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- PDB-8c0f: Tubulin-PTC596 complex -

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Basic information

Entry
Database: PDB / ID: 8c0f
TitleTubulin-PTC596 complex
Components
  • (Tubulin beta-2B ...) x 2
  • Stathmin-4
  • Tubulin alpha-1B chain
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 / cytosol / cytoplasm
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-SOZ / 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: 2.1005 Å
AuthorsProta, A.E. / Muehlethaler, T. / Weetall, M. / Steinmetz, M.O.
Funding support United Kingdom, Switzerland, 2items
OrganizationGrant numberCountry
Wellcome Trust092687 United Kingdom
Swiss National Science Foundation31003A_166608 Switzerland
CitationJournal: Mol Cancer Ther / Year: 2021
Title: Preclinical and Early Clinical Development of PTC596, a Novel Small-Molecule Tubulin-Binding Agent
Authors: Jernigan, F. / Branstrom, A. / Baird, J.D. / Cao, L. / Dali, M. / Furia, B. / Kim, M.J. / O'Keefe, K. / Kong, R. / Laskin, O.L. / Colacino, J.M. / Pykett, M. / Mollin, A. / Sheedy, J. / ...Authors: Jernigan, F. / Branstrom, A. / Baird, J.D. / Cao, L. / Dali, M. / Furia, B. / Kim, M.J. / O'Keefe, K. / Kong, R. / Laskin, O.L. / Colacino, J.M. / Pykett, M. / Mollin, A. / Sheedy, J. / Dumble, M. / Moon, Y.-C. / Sheridan, R. / Muehlethaler, T. / Spiegel, R.J. / Prota, A.E. / Steinmetz, M.O. / Weetall, M.
History
DepositionDec 16, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 28, 2022Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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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 beta-2B chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,47827
Polymers261,6316
Non-polymers3,84721
Water10,034557
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.680, 158.260, 180.540
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 , 2 types, 3 molecules ACE

#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) / Organ: Brain / References: UniProt: P81947
#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

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Tubulin beta-2B ... , 2 types, 3 molecules BDF

#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) / Organ: Brain / References: UniProt: Q6B856
#4: Protein Tubulin beta-2B chain


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, 578 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.: 2 / 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-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H8O3
#11: Chemical ChemComp-SOZ / 5-fluoranyl-2-(6-fluoranyl-2-methyl-benzimidazol-1-yl)-~{N}4-[4-(trifluoromethyl)phenyl]pyrimidine-4,6-diamine


Mass: 420.339 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H13F5N6 / Feature type: SUBJECT OF INVESTIGATION
#12: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#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.: 557 / 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: 2.8 Å3/Da / Density % sol: 56.6 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 3% PEG 4K, 3% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.999995 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Apr 14, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.999995 Å / Relative weight: 1
ReflectionResolution: 2.1→49.55 Å / Num. obs: 174197 / % possible obs: 99.7 % / Redundancy: 13.653 % / Biso Wilson estimate: 54.364 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.138 / Rrim(I) all: 0.144 / Χ2: 1.035 / Net I/σ(I): 15.97 / Num. measured all: 2378365 / Scaling rejects: 361
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.1-2.1613.283.9650.716779712818126350.2594.12298.6
2.16-2.2114.2813.4410.8517675912428123770.3573.56799.6
2.21-2.2814.2212.3971.2417235512175121200.4662.48599.5
2.28-2.3514.1662.121.3916669711796117670.5792.19899.8
2.35-2.4313.9531.5961.8715948211455114300.6861.65599.8
2.43-2.5113.8171.192.5115232011045110240.8041.23699.8
2.51-2.6113.4580.93.2814384110699106880.8650.93599.9
2.61-2.7112.6280.7024.0412990310298102870.8930.73299.9
2.71-2.8313.9090.5145.76137825991799090.9520.53399.9
2.83-2.9713.7220.3727.91129576944594430.9730.386100
2.97-3.1312.8450.24311.32115370898389820.9870.253100
3.13-3.3214.1130.17116.38121077858485790.9950.17899.9
3.32-3.5514.2060.11623.48114176803880370.9970.12100
3.55-3.8313.9540.07733.34104561749374930.9990.08100
3.83-4.213.5850.05443.5794337694469440.9990.056100
4.2-4.712.7650.03856.14801536282627910.04100
4.7-5.4212.930.03559.88721655581558110.036100
5.42-6.6412.8640.03657.91611064750475010.038100
6.64-9.3913.9210.02483.67520233738373710.025100
9.39-49.5512.5720.019101.29268422165213510.01998.6

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Processing

Software
NameVersionClassification
PHENIX1.15.2_3472refinement
XSCALEdata scaling
PDB_EXTRACT3.28data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5LXT

