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- PDB-7zyw: Crystal structure of T2R-TTL-PM534 complex -

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Basic information

Entry
Database: PDB / ID: 7zyw
TitleCrystal structure of T2R-TTL-PM534 complex
Components
  • (Tubulin beta-2B ...) x 2
  • Stathmin-4
  • Tubulin alpha-1B chain
KeywordsCELL CYCLE/INHIBITOR / Tubulin / microtubule destabilizing agents / inhibitor / CELL CYCLE-INHIBITOR complex
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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-KG0 / 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 / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.45 Å
AuthorsOliva, M.A. / Diaz, J.F. / Cuevas, C.
Funding support Spain, 1items
OrganizationGrant numberCountry
Ministerio de Ciencia e Innovacion (MCIN)PID2019-104545RBI00/AEI/10.13039/501100011033 Spain
CitationJournal: J.Med.Chem. / Year: 2024
Title: PM534, an Optimized Target-Protein Interaction Strategy through the Colchicine Site of Tubulin.
Authors: Lucena-Agell, D. / Guillen, M.J. / Matesanz, R. / Alvarez-Bernad, B. / Hortiguela, R. / Aviles, P. / Martinez-Diez, M. / Santamaria-Nunez, G. / Contreras, J. / Plaza-Menacho, I. / Gimenez- ...Authors: Lucena-Agell, D. / Guillen, M.J. / Matesanz, R. / Alvarez-Bernad, B. / Hortiguela, R. / Aviles, P. / Martinez-Diez, M. / Santamaria-Nunez, G. / Contreras, J. / Plaza-Menacho, I. / Gimenez-Abian, J.F. / Oliva, M.A. / Cuevas, C. / Diaz, J.F.
History
DepositionMay 25, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 29, 2023Provider: repository / Type: Initial release
Revision 1.1Jun 12, 2024Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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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)271,08827
Polymers266,9126
Non-polymers4,17621
Water2,126118
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.803, 158.026, 181.080
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 / Details: Alpha tubulin-1B / Source: (natural) Bos taurus (cattle) / Tissue: brain / References: UniProt: P81947
#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
Details: Stathmin-4 / 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 / Details: Beta tubulin-2B / Source: (natural) Bos taurus (cattle) / Tissue: 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
Details: Tubulin Tyrosine Ligase / 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, 139 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-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#9: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#10: 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
#11: 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
#12: Chemical ChemComp-KG0 / (4R)-N-[(1R)-1-[4-(cyclopropylmethoxy)-6-oxidanylidene-pyran-2-yl]butyl]-4-methyl-2-[(E)-C-methyl-N-oxidanyl-carbonimidoyl]-5H-1,3-thiazole-4-carboxamide


Mass: 421.510 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H27N3O5S / Feature type: SUBJECT OF INVESTIGATION
#13: Chemical ChemComp-DMS / DIMETHYL SULFOXIDE / Dimethyl sulfoxide


Mass: 78.133 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6OS / Comment: DMSO, precipitant*YM
#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 / Water


Mass: 18.015 Da / Num. of mol.: 118 / 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: 2.82 Å3/Da / Density % sol: 56.35 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: Mes, Imidazole, Calcium Chloride, Magnesium Chloride, L-tyrosine, Glycerol, PEG4000

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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: Sep 15, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979257 Å / Relative weight: 1
ReflectionResolution: 2.45→49.66 Å / Num. obs: 110428 / % possible obs: 99.6 % / Redundancy: 4.7 % / Biso Wilson estimate: 58.85 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.088 / Rpim(I) all: 0.044 / Rrim(I) all: 0.099 / Net I/σ(I): 9.6 / Num. measured all: 524464 / Scaling rejects: 45
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
2.45-2.494.90.9192644554330.6030.4581.0311.7100
13.42-49.664.50.07234027630.9820.0390.08321.698.1

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.51 Å49.66 Å
Translation8.51 Å49.66 Å

