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- PDB-5lxs: Tubulin-KS-1-199-32 complex -

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Basic information

Entry
Database: PDB / ID: 5lxs
TitleTubulin-KS-1-199-32 complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin tyrosine ligase
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 / structural constituent of cytoskeleton ...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 / structural constituent of cytoskeleton / protein modification process / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / growth cone / microtubule cytoskeleton / 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 / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / 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 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / 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; / 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 / Dna Ligase; domain 1 / 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
Chem-7AO / 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: 2.2 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 1.0Sep 20, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 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 1.2Jan 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)266,13823
Polymers261,6316
Non-polymers4,50717
Water16,412911
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22660 Å2
ΔGint-167 kcal/mol
Surface area80990 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.580, 157.800, 179.440
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, 928 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-7AO / [(3~{Z},5~{S},6~{S},7~{S},8~{R},9~{S},11~{Z},13~{S},14~{S},15~{S},16~{Z},18~{S})-19-[(2~{S},3~{R},4~{S},5~{R})-3,5-dimethyl-4-oxidanyl-6-oxidanylidene-oxan-2-yl]-5,7,9,11,13,15-hexamethyl-8,14,18-tris(oxidanyl)nonadeca-1,3,11,16-tetraen-6-yl] ~{N}-[3-[(3-azidophenyl)carbonylamino]propyl]carbamate


