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- PDB-5lov: DZ-2384 tubulin complex -

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Basic information

Entry
Database: PDB / ID: 5lov
TitleDZ-2384 tubulin complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE
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
DZ 2384 / 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: 2.4 Å
AuthorsProta, A.E. / Steinmetz, M.O. / Shore, G.C. / Brouhard, G. / Roulston, A.
Funding support Canada, 4items
OrganizationGrant numberCountry
CQDMMOP-6192 Canada
CIHRMOP-137055 Canada
CIHRMOP-106530 Canada
CIHRMOP-119401 Canada
CitationJournal: Sci Transl Med / Year: 2016
Title: The synthetic diazonamide DZ-2384 has distinct effects on microtubule curvature and dynamics without neurotoxicity.
Authors: Wieczorek, M. / Tcherkezian, J. / Bernier, C. / Prota, A.E. / Chaaban, S. / Rolland, Y. / Godbout, C. / Hancock, M.A. / Arezzo, J.C. / Ocal, O. / Rocha, C. / Olieric, N. / Hall, A. / Ding, H. ...Authors: Wieczorek, M. / Tcherkezian, J. / Bernier, C. / Prota, A.E. / Chaaban, S. / Rolland, Y. / Godbout, C. / Hancock, M.A. / Arezzo, J.C. / Ocal, O. / Rocha, C. / Olieric, N. / Hall, A. / Ding, H. / Bramoulle, A. / Annis, M.G. / Zogopoulos, G. / Harran, P.G. / Wilkie, T.M. / Brekken, R.A. / Siegel, P.M. / Steinmetz, M.O. / Shore, G.C. / Brouhard, G.J. / Roulston, A.
History
DepositionAug 10, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 30, 2016Provider: repository / Type: Initial release
Revision 1.1Jan 10, 2024Group: 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
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.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_conn.ptnr2_label_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)265,02317
Polymers261,6316
Non-polymers3,39211
Water2,432135
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22820 Å2
ΔGint-124 kcal/mol
Surface area78660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.160, 154.700, 180.320
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, 146 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.: 3 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 1 / 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-71E / DZ 2384 / optimized synthetic derivative of diazonamide AB-5


Mass: 645.677 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H36FN5O7
#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.: 135 / 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: 2.75 Å3/Da / Density % sol: 55.27 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 4-10% PEG 4000, 4-6% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 100 mM MES/Imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 22, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→77.35 Å / Num. obs: 112935 / % possible obs: 99.8 % / Redundancy: 13.6 % / CC1/2: 1 / Rmerge(I) obs: 0.11 / Net I/σ(I): 18.6
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 13.5 % / Rmerge(I) obs: 4.07 / Mean I/σ(I) obs: 0.75 / CC1/2: 0.33 / % possible all: 99.7