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Processing

Software
NameVersionClassification
PHENIX1.19refinement
XDSdata reduction
Aimless0.5.32data scaling
PHASER2.7.16phasing
PDB_EXTRACT3.27data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4O2B

4o2b


Resolution: 2.45→49.66 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 27.08 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.244 5500 4.98 %
Rwork0.2185 104832 -
obs0.2198 110332 99.49 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 218.44 Å2 / Biso mean: 78.6072 Å2 / Biso min: 29.65 Å2
Refinement stepCycle: final / Resolution: 2.45→49.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16501 0 415 118 17034
Biso mean--68.71 55.4 -
Num. residues----2085
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 (%)
2.45-2.480.34871800.320134763656100
2.48-2.510.33631930.319334303623100
2.51-2.540.34471730.311934673640100
2.54-2.570.34381660.305535143680100
2.57-2.60.33751930.28834493642100
2.6-2.640.35181960.297234613657100
2.64-2.680.35551790.292534943673100
2.68-2.720.33351870.290534323619100
2.72-2.760.31021630.28173458362198
2.76-2.80.29291620.28234673629100
2.8-2.850.33152050.289334573662100
2.85-2.90.30131930.291634773670100
2.9-2.960.35381730.299534863659100
2.96-3.020.2971940.283334673661100
3.02-3.090.3111600.271335323692100
3.09-3.160.28381760.265135003676100
3.16-3.240.32961830.269734593642100
3.24-3.320.28671910.26033479367099
3.33-3.420.2851870.24743411359898
3.42-3.530.27271940.241134853679100
3.53-3.660.28331770.237735183695100
3.66-3.810.242110.214834793690100
3.81-3.980.22321770.193835023679100
3.98-4.190.20131850.18113532371799
4.19-4.450.20381710.16473479365098
4.45-4.790.17881740.1553534370899
4.79-5.280.17011890.163335453734100
5.28-6.040.2062050.19473540374599
6.04-7.60.22691710.20583580375198
7.6-49.660.20511920.19543722391499
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)
10.3769-0.27770.0750.2021-0.0510.0165-0.08760.022-0.0875-0.3040.3556-0.0466-0.42520.32830.05920.8104-0.14880.13010.4706-0.11770.44628.796796.284452.7506
20.26240.01390.08930.1436-0.00750.04090.0643-0.0085-0.4633-0.1103-0.09560.2659-0.2820.22540.00460.7932-0.09310.12660.4509-0.14060.464629.38987.418643.33
3-0.00720.0383-0.02650.275-0.0970.0593-0.00330.1341-0.16330.07320.3513-0.2807-0.07940.14770.11170.4913-0.05690.08860.6357-0.25840.628835.016778.274155.4506
40.04-0.0106-0.00560.0785-0.04130.03120.38950.1044-0.01450.2323-0.03530.1047-0.0221-0.0386-00.56170.07850.02860.6386-0.14020.669711.652679.375159.8829
50.0393-0.03180.02860.06380.04590.0812-0.1130.0632-0.0740.0870.0776-0.1586-0.33550.422100.6073-0.02680.05650.5837-0.09270.573225.007690.582265.5895
60.05670.1007-0.0060.1784-0.0148-0.0120.10840.14860.05980.2802-0.12270.20620.01080.053400.53870.01850.11310.4403-0.16160.545714.5683.763671.2228
70.1483-0.02170.09070.05440.04560.0973-0.0681-0.27230.08370.13820.21490.0525-0.2282-0.0476-00.72240.09270.070.5292-0.14940.507316.543787.482180.6943
