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- PDB-7ogn: Crystal structure of T2R-TTL -mebendazole complex -

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Basic information

Entry
Database: PDB / ID: 7ogn
TitleCrystal structure of T2R-TTL -mebendazole complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine Ligase
KeywordsSTRUCTURAL PROTEIN / cytoskeleton / microtubules / tubulin / mebendazole
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
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. ...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. / 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. / 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 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-V95 / 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 / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.2 Å
AuthorsOliva, M.A. / Bonato, F. / Diaz, J.F.
Funding support Spain, European Union, 3items
OrganizationGrant numberCountry
Spanish Ministry of Science, Innovation, and UniversitiesPID2019-104545RB-I00/AEI/10.13039/501100011033 Spain
Spanish National Research CouncilFondo de Investigaciones Sanitarias COV20/01007 Spain
European Research Council (ERC)H2020-MSCA-ITN-2019 860070 TUBINTRAINEuropean Union
CitationJournal: Int J Mol Sci / Year: 2022
Title: Effect of Clinically Used Microtubule Targeting Drugs on Viral Infection and Transport Function.
Authors: Oliva, M.A. / Tosat-Bitrian, C. / Barrado-Gil, L. / Bonato, F. / Galindo, I. / Garaigorta, U. / Alvarez-Bernad, B. / Paris-Ogayar, R. / Lucena-Agell, D. / Gimenez-Abian, J.F. / Garcia- ...Authors: Oliva, M.A. / Tosat-Bitrian, C. / Barrado-Gil, L. / Bonato, F. / Galindo, I. / Garaigorta, U. / Alvarez-Bernad, B. / Paris-Ogayar, R. / Lucena-Agell, D. / Gimenez-Abian, J.F. / Garcia-Dorival, I. / Urquiza, J. / Gastaminza, P. / Diaz, J.F. / Palomo, V. / Alonso, C.
History
DepositionMay 7, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Apr 6, 2022Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2022Group: Database references / Category: citation / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 31, 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)270,89430
Polymers266,9126
Non-polymers3,98224
Water4,089227
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area24580 Å2
ΔGint-175 kcal/mol
Surface area79060 Å2
Unit cell
Length a, b, c (Å)104.900, 158.010, 179.689
Angle α, β, γ (deg.)90.000, 90.000, 90.000
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: 22125.301 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 BL21(DE3) / 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 BL21(DE3) / References: UniProt: E1BQ43

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Non-polymers , 11 types, 251 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.: 7 / 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-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#10: 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
#11: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: Chemical ChemComp-V95 / methyl N-(6-benzoyl-1H-benzimidazol-2-yl)carbamate / Mebendazole / 4030


Mass: 295.293 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H13N3O3 / Feature type: SUBJECT OF INVESTIGATION
#13: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 1 / 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.: 227 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 2.79 Å3/Da / Density % sol: 55.91 %
Crystal growTemperature: 295.15 K / Method: vapor diffusion, hanging drop
Details: MES, Imidazole, calcium chloride, magnesium chloride, L-Tyrosine, glycerol, PEG 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: ALBA / Beamline: XALOC / Wavelength: 0.979257 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Oct 29, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979257 Å / Relative weight: 1
ReflectionResolution: 2.2→50.35 Å / Num. obs: 150908 / % possible obs: 99.6 % / Redundancy: 9.5 % / Biso Wilson estimate: 48.71 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.074 / Rpim(I) all: 0.025 / Rrim(I) all: 0.078 / Net I/σ(I): 16.7 / Num. measured all: 1440160 / Scaling rejects: 38
Reflection shell

Diffraction-ID: 1 / % possible all: 98.8

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs
2.2-2.249.91.3547299473750.670.4461.4271.7
12.05-50.358.40.031878210460.9990.0110.03351.7