Mass: 796.004 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C43H65N5O9
#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-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.: 911 / 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: 56.53 %
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: 2.2→72.226 Å / Num. obs: 150705 / % possible obs: 100 % / Redundancy: 13.3 % / CC1/2: 0.998 / Rmerge(I) obs: 0.229 / Net I/σ(I): 12.5
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 12.9 % / Rmerge(I) obs: 4.116 / CC1/2: 0.309 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(dev_2875: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.2→72.226 Å / SU ML: 0.33 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 25.02 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2269 7568 5.02 %
Rwork0.1865 --
obs0.1885 150703 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.2→72.226 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17429 0 286 911 18626
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00318370
X-RAY DIFFRACTIONf_angle_d0.61524986
X-RAY DIFFRACTIONf_dihedral_angle_d10.58211078
X-RAY DIFFRACTIONf_chiral_restr0.0432721
X-RAY DIFFRACTIONf_plane_restr0.0043239
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.2250.38292370.35824764X-RAY DIFFRACTION100
2.225-2.25110.36582430.33244708X-RAY DIFFRACTION100
2.2511-2.27860.35312530.32224736X-RAY DIFFRACTION100
2.2786-2.30740.34592550.31454703X-RAY DIFFRACTION100
2.3074-2.33780.34422480.29724726X-RAY DIFFRACTION100
2.3378-2.36980.3312290.2974744X-RAY DIFFRACTION100
2.3698-2.40370.31892740.27954694X-RAY DIFFRACTION100
2.4037-2.43960.3312600.27814745X-RAY DIFFRACTION100
2.4396-2.47770.31982400.27234690X-RAY DIFFRACTION100
2.4777-2.51830.31182410.26084752X-RAY DIFFRACTION100
2.5183-2.56170.27952670.23794769X-RAY DIFFRACTION100
2.5617-2.60830.29382340.23354707X-RAY DIFFRACTION100
2.6083-2.65850.28092440.23074754X-RAY DIFFRACTION100
2.6585-2.71280.2842280.22764761X-RAY DIFFRACTION100
2.7128-2.77170.2852660.21834737X-RAY DIFFRACTION100
2.7717-2.83620.28182590.21444749X-RAY DIFFRACTION100
2.8362-2.90720.252450.20624762X-RAY DIFFRACTION100
2.9072-2.98580.25732470.2054756X-RAY DIFFRACTION100
2.9858-3.07360.24192290.1964772X-RAY DIFFRACTION100
3.0736-3.17280.23472820.18944745X-RAY DIFFRACTION100
3.1728-3.28620.23832460.18354753X-RAY DIFFRACTION100
3.2862-3.41780.23742460.17234774X-RAY DIFFRACTION100
3.4178-3.57330.1832860.16674777X-RAY DIFFRACTION100
3.5733-3.76170.18942640.15354769X-RAY DIFFRACTION100
3.7617-3.99740.18332140.14194835X-RAY DIFFRACTION100
3.9974-4.3060.16782580.13244819X-RAY DIFFRACTION100
4.306-4.73930.14632800.11824824X-RAY DIFFRACTION100
4.7393-5.42480.17352790.13574826X-RAY DIFFRACTION100
5.4248-6.83390.21442430.16664901X-RAY DIFFRACTION100
6.8339-72.26520.20472710.16325083X-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)
11.2298-0.2281-0.37973.35890.91912.03160.11040.02340.2128-0.21080.0791-0.167-0.54920.1688-0.16450.4131-0.03780.07050.3218-0.10040.312532.149588.11851.5355
21.7354-0.1682-0.37512.7010.5342.6950.1515-0.0310.18320.2561-0.06810.1529-0.2698-0.0551-0.05870.34760.00790.04520.2687-0.08530.288820.132782.070465.3269
30.80730.08780.03593.57121.19013.05630.0377-0.14710.19370.7378-0.01480.2572-0.2609-0.0809-0.04880.3771-0.03660.12890.3516-0.09440.357919.088683.465873.0513
42.5266-0.2825-0.22174.74593.70365.11060.0559-0.1376-0.09880.50350.1328-0.21320.50990.4529-0.12940.3060.0779-0.02470.2491-0.07170.357132.714961.877760.8988
55.199-1.65-0.87756.68530.99123.66040.15750.4210.6799-0.4691-0.14890.2351-0.8586-0.33950.04270.3990.0663-0.01110.32320.00950.349915.931169.835518.9202
62.4422-0.6817-1.19747.7969-1.02223.97470.15010.31510.0769-0.5545-0.0748-0.3453-0.28470.1259-0.07620.2443-0.01980.04440.371-0.07360.248529.088156.117714.2596
72.88741.47880.49786.36781.58443.4471-0.0359-0.08740.12570.0501-0.07930.1071-0.1764-0.00730.09750.21840.02410.02380.2931-0.07090.240824.547853.008825.9888
82.9261-0.72983.40761.2978-0.57374.2983-0.3533-0.3986-0.5805-0.12490.08360.55830.3276-0.88680.33780.3796-0.06520.08220.576-0.25460.54465.264150.955128.258
92.9045-1.129-0.01661.51240.57492.0046-0.0877-0.03740.0389-0.1292-0.05030.2316-0.3158-0.49590.11950.30670.05440.00470.4084-0.13320.37458.794761.75735.0704
104.1821-2.09551.97542.852-1.65774.4448-0.2567-0.27970.01840.3145-0.00410.2662-0.3029-1.15670.19540.36810.0270.00690.6483-0.20910.44286.492460.650144.4446
112.0567-2.2461-0.86043.04612.54253.8016-0.0331-0.0303-0.13330.5337-0.13990.35550.6175-0.29730.21450.3484-0.06750.08090.2987-0.05790.290215.619141.990234.0529
121.4392-0.9393-1.17783.7814.34719.14830.0134-0.2615-0.20140.8180.1057-0.24810.89460.5413-0.14960.4203-0.0325-0.06610.31870.00040.302525.871937.890330.8291
131.3208-0.40250.01662.96790.32841.596-0.00040.12920.1288-0.21170.08760.0131-0.2490.1427-0.06980.2471-0.07270.02750.2909-0.04250.249820.180432.8435-12.0279
140.7955-0.33290.13271.36540.89141.5922-0.0084-0.02820.06890.1207-0.06890.1338-0.007-0.20150.07010.2211-0.04370.03890.2632-0.04230.26877.694825.96653.1723
154.1653-2.0219-0.47115.72941.51353.6083-0.05080.74970.1201-0.73710.1770.1308-0.1742-0.0406-0.10840.3608-0.1466-0.01330.58960.0030.230717.00899.516-44.4601
161.29450.0543-0.23681.59410.14322.0009-0.08430.3672-0.1472-0.23970.1713-0.07610.18350.0647-0.07620.3009-0.0367-0.00350.4242-0.11740.267319.3399-2.5067-33.8836
171.7747-0.1911-0.39731.93970.56762.574-0.14240.2726-0.15460.08890.13190.10060.2286-0.14510.05140.2801-0.0598-0.01150.3071-0.0620.25938.9419-4.1009-21.4204
183.2579-1.2423-2.85732.93820.90774.4296-0.3814-0.1046-0.69580.13910.1246-0.18580.90070.64470.0380.40960.1065-0.03960.4832-0.22620.542430.267-16.5232-24.5318
193.7269-3.8771-0.52465.18691.27050.5529-0.2113-0.33090.3711.09110.4445-0.57090.19840.4835-0.19470.911-0.1161-0.02710.5931-0.22230.568727.64193.324581.2946
200.0612-0.1656-0.19672.46652.57183.02690.04080.085-0.06220.16490.4695-0.5580.28160.5789-0.61490.31940.02220.01920.6044-0.24250.544642.995127.68723.7401
211.46272.02390.2453.77420.64530.3564-0.6450.6648-0.7053-0.48640.0874-0.34641.4909-0.291-0.06841.0954-0.23990.18940.5254-0.21240.49436.739654.57869.5301
222.10010.56420.34363.0976-0.33781.89890.0987-0.8637-0.4610.5528-0.4942-0.95510.44061.48260.30320.64470.1659-0.08131.08050.22280.659315.461458.325105.3295
231.96990.6981-1.7411.2285-0.05831.908-0.3830.0777-0.52760.03720.1818-0.0190.8812-0.06830.01850.69210.00630.08060.28450.02120.4605-1.014454.21793.2563
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 180)
2X-RAY DIFFRACTION2chain 'A' and (resid 181 through 311)
3X-RAY DIFFRACTION3chain 'A' and (resid 312 through 401)
4X-RAY DIFFRACTION4chain 'A' and (resid 402 through 437)
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 88)
6X-RAY DIFFRACTION6chain 'B' and (resid 89 through 127)
7X-RAY DIFFRACTION7chain 'B' and (resid 128 through 197)
8X-RAY DIFFRACTION8chain 'B' and (resid 198 through 223)
9X-RAY DIFFRACTION9chain 'B' and (resid 224 through 295)
10X-RAY DIFFRACTION10chain 'B' and (resid 296 through 373)
11X-RAY DIFFRACTION11chain 'B' and (resid 374 through 401)
12X-RAY DIFFRACTION12chain 'B' and (resid 402 through 438)
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 197)
14X-RAY DIFFRACTION14chain 'C' and (resid 198 through 440)
15X-RAY DIFFRACTION15chain 'D' and (resid 2 through 88)
16X-RAY DIFFRACTION16chain 'D' and (resid 89 through 295)
17X-RAY DIFFRACTION17chain 'D' and (resid 296 through 401)
18X-RAY DIFFRACTION18chain 'D' and (resid 402 through 441)
19X-RAY DIFFRACTION19chain 'E' and (resid 6 through 46)
20X-RAY DIFFRACTION20chain 'E' and (resid 47 through 143)
21X-RAY DIFFRACTION21chain 'F' and (resid 1 through 66)
22X-RAY DIFFRACTION22chain 'F' and (resid 67 through 198)
23X-RAY DIFFRACTION23chain 'F' and (resid 199 through 381)

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