5lxt


Resolution: 2.1005→49.55 Å / Cross valid method: FREE R-VALUE
RfactorNum. reflection% reflection
Rfree0.2252 8648 4.96 %
Rwork0.1941 --
obs0.1956 174186 99.76 %
Refinement stepCycle: final / Resolution: 2.1005→49.55 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17268 0 271 557 18096
Biso mean--68.27 60.87 -
Num. residues----2180
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.1005-2.12440.42980.3716535698
2.1244-2.14940.39012700.3593543099
2.1494-2.17560.38122970.34255446100
2.1756-2.20320.36542780.3335546299
2.2032-2.23210.34012770.3227547399
2.2321-2.26270.35692910.31415442100
2.2627-2.2950.34272430.30275525100
2.295-2.32930.32422900.29825432100
2.3293-2.36570.31712700.28875499100
2.3657-2.40450.32962650.27715486100
2.4045-2.44590.27382820.26035495100
2.4459-2.49040.30342810.25045501100
2.4904-2.53830.30882820.24445447100
2.5383-2.59010.26692730.23795528100
2.5901-2.64640.26643400.22885453100
2.6464-2.7080.28682810.23815491100
2.708-2.77570.27463130.22475499100
2.7757-2.85080.28152690.22835518100
2.8508-2.93460.26913140.22485486100
2.9346-3.02930.23962770.20795520100
3.0293-3.13760.23933170.20145508100
3.1376-3.26320.23462890.19655555100
3.2632-3.41170.22073110.1945520100
3.4117-3.59150.2263110.18615534100
3.5915-3.81640.19852700.16665553100
3.8164-4.1110.18242890.1525583100
4.111-4.52440.15472850.14075623100
4.5244-5.17850.17062850.13935619100
5.1785-6.52210.19982970.17365686100
6.5221-49.550.18883030.16955868100
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)
11.8404-0.5109-0.6733.7917-0.57421.1975-0.01370.14730.3147-0.78670.2569-0.1752-1.0270.1902-0.28590.8832-0.11850.12780.5764-0.14920.494528.189896.718451.5602
21.88490.3850.20232.19180.51772.1966-0.14740.26180.1143-0.51360.5343-0.6826-0.61150.7216-0.3840.5248-0.15190.14510.7178-0.30240.624337.285781.311950.3407
31.60590.9141-0.68174.49270.40652.0830.0348-0.0496-0.1430.39850.2444-0.42290.16390.54-0.29340.51720.0625-0.00030.5288-0.19370.473530.190874.438159.1426
47.4162-2.11410.71843.7714-0.41113.44510.15-0.0665-0.37110.2278-0.05670.69530.1029-0.6468-0.17610.38120.01340.05340.4981-0.14740.550111.768579.508959.9775
50.93010.67310.07653.14051.03993.84280.1621-0.06540.12940.5324-0.0640.2272-0.27590.0203-0.14980.50780.02820.09460.4307-0.14190.476119.10387.180468.4822
60.4946-0.07190.48433.24440.86550.74520.0248-0.29050.06021.3458-0.06240.6248-0.074-0.14270.00940.9630.02970.23950.5253-0.12630.571816.6987.386780.7443
71.67970.68040.4952.07210.3662.56290.066-0.09250.02160.6179-0.00620.3507-0.18470.1602-0.08650.71610.00290.16570.527-0.17440.561418.592389.587973.4496
81.4124-0.0375-0.28463.50131.88163.5323-0.0004-0.0878-0.19080.89720.2977-0.33780.95380.456-0.30330.6270.1057-0.05460.4851-0.1580.550129.461562.554562.0768
92.1098-0.3266-0.78072.41381.27062.83030.19920.12410.4131-0.215-0.022-0.0398-0.5410.0148-0.17270.39790.00850.07780.4024-0.08410.465320.138160.424921.5288
101.7437-0.4397-0.06571.54480.78323.23650.0139-0.26290.18410.1611-0.110.3319-0.0818-0.66150.11330.44260.00470.1080.6097-0.21780.5987.437160.851139.3969
111.1924-0.7796-0.0663.36721.52623.22170.0087-0.1946-0.03150.67260.05160.0570.5760.1586-0.07580.3937-0.04370.01080.4052-0.07060.350620.778840.355532.3072
121.6056-0.15040.00281.93940.4091.8402-0.03510.23270.0656-0.27670.0493-0.0423-0.11950.0982-0.0160.3233-0.0590.02240.3981-0.05030.352318.138531.7833-11.3462
130.8603-0.29130.00711.66721.21041.9342-0.0216-0.01410.07410.1222-0.08750.10850.1054-0.21790.09850.2518-0.07350.05140.3039-0.03640.33048.438426.50624.3085
143.0894-1.4215-0.41994.3926-0.22961.1859-0.10180.9088-0.3045-0.5440.23980.15960.4288-0.4757-0.17940.6699-0.15020.04840.9295-0.12230.397817.68864.7015-40.7926
157.1282-2.24910.25213.59432.09675.974-0.38780.73750.8204-0.51580.0819-0.0675-0.6321-0.13170.280.7754-0.0862-0.00660.88770.05260.556713.753318.1876-42.3893