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.25 Å50.35 Å

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Processing

Software
NameVersionClassificationNB
PHENIX1.19.1_4122refinement
XDSdata reduction
Aimless0.7.4data scaling
PHASER2.8.3phasing
PDB_EXTRACT3.27data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4o2b

4o2b


Resolution: 2.2→50.35 Å / SU ML: 0.27 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.46 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2342 7565 5.02 %
Rwork0.2087 143239 -
obs0.21 150804 99.48 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 214.98 Å2 / Biso mean: 65.2179 Å2 / Biso min: 26.06 Å2
Refinement stepCycle: final / Resolution: 2.2→50.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17200 0 359 227 17786
Biso mean--54.97 46.3 -
Num. residues----2171
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2-2.230.31632690.30294708497799
2.23-2.250.32412630.2994664492799
2.25-2.280.33612670.28914707497498
2.28-2.310.3062270.279547224949100
2.31-2.340.30432440.28464709495399
2.34-2.370.29232680.281247154983100
2.37-2.40.31392260.29534694492099
2.4-2.440.33692430.29894741498499
2.44-2.480.30262440.278147284972100
2.48-2.520.30652600.27574703496399
2.52-2.560.30223060.26384698500499
2.56-2.610.28092250.245247835008100
2.61-2.660.27582450.24654699494499
2.66-2.710.29022130.24864791500499
2.71-2.770.27532590.25084731499099
2.77-2.840.26742430.25134769501299
2.84-2.910.29322380.266647905028100
2.91-2.990.29852270.276547674994100
2.99-3.070.33052600.257447595019100
3.07-3.170.27442460.243147945040100
3.17-3.290.24982760.238647575033100
3.29-3.420.26422520.22874746499899
3.42-3.570.24972840.224247885072100
3.57-3.760.23642620.203747855047100
3.76-40.19552690.173548115080100
4-4.310.17082270.158748705097100
4.31-4.740.15972480.138748735121100
4.74-5.420.1842620.151448765138100
5.42-6.830.19912360.190949455181100
6.83-50.350.20292760.181751165392100
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)
10.5076-0.2266-0.32210.2764-0.09190.33280.05630.0475-0.0783-0.23030.1306-0.1234-0.4650.20110.05780.6382-0.08460.10240.4049-0.11830.392728.89597.33653.319
2-0.03-0.11190.14640.54830.80570.6461-0.04890.0171-0.061-0.18350.2424-0.1148-0.19770.19090.01990.4181-0.05850.06480.4588-0.160.460933.42280.68351.694
30.2121-0.2180.32560.26110.22320.61360.0530.1048-0.04830.09770.02820.0544-0.11310.123900.46130.00110.04240.4515-0.08950.515621.20384.57664.461
40.13150.10870.00410.18670.2110.15750.1812-0.0170.21430.1173-0.19790.15830.0178-0.1247-00.51190.00530.10280.427-0.12150.56159.20184.69471.421
50.15470.20120.14820.80510.09410.26940.0149-0.0053-0.02170.2659-0.01760.1970.03-0.006700.5620.02280.05630.3968-0.11810.4519.05183.56273.103
60.09760.3009-0.11990.39170.04640.4322-0.06390.1477-0.07270.38650.1848-0.07480.28290.25610.04080.45780.1338-0.04560.4078-0.16480.44631.17261.35262.367
