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- PDB-5sba: Tubulin-maytansinoid-4b-complex -

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Basic information

Entry
Database: PDB / ID: 5sba
TitleTubulin-maytansinoid-4b-complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine LigaseTubulin—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 / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / 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 / tubulin binding / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / spindle microtubule / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / nervous system development / mitotic cell cycle / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
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-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-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 / 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
Similarity search - Domain/homology
Chem-5IJ / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / DIFFERENCE FOURIER / Resolution: 2.25 Å
AuthorsMarzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. ...Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
H2020-MSCA-ITN-2019860070 TUBINTRAINEuropean Union
CitationJournal: Chemistry / Year: 2022
Title: Maytansinol Derivatives: Side Reactions as a Chance for New Tubulin Binders.
Authors: Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Altmann, K.H. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
History
DepositionJul 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 9, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2Mar 9, 2022Group: Data collection / Category: reflns
Item: _reflns.number_obs / _reflns.pdbx_number_measured_all ..._reflns.number_obs / _reflns.pdbx_number_measured_all / _reflns.pdbx_redundancy / _reflns.pdbx_scaling_rejects
Revision 1.3May 22, 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-Tyrosine Ligase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,27523
Polymers261,6316
Non-polymers3,64317
Water14,088782
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.174, 156.450, 180.827
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 (cattle) / Organ: Brain / 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 (cattle) / Organ: Brain / 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 / 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 , 10 types, 799 molecules

#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine 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.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine 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 / MES (buffer)


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 / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#11: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#12: Chemical ChemComp-5IJ / (1S,2R,3S,5S,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.1~10,14~.0~3,5~]hexacosa-10(26),11,13,16,18-pentaen-6-yl acetate


Mass: 607.092 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C30H39ClN2O9 / Feature type: SUBJECT OF INVESTIGATION
#13: 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
#14: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 782 / 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, hanging drop / pH: 6.5
Details: 3% PEG 4K, 4% 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
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00003 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Feb 23, 2021
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2.25→49.49 Å / Num. obs: 140740 / % possible obs: 100 % / Redundancy: 13.628 % / Biso Wilson estimate: 46.72 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.192 / Rrim(I) all: 0.2 / Χ2: 0.764 / Net I/σ(I): 11.85 / Num. measured all: 1918037
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
2.25-2.3112.8732.9740.8413245510293102890.3433.097100
2.31-2.3714.142.2541.2114176810029100260.4742.338100
2.37-2.4414.2421.8971.47138947976097560.561.967100
2.44-2.5214.1871.5251.85133985944994440.6741.58299.9
2.52-2.614.0531.2252.31128996918091790.761.271100
2.6-2.6913.8881.0292.78123797891589140.8061.068100
2.69-2.7913.6760.813.5117117856485640.8710.842100
2.79-2.912.8490.6044.53106169826582630.920.63100
2.9-3.0313.4580.4616.09107316797479740.9530.479100
3.03-3.1813.8610.3368.42105333760075990.9780.349100
3.18-3.3513.1180.24710.9495051724772460.9880.257100
3.35-3.5613.6090.17315.5193292685568550.9930.18100
3.56-3.814.2310.12421.4592119647364730.9970.129100
3.8-4.1114.0450.09227.3384819603960390.9980.095100
4.11-4.513.7630.07233.176604556655660.9990.074100
4.5-5.0313.2720.06236.967222506550650.9990.064100
5.03-5.8112.7640.06932.8557274448744870.9980.072100
5.81-7.1213.0740.06833.849890381638160.9990.07100
7.12-10.0613.7750.04549.3741615302130210.9990.046100
10.06-49.4912.6990.03856.3121956175017290.9990.0498.8

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Processing

Software
NameVersionClassificationNB
PHENIX1.19.1_4122refinement
XSCALEdata scaling
PDB_EXTRACT3.28data extraction
XDSdata reduction
PHENIX1.19.1_4122phasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 5LXT

