33191.58080.35072.5463-0.11060.4608-0.1448-0.32230.1715-0.12930.2736-0.0406-0.07890.3715-0.05210.01750.4729-0.15770.293120.2447-2.3394-33.7248
182.0016-0.0799-0.76041.56890.28112.1895-0.17710.3825-0.2390.00030.11810.19690.311-0.2550.07340.3335-0.0935-0.01310.3687-0.10140.26668.8587-3.8827-21.3308
193.0285-1.1024-2.35323.12461.26654.3883-0.20220.0949-0.71210.04260.112-0.30460.72480.4021-0.1450.540.09730.01330.4435-0.23560.578830.0371-16.4529-24.3384
203.1569-0.7996-0.36583.55291.15592.42880.0333-0.42260.20691.00690.1957-0.0196-0.07310.5009-0.23510.7979-0.0652-0.05280.4981-0.13160.456427.167893.314581.4322
210.17390.033-0.0827-0.0439-0.00180.4168-0.10110.0596-0.07660.23680.6486-0.49550.37020.9209-0.59460.3280.07640.00980.6336-0.2730.556142.841827.72253.8164
221.35431.7805-0.03184.24780.45630.8188-0.41240.5076-0.6399-0.31510.0558-0.26141.3271-0.2141-0.090.9161-0.14050.17970.4522-0.19530.49366.268754.733269.6779
232.20160.08020.30343.382-0.86132.852-0.1045-0.8748-0.40050.7555-0.3491-1.07130.31211.72890.39330.75740.154-0.14341.14080.25970.776415.724858.2872105.0389
242.61840.7289-2.15791.7503-0.60294.1517-0.3872-0.0579-0.69270.20940.1297-0.07110.741-0.0767-0.10240.66380.01680.10070.22980.04080.497-1.781854.594693.5573
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 437:450)
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 47:143)
22X-RAY DIFFRACTION22chain 'F' and (resseq 1:66)
23X-RAY DIFFRACTION23chain 'F' and (resseq 67:198)
24X-RAY DIFFRACTION24chain 'F' and (resseq 199:384)

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