70.4099-0.0901-0.53060.2384-0.00330.2736-0.0305-0.0147-0.007-0.09340.07180.0979-0.177-0.0533-00.43950.0436-0.01920.2982-0.05930.422115.38872.60521.901
8-0.0178-0.1435-0.20690.15130.46090.37020.12750.1089-0.0168-0.3418-0.0087-0.1064-0.14790.180300.3847-0.02890.03430.3744-0.07760.383424.58759.05713.097
90.23080.0426-0.08760.48520.89041.0044-0.0291-0.02450.0643-0.0096-0.06140.0254-0.0019-0.047-0.00050.2989-0.00040.00770.3976-0.09040.408217.41353.47526.396
10-0.04250.05020.01980.0409-0.06240.29080.09410.07990.12130.2244-0.14650.0779-0.18880.118900.43840.01720.0640.397-0.10920.518919.9564.35938.868
110.06180.03180.02950.28840.00920.1314-0.02370.16780.06020.1425-0.2343-0.16080.0491-0.326-0.01480.3793-0.01390.07860.5803-0.18460.46371.78656.30239.07
120.15720.05710.06070.05220.01570.07290.1034-0.07080.31440.0054-0.1991-0.09120.0189-0.421100.45130.08180.04520.6162-0.16240.52764.37764.80646.807
130.14590.0135-0.14090.30890.21120.13780.04620.12810.3118-0.0177-0.19670.09880.1806-0.103800.47460.05530.02280.5364-0.08860.47168.9462.48844.77
14-0.0934-0.29550.28750.00720.30330.07140.0338-0.12070.15770.13270.006-0.00670.2324-0.065400.4582-0.0050.06070.4006-0.07740.460614.8843.32734.166
150.08530.2553-0.20150.17170.06780.0730.0240.1004-0.03020.2784-0.0006-0.1280.1370.1374-00.39350.0404-0.04030.4015-0.05640.372325.86438.1630.836
160.0703-0.00430.09840.73240.00410.5415-0.04630.0833-0.0039-0.07460.0867-0.0038-0.06240.0999-00.2992-0.05380.01910.3677-0.02160.357120.38433.126-11.897
170.2652-0.29550.06640.67470.62840.5041-0.00750.0580.02370.0478-0.05960.040.0753-0.087900.301-0.0310.03550.3305-0.02790.3367.56426.2063.067
180.8059-0.0569-0.20880.6241-0.45460.2251-0.05310.44650.123-0.25480.1855-0.09380.08590.09150.31160.5799-0.0860.08530.7309-0.12190.427622.2946.648-44.079
190.46440.2602-0.49080.1097-0.05410.3474-0.12430.2264-0.0319-0.04410.1295-0.11020.1231-0.0364-0.00040.519-0.04780.04510.5453-0.16540.405320.371-3.513-32.114
200.4535-0.1936-0.1210.41-0.04890.6666-0.09650.1508-0.14630.03340.08730.02080.0909-0.164600.5255-0.03570.02850.4685-0.13920.46113.236-6.867-22.767
210.05070.09910.00220.0650.01790.0504-0.05570.34510.46770.05360.19830.0316-0.01430.2793-0.00060.6999-0.07040.05540.5143-0.17280.660324.86399.70981.62
220.276-0.172-0.0750.3168-0.07790.2080.0908-0.1453-0.47470.3930.46190.0083-0.20450.11950.11751.06730.0208-0.16450.762-0.20140.618532.07683.56181.108
230.249-0.2638-0.23890.03050.18950.3144-0.0202-0.03260.0014-0.010.0416-0.03840.02340.1170.01210.4358-0.00180.0490.6114-0.20320.57242.88528.9164.937
240.244-0.30820.20561.3963-0.82880.8387-0.85710.2293-0.3121-0.31730.0596-0.58711.1714-0.3958-0.44930.9648-0.21760.24650.4725-0.16520.53595.41851.84569.355
250.04950.243-0.1315-0.06930.0230.0821-0.18070.1018-0.0711-0.0790.0686-0.1161-0.01450.001900.5399-0.00880.06380.4805-0.02380.42511.4263.52680.67