5lxt


Resolution: 2.25→49.49 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 23.06 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2269 7037 5 %
Rwork0.1839 133691 -
obs0.186 140728 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 173.67 Å2 / Biso mean: 61.5954 Å2 / Biso min: 27.38 Å2
Refinement stepCycle: final / Resolution: 2.25→49.49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17313 0 237 782 18332
Biso mean--60.89 56.37 -
Num. residues----2186
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 (%)
2.25-2.270.36572300.34824376460699
2.27-2.30.36122330.307144284661100
2.3-2.330.31792310.291743964627100
2.33-2.360.29262330.291444154648100
2.36-2.390.34662320.283944124644100
2.39-2.420.33752320.287344114643100
2.42-2.460.31132320.272744074639100
2.46-2.490.29532330.256344334666100
2.49-2.530.28752330.242544164649100
2.53-2.570.28912320.235444054637100
2.57-2.620.27942330.224644314664100
2.62-2.660.26442330.211544404673100
2.66-2.720.25592340.207944294663100
2.72-2.770.25362320.212444074639100
2.77-2.830.24782330.210544414674100
2.83-2.90.25392360.220244694705100
2.9-2.970.25142310.214844044635100
2.97-3.050.24152330.184744234656100
3.05-3.140.22562360.185144904726100
3.14-3.240.27182330.189844284661100
3.24-3.360.2282350.181644654700100
3.36-3.490.23662350.175644494684100
3.49-3.650.22142350.170444624697100
3.65-3.840.19272360.153844974733100
3.84-4.080.18652350.145344604695100
4.08-4.40.17372360.140944834719100
4.4-4.840.17952390.132745344773100
4.84-5.540.20412380.155545394777100
5.54-6.980.21982420.18345954837100
6.98-49.490.19772510.173147464997100
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)
11.1438-0.2918-0.27412.87521.38022.7677-0.00450.02320.0505-0.20850.2332-0.2452-0.50470.34540.00870.4977-0.0860.06160.46-0.11720.445428.626485.182256.1418
20.80990.3965-0.10411.06170.66361.32550.2398-0.02530.11410.1838-0.33190.6038-0.0447-0.488-0.00020.5904-0.00070.13730.522-0.15450.629.395883.168272.1128
30.86220.16060.02362.55461.85662.3710.0354-0.05220.00740.5790.02360.03290.27190.125500.5482-0.0030.03560.4297-0.06330.451922.919476.168770.1316
42.0664-0.7358-0.2011.6051-0.51711.14950.05440.14510.4994-0.1992-0.04870.1197-0.6717-0.2077-00.62260.0613-0.00160.5204-0.04310.597816.28169.574219.5503
51.0918-0.4983-0.19641.48811.35843.3059-0.0555-0.01160.060.0494-0.12060.1476-0.174-0.2779-0.03440.33820.00860.01550.4458-0.1050.489115.600256.511730.7514
60.412-0.00510.25451.31751.20132.2917-0.0205-0.1043-0.01690.4531-0.10370.12730.3564-0.1193-0.00040.4146-0.04090.03530.4647-0.05180.476717.793845.676135.6602
71.074-0.2304-0.03792.58180.35591.6824-0.03230.13680.076-0.30950.0954-0.0187-0.15490.135600.336-0.07830.0370.4379-0.03860.400220.356132.6917-11.8943
80.7572-0.2664-0.17191.58991.25941.69660.0006-0.01210.08470.0765-0.09270.12780.0873-0.1934-0.00040.3304-0.06930.04790.3949-0.02780.43157.685125.51623.2067
90.9079-0.25750.19810.4235-0.44850.5559-0.27390.41440.0269-0.4250.33580.04870.0471-0.13880.00010.6861-0.11770.01960.7534-0.1080.457917.56885.302-40.358
100.5927-0.30010.14530.35070.12120.2119-0.2720.580.4679-0.5380.03890.1669-0.30290.163-0.00010.7875-0.0595-0.02410.85780.00380.57214.104617.7974-42.5241
112.00690.36690.21670.42580.13330.053-0.03061.150.4489-1.3453-0.0647-0.20310.18640.003-0.02341.0221-0.12230.13081.0706-0.20820.524422.18862.0566-50.4438
120.2414-0.1058-0.0790.3344-0.21390.22070.0310.36050.0354-0.83040.0752-0.63010.18550.5414-0.00030.86860.00180.22220.9071-0.21070.663833.9389-0.9317-44.0428
131.4718-0.2777-0.42750.90950.0152.0204-0.21150.3045-0.3068-0.41610.1879-0.19610.42020.0799-00.6918-0.02690.08670.6101-0.17220.533122.384-6.061-33.6642
140.70810.038-0.50940.4654-0.23930.6842-0.13240.2243-0.0034-0.52880.22290.0828-0.2680.00690.00010.562-0.04550.02930.5844-0.09630.490713.49644.8936-30.0746