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XSCALEdata scaling
PHENIX1.9_1692phasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.4→77.35 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 29.37
RfactorNum. reflection% reflection
Rfree0.2415 5650 5 %
Rwork0.1883 --
obs0.1911 112921 99.75 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.4→77.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16832 0 214 135 17181
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00417531
X-RAY DIFFRACTIONf_angle_d0.78823814
X-RAY DIFFRACTIONf_dihedral_angle_d15.0016501
X-RAY DIFFRACTIONf_chiral_restr0.032613
X-RAY DIFFRACTIONf_plane_restr0.0033072
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4-2.42730.3831860.37943502X-RAY DIFFRACTION100
2.4273-2.45580.36141880.33353574X-RAY DIFFRACTION100
2.4558-2.48580.3831850.33053507X-RAY DIFFRACTION100
2.4858-2.51730.37611900.32953599X-RAY DIFFRACTION100
2.5173-2.55040.40241840.30953485X-RAY DIFFRACTION100
2.5504-2.58530.32461870.29353564X-RAY DIFFRACTION100
2.5853-2.62230.361860.28373532X-RAY DIFFRACTION100
2.6223-2.66140.33961870.28923536X-RAY DIFFRACTION100
2.6614-2.7030.37791850.28913536X-RAY DIFFRACTION100
2.703-2.74730.33541850.27173537X-RAY DIFFRACTION100
2.7473-2.79470.311870.25733549X-RAY DIFFRACTION100
2.7947-2.84550.29621860.24923534X-RAY DIFFRACTION99
2.8455-2.90020.35131860.25523511X-RAY DIFFRACTION99
2.9002-2.95940.30251880.24373584X-RAY DIFFRACTION100
2.9594-3.02380.30431870.22513541X-RAY DIFFRACTION100
3.0238-3.09410.2771880.21063558X-RAY DIFFRACTION100
3.0941-3.17150.31361880.22773573X-RAY DIFFRACTION100
3.1715-3.25730.3181880.21833570X-RAY DIFFRACTION100
3.2573-3.35310.28181890.21063581X-RAY DIFFRACTION100
3.3531-3.46130.27171880.20133565X-RAY DIFFRACTION100
3.4613-3.58510.2691890.19453594X-RAY DIFFRACTION100
3.5851-3.72860.22271880.18723566X-RAY DIFFRACTION100
3.7286-3.89830.21471890.1683585X-RAY DIFFRACTION100
3.8983-4.10380.22091900.15823609X-RAY DIFFRACTION100
4.1038-4.36090.21931880.15723571X-RAY DIFFRACTION99
4.3609-4.69760.20821900.13833637X-RAY DIFFRACTION100
4.6976-5.17020.17551920.14773641X-RAY DIFFRACTION100
5.1702-5.91810.22521900.16383628X-RAY DIFFRACTION100
5.9181-7.45520.2281940.17313685X-RAY DIFFRACTION100
7.4552-77.39020.17952020.15973817X-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)
12.0614-0.2113-0.93633.55161.50833.13490.11060.21970.0999-0.60720.1575-0.3024-0.56120.3195-0.24080.6409-0.0240.08340.5623-0.12260.51629.920686.635451.0835
21.3136-1.112-0.7894.44171.80434.39990.0483-0.06430.11330.3833-0.03830.2975-0.0305-0.1384-0.02350.54540.0640.08190.5427-0.11480.55518.180280.102265.3453
31.0559-0.6464-0.2494.56121.9831.9504-0.0512-0.20490.19670.67710.04020.33080.1876-0.15140.04320.78440.03840.12840.6864-0.13610.601817.965281.184972.918
42.18260.5887-0.68322.70431.90176.5387-0.272-0.2814-0.21040.63610.1671-0.60990.60190.80960.13980.6350.2193-0.13750.6861-0.09770.688832.986860.618760.0303
51.64860.1542-0.25431.57570.69770.5679-0.12820.6989-0.0691-0.1632-0.1054-0.30610.155-0.090.18350.59010.11310.08850.4689-0.12460.750622.469872.469654.1988
63.8988-1.3836-0.9273.9230.0053.16790.10850.23980.767-0.7115-0.280.7026-0.9155-0.63070.1340.96370.2148-0.15710.6652-0.09560.857813.942166.592119.1641
72.96110.09410.47473.77940.763.68080.1080.24240.1891-0.7315-0.0542-0.2724-0.90940.3634-0.03710.90110.02340.07140.7583-0.03790.598527.972254.165313.919
82.00911.5315-0.05643.42130.62643.8555-0.0552-0.28340.1769-0.21530.0184-0.0034-0.40670.12930.03060.46140.04060.030.5287-0.10740.484424.163350.872325.945
96.4621-0.38471.69562.5837-0.31113.0226-0.3094-1.1639-0.0858-0.2174-0.20260.6833-0.0787-1.30990.58660.56040.07280.01370.8713-0.23770.58885.101547.25229.1945