260.11470.08380.14340.18310.16560.1282-0.1024-0.28280.15890.1944-0.225-0.2121-0.3040.6575-0.05450.4950.118-0.10161.01330.27760.474917.50159.789107.314
270.08110.04150.05920.0190.070.1737-0.3397-0.111-0.45080.2980.01320.04080.39910.23490.08450.94130.12550.16750.31480.18760.6084-0.30550.454103.069
280.1870.045-0.213-0.0631-0.0450.1134-0.38380.325-0.28720.1372-0.199-0.35560.0513-0.1216-0.26830.69770.01220.18990.30880.1090.6246-0.4652.18895.539
290.1861-0.00390.37380.0296-0.10640.951-0.31760.2054-0.038-0.1133-0.2669-0.02350.43640.83880.00111.49490.26170.47310.59880.19951.24544.13139.343101.44
30-0.17260.0922-0.13930.02530.08240.2993-0.23420.1816-0.0480.12180.3684-0.01330.2637-0.05810.00050.7435-0.00060.12640.41360.08830.5244-6.43357.38697.671
310.73840.0203-0.5032-0.0463-0.03170.3437-0.34920.1108-0.14960.02970.1895-0.14070.3049-0.2333-00.7074-0.07060.0710.44720.03150.5211-1.34458.37985.342
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 1:72 )A1 - 72
2X-RAY DIFFRACTION2( CHAIN A AND RESID 73:199 )A73 - 199
3X-RAY DIFFRACTION3( CHAIN A AND RESID 200:273 )A200 - 273
4X-RAY DIFFRACTION4( CHAIN A AND RESID 274:311 )A274 - 311
5X-RAY DIFFRACTION5( CHAIN A AND RESID 312:401 )A312 - 401
6X-RAY DIFFRACTION6( CHAIN A AND RESID 402:450 )A402 - 450
7X-RAY DIFFRACTION7( CHAIN B AND RESID 1:64 )B1 - 64
8X-RAY DIFFRACTION8( CHAIN B AND RESID 65:127 )B65 - 127
9X-RAY DIFFRACTION9( CHAIN B AND RESID 128:238 )B128 - 238
10X-RAY DIFFRACTION10( CHAIN B AND RESID 239:268 )B239 - 268
11X-RAY DIFFRACTION11( CHAIN B AND RESID 269:311 )B269 - 311
12X-RAY DIFFRACTION12( CHAIN B AND RESID 312:338 )B312 - 338
13X-RAY DIFFRACTION13( CHAIN B AND RESID 339:372 )B339 - 372
14X-RAY DIFFRACTION14( CHAIN B AND RESID 373:401 )B373 - 401
15X-RAY DIFFRACTION15( CHAIN B AND RESID 402:438 )B402 - 438
16X-RAY DIFFRACTION16( CHAIN C AND RESID 1:199 )C1 - 199
17X-RAY DIFFRACTION17( CHAIN C AND RESID 200:440 )C200 - 440
18X-RAY DIFFRACTION18( CHAIN D AND RESID 1:128 )D1 - 128
19X-RAY DIFFRACTION19( CHAIN D AND RESID 129:268 )D129 - 268
20X-RAY DIFFRACTION20( CHAIN D AND RESID 269:441 )D269 - 441
21X-RAY DIFFRACTION21( CHAIN E AND RESID 6:20 )E6 - 20
22X-RAY DIFFRACTION2250:71 )E50 - 71
23X-RAY DIFFRACTION23( CHAIN E AND RESID 88:185 )E88 - 185
24X-RAY DIFFRACTION24( CHAIN F AND RESID 1:48 )F1 - 48
25X-RAY DIFFRACTION25( CHAIN F AND RESID 49:83 )F49 - 83
26X-RAY DIFFRACTION26( CHAIN F AND RESID 84:184 )F84 - 184
27X-RAY DIFFRACTION27( CHAIN F AND RESID 185:207 )F185 - 207
28X-RAY DIFFRACTION28( CHAIN F AND RESID 208:235 )F208 - 235
29X-RAY DIFFRACTION29( CHAIN F AND RESID 236:257 )F236 - 257
30X-RAY DIFFRACTION30( CHAIN F AND RESID 258:302 )F258 - 302
31X-RAY DIFFRACTION31( CHAIN F AND RESID 303:380 )F303 - 380

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