150.6228-0.7341-0.77711.81340.70361.01640.04070.3969-0.3266-0.345-0.08630.32010.4501-0.4094-00.6564-0.09580.00670.6414-0.13820.54347.2025-5.5437-24.1687
161.6155-0.38080.01020.90150.41112.3879-0.21040.1797-0.0718-0.00960.10550.13160.2776-0.352100.5782-0.11610.03470.528-0.08590.48218.997-2.5439-21.0284
171.38740.41050.60811.0668-0.35790.5689-0.357-0.0341-0.50140.25480.2668-0.10570.98220.5365-0.00020.89390.06670.07870.5804-0.15850.70730.3306-17.2283-24.6455
180.61010.23970.12270.40390.37480.3519-0.1869-0.28430.07490.80440.4009-0.58520.22710.82380.00111.0872-0.00120.0160.7612-0.11730.624327.324991.853382.2035
190.2426-0.4663-0.58290.11140.26830.8269-0.0195-0.0173-0.04830.42160.38-0.43290.62070.56240.02670.50860.06760.03460.7967-0.24690.718542.919628.52345.1439
201.43590.164-1.27470.7470.33961.4186-0.30820.4212-0.6118-0.1961-0.0726-0.21140.8274-0.3123-00.9996-0.11820.13460.6503-0.14440.72266.058253.974969.8783
210.23920.11640.08890.1223-0.06120.20660.1549-0.35810.05880.3345-0.1843-0.3781-0.40540.93830.00020.83110.01240.00110.8932-0.00250.748111.216664.903397.4866
220.13490.122-0.0810.1886-0.05240.04850.6113-0.21490.55580.4541-0.9869-1.0702-0.17110.6706-0.00471.0568-0.0194-0.33241.82670.31351.243421.680761.1319109.7336
230.19330.38630.05820.73260.11480.01640.3805-0.36250.06471.1018-0.0282-1.4410.5011.3050.01451.14580.3371-0.08251.74890.45111.212218.950952.2842108.3158
241.6210.2829-1.16070.65420.2291.0941-0.4503-0.3084-0.6483-0.0135-0.0829-0.20581.0130.1771-0.00020.96950.0430.17490.60070.15790.7656-1.961452.41396.9412
250.65540.6755-0.44750.7858-0.12771.1743-0.5162-0.3021-0.86420.23050.0085-0.46771.06760.4656-0.00381.44190.20070.3840.71880.26251.1758-1.700142.8975103.8948
262.47890.0875-1.7330.89380.26261.8411-0.23920.134-0.41950.08490.21110.10840.4401-0.1494-00.7958-0.01760.10660.52420.00870.648-0.947459.42587.3753
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 273 )A1 - 273
2X-RAY DIFFRACTION2chain 'A' and (resid 274 through 311 )A274 - 311
3X-RAY DIFFRACTION3chain 'A' and (resid 312 through 438 )A312 - 438
4X-RAY DIFFRACTION4chain 'B' and (resid 1 through 88 )B1 - 88
5X-RAY DIFFRACTION5chain 'B' and (resid 89 through 338 )B89 - 338
6X-RAY DIFFRACTION6chain 'B' and (resid 339 through 437 )B339 - 437
7X-RAY DIFFRACTION7chain 'C' and (resid 1 through 199 )C1 - 199
8X-RAY DIFFRACTION8chain 'C' and (resid 200 through 440 )C200 - 440
9X-RAY DIFFRACTION9chain 'D' and (resid 1 through 28 )D1 - 28
10X-RAY DIFFRACTION10chain 'D' and (resid 29 through 64 )D29 - 64
11X-RAY DIFFRACTION11chain 'D' and (resid 65 through 88 )D65 - 88
12X-RAY DIFFRACTION12chain 'D' and (resid 89 through 127 )D89 - 127
13X-RAY DIFFRACTION13chain 'D' and (resid 128 through 223 )D128 - 223
14X-RAY DIFFRACTION14chain 'D' and (resid 224 through 259 )D224 - 259
15X-RAY DIFFRACTION15chain 'D' and (resid 260 through 311 )D260 - 311
16X-RAY DIFFRACTION16chain 'D' and (resid 312 through 400 )D312 - 400
17X-RAY DIFFRACTION17chain 'D' and (resid 401 through 441 )D401 - 441
18X-RAY DIFFRACTION18chain 'E' and (resid 6 through 46 )E6 - 46
19X-RAY DIFFRACTION19chain 'E' and (resid 47 through 141 )E47 - 141
20X-RAY DIFFRACTION20chain 'F' and (resid 1 through 66 )F1 - 66
21X-RAY DIFFRACTION21chain 'F' and (resid 67 through 96 )F67 - 96
22X-RAY DIFFRACTION22chain 'F' and (resid 97 through 140 )F97 - 140
23X-RAY DIFFRACTION23chain 'F' and (resid 141 through 184 )F141 - 184
24X-RAY DIFFRACTION24chain 'F' and (resid 185 through 223 )F185 - 223
25X-RAY DIFFRACTION25chain 'F' and (resid 224 through 283 )F224 - 283
26X-RAY DIFFRACTION26chain 'F' and (resid 284 through 380 )F284 - 380

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