101.56630.51330.80130.7890.42831.81630.1040.06430.1298-0.004-0.38070.479-0.3884-0.20520.23210.5790.1494-0.01010.6591-0.30010.739911.291158.216536.1089
113.10440.15640.19223.55461.02981.685-0.0395-0.0205-0.13560.5875-0.31231.1676-0.0627-1.04370.35840.79310.04540.10490.9725-0.26230.7526.324956.831945.0171
121.8966-0.7778-1.10582.50152.48884.3761-0.2281-0.3025-0.06080.7458-0.14450.67080.8548-0.25070.27330.5164-0.0250.04410.6965-0.12250.528716.994839.056934.2879
131.6050.0734-1.06642.59821.63483.2122-0.0685-0.0783-0.27020.71260.0185-0.16630.66740.40990.0360.69220.0198-0.0290.5648-0.01240.586126.295136.879728.5181
141.5506-0.4614-0.49313.16130.3441.7813-0.06870.32690.1314-0.25770.0303-0.034-0.21190.10570.04150.4197-0.1129-0.00010.5749-0.0250.458721.450531.6964-12.3775
151.5161-0.3736-0.30092.04731.25582.6063-0.05910.0411-0.00390.0236-0.010.2797-0.0164-0.23180.06580.3721-0.08430.01190.4285-0.00960.41339.343625.06923.0571
163.543-0.8895-0.2683.4793-0.06521.8092-0.09960.66750.0601-0.55880.0499-0.02780.1134-0.06160.03650.9251-0.1480.08241.2732-0.14790.584517.35648.2213-44.1598
172.0589-0.0632-0.371.71450.26612.2049-0.070.6403-0.3518-0.43340.121-0.210.3320.1721-0.05620.7898-0.06230.09880.8505-0.27810.678221.0087-3.6323-33.6996
181.81980.22250.20131.46970.6242.3683-0.23690.5274-0.38140.01020.15280.04450.4011-0.14360.10030.6405-0.14130.09420.7094-0.16820.6179.2068-4.9329-21.0904
193.6674-0.8918-2.20841.8370.11053.7983-0.3940.1441-0.92980.37580.2537-0.1171.45241.17590.05281.12660.1367-0.00121.0758-0.39291.075330.1544-17.8199-24.4295
203.462-0.3756-1.19150.69130.82522.3613-0.0619-0.49840.88730.16910.4865-0.34670.11290.4485-0.4481.1394-0.0998-0.00470.9899-0.32310.862126.40792.068879.4898
210.1093-0.4752-0.61693.89874.32545.0363-0.1128-0.0265-0.08890.68270.5317-0.33970.84760.7477-0.53930.67780.04890.00850.958-0.25630.8443.257827.52674.4036
223.2670.346-1.21653.74960.67022.8274-0.55770.3503-0.75620.41180.40250.0031.168-0.2130.16311.3366-0.10220.24980.8599-0.17091.0076.465852.098569.7296
232.39560.1781-1.04353.8061-1.09153.78460.0582-0.9249-0.48680.588-0.3113-0.9640.2061.29350.22151.08770.1681-0.11171.21190.17411.094213.822156.983104.8125
241.81340.8594-0.97811.59760.50352.7689-0.3374-0.1027-0.72070.30030.14910.04240.5905-0.07910.19451.21020.10580.2740.63630.0950.9945-3.147553.858191.4601
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 436)
5X-RAY DIFFRACTION5chain 'A' and (resid 437 through 437)
6X-RAY DIFFRACTION6chain 'B' and (resid 2 through 88)
7X-RAY DIFFRACTION7chain 'B' and (resid 89 through 127)
8X-RAY DIFFRACTION8chain 'B' and (resid 128 through 197)
9X-RAY DIFFRACTION9chain 'B' and (resid 198 through 223)
10X-RAY DIFFRACTION10chain 'B' and (resid 224 through 295)
11X-RAY DIFFRACTION11chain 'B' and (resid 296 through 373)
12X-RAY DIFFRACTION12chain 'B' and (resid 374 through 401)
13X-RAY DIFFRACTION13chain 'B' and (resid 402 through 436)
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 197)
15X-RAY DIFFRACTION15chain 'C' and (resid 198 through 440)
16X-RAY DIFFRACTION16chain 'D' and (resid 2 through 88)
17X-RAY DIFFRACTION17chain 'D' and (resid 89 through 295)
18X-RAY DIFFRACTION18chain 'D' and (resid 296 through 401)
19X-RAY DIFFRACTION19chain 'D' and (resid 402 through 441)
20X-RAY DIFFRACTION20chain 'E' and (resid 8 through 46)
21X-RAY DIFFRACTION21chain 'E' and (resid 47 through 141)
22X-RAY DIFFRACTION22chain 'F' and (resid 1 through 66)
23X-RAY DIFFRACTION23chain 'F' and (resid 67 through 198)
24X-RAY DIFFRACTION24chain 'F' and (resid 199 through 380)

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