167.4775-2.852-0.29215.4978-0.0652.29710.18481.3922-0.3134-1.470.01430.280.6879-0.5208-0.08991.0362-0.21680.12151.2373-0.20310.517222.03042.6264-50.501
171.7732-0.2514-0.17213.1451-0.22571.0437-0.22630.7942-0.0263-0.82930.3848-0.69820.2530.3753-0.16990.9209-0.05510.29071.1978-0.29260.723533.87310.0087-44.0449
181.1569-0.11870.16771.6168-0.00831.8567-0.08530.4101-0.4187-0.47990.0627-0.31020.5228-0.0762-0.02990.7468-0.08350.13050.7371-0.29270.586622.4364-5.7263-33.6429
192.30960.14160.20162.48880.0023.1792-0.04440.4151-0.0057-0.24970.26210.09370.1814-0.2443-0.24690.4475-0.06040.07290.5893-0.13620.472815.5253.9903-27.8346
202.0218-0.0858-0.38841.60830.56582.5375-0.21020.4186-0.3781-0.08480.12940.10620.495-0.43960.14470.5236-0.14440.04940.5616-0.15010.45738.2066-3.5142-21.6055
213.4403-0.7455-1.50652.292-0.03093.2984-0.25120.1118-0.78280.41970.177-0.28971.120.5140.00480.88420.05420.03740.621-0.28440.898430.5524-16.1722-24.2686
223.3184-1.8228-0.12163.84950.47331.2951-0.1288-0.24140.12491.17560.4569-0.2045-0.00360.7417-0.27321.0704-0.11670.01640.8035-0.22450.663427.520993.519381.7052
230.4046-0.3719-0.47021.05311.12931.60040.0013-0.0341-0.02110.1760.3863-0.47940.30850.5265-0.53480.48530.05230.06910.7953-0.23370.690843.023928.33894.2383
242.8590.2498-1.86891.6143-0.42674.8467-0.3580.2087-0.4994-0.09360.1795-0.37341.071-0.0750.16280.854-0.01570.10810.5681-0.07220.64697.633658.434478.1184
252.50310.32550.66192.4556-0.77571.0088-0.2118-0.9801-0.02470.86710.0733-0.80130.41961.67060.19251.05870.1717-0.11482.12230.36951.23819.68257.4603109.4625
261.52040.3987-1.15911.9564-0.94642.2777-0.5725-0.2082-0.94760.25830.1687-0.15541.32640.15250.39221.50160.1470.31540.74850.20161.0867-2.030648.1041101.0947
272.8859-0.0629-2.07911.42090.35173.6568-0.37170.2821-0.4819-0.05610.31530.03180.7299-0.27010.01950.8797-0.00260.12070.54730.00810.6054-1.283860.609287.382
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 88 )A1 - 88
2X-RAY DIFFRACTION2chain 'A' and (resid 89 through 160 )A89 - 160
3X-RAY DIFFRACTION3chain 'A' and (resid 161 through 199 )A161 - 199
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 223 )A200 - 223
5X-RAY DIFFRACTION5chain 'A' and (resid 224 through 306 )A224 - 306
6X-RAY DIFFRACTION6chain 'A' and (resid 307 through 339 )A307 - 339
7X-RAY DIFFRACTION7chain 'A' and (resid 340 through 381 )A340 - 381
8X-RAY DIFFRACTION8chain 'A' and (resid 382 through 437 )A382 - 437
9X-RAY DIFFRACTION9chain 'B' and (resid 2 through 215 )B2 - 215
10X-RAY DIFFRACTION10chain 'B' and (resid 216 through 372 )B216 - 372
11X-RAY DIFFRACTION11chain 'B' and (resid 373 through 438 )B373 - 438
12X-RAY DIFFRACTION12chain 'C' and (resid 1 through 223 )C1 - 223
13X-RAY DIFFRACTION13chain 'C' and (resid 224 through 440 )C224 - 440
14X-RAY DIFFRACTION14chain 'D' and (resid 2 through 27 )D2 - 27
15X-RAY DIFFRACTION15chain 'D' and (resid 28 through 64 )D28 - 64
16X-RAY DIFFRACTION16chain 'D' and (resid 65 through 88 )D65 - 88
17X-RAY DIFFRACTION17chain 'D' and (resid 89 through 128 )D89 - 128
18X-RAY DIFFRACTION18chain 'D' and (resid 129 through 223 )D129 - 223
19X-RAY DIFFRACTION19chain 'D' and (resid 224 through 266 )D224 - 266
20X-RAY DIFFRACTION20chain 'D' and (resid 267 through 401 )D267 - 401
21X-RAY DIFFRACTION21chain 'D' and (resid 402 through 441 )D402 - 441
22X-RAY DIFFRACTION22chain 'E' and (resid 6 through 46 )E6 - 46
23X-RAY DIFFRACTION23chain 'E' and (resid 47 through 143 )E47 - 143
24X-RAY DIFFRACTION24chain 'F' and (resid 1 through 96 )F1 - 96
25X-RAY DIFFRACTION25chain 'F' and (resid 97 through 184 )F97 - 184
26X-RAY DIFFRACTION26chain 'F' and (resid 185 through 283 )F185 - 283
27X-RAY DIFFRACTION27chain 'F' and (resid 284 through 380 )F284 - 380

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