80.2790.0525-0.06410.17670.17630.14110.00590.0796-0.09080.2275-0.02930.17190.01550.0492-00.52370.03920.02080.4211-0.13050.460422.009776.632266.5501
90.0315-0.0061-0.02830.0006-0.00720.0757-0.01860.49170.00060.3834-0.2297-0.1157-0.06330.0843-0.00210.70880.196-0.06880.6771-0.17470.611432.434863.514168.7123
100.144-0.0653-0.16790.09250.05720.1534-0.00280.1793-0.05660.07280.07210.1708-0.2048-0.011400.50550.03880.05370.3345-0.01850.557315.22972.54822.0282
110.1232-0.1965-0.15330.41070.33980.25810.03390.03160.0201-0.10430.03920.0032-0.06520.0277-00.348-0.00720.03780.4249-0.09720.452822.257255.085821.3735
120.0825-0.0708-0.19910.05020.15020.36750.1880.06870.07970.0234-0.17420.0923-0.0223-0.121600.45360.03330.03240.5948-0.16580.644310.340762.149531.0426
130.0154-0.0096-0.02010.025-0.0640.12390.04450.065-0.0705-0.009-0.13390.08020.0683-0.2414-0.00180.38860.07580.01470.5554-0.19470.57167.331458.046339.3849
140.2993-0.06140.13410.08190.04150.10750.0152-0.32870.0757-0.0392-0.0477-0.1729-0.0555-0.2904-0.00870.4750.05610.08350.6857-0.20250.51065.041359.573944.8355
150.0574-0.05030.01530.06440.05240.06370.0989-0.20420.4732-0.1367-0.22630.05740.1905-0.0419-00.48940.03550.03440.5751-0.14840.68.710662.548544.9251
160.09260.07280.15040.05530.13180.16560.0022-0.02080.01060.2678-0.0346-0.07590.20870.064200.43880.00740.00360.4577-0.07630.43321.280739.883232.1043
170.31320.10870.25660.44560.0140.2868-0.06550.1117-0.0205-0.06670.0712-0.0093-0.0750.051400.4148-0.05820.02460.4672-0.01920.44320.536733.0874-11.7599
180.1191-0.15620.01680.35780.4950.5213-0.02620.03730.0250.0477-0.02840.06370.0764-0.075200.391-0.03620.02410.4193-0.04210.45827.677326.08393.106
190.8640.0754-0.37721.0572-0.2240.4606-0.30140.68570.1211-0.06160.47940.04760.1711-0.4560.15110.6662-0.29330.03951.0392-0.08780.385118.55317.2574-45.1185
200.26280.11080.09740.05120.02620.0631-0.07040.25610.23930.07730.2825-0.058-0.12410.4686-0.01660.7699-0.19270.32240.8381-0.23860.501835.55151.062-41.5514
210.6264-0.25690.29020.3709-0.00590.2357-0.2480.392-0.0585-0.11790.1997-0.11950.2153-0.1623-0.13560.7266-0.17320.12020.7346-0.28160.502724.6065-5.0755-33.04
220.273-0.0259-0.15850.4313-0.32790.3639-0.32280.3982-0.0271-0.0510.3282-0.05690.2539-0.26370.00310.5373-0.17420.05060.6404-0.140.40099.8332-2.735-24.2568
230.1702-0.03590.10790.1497-0.12590.13650.12650.0336-0.0633-0.02320.1815-0.20770.11380.23430.29560.85050.02170.18690.5751-0.25130.678630.8546-16.3717-24.0299
240.6645-0.092-0.10760.02010.0010.03850.08740.17490.13680.1085-0.0113-0.07350.01890.0086-0.06010.7656-0.15490.03190.5521-0.26920.674824.740599.788282.1126
250.07240.02330.07180.02030.01980.06090.00610.184-0.04480.43830.0894-0.2449-0.0520.1397-01.2631-0.1373-0.13720.7719-0.14020.487931.505282.736382.5771
260.39020.0463-0.11440.25030.22930.0174-0.0642-0.07650.046-0.1153-0.03890.08220.01640.2248-0.21740.47870.00040.04860.6491-0.27790.554542.917629.96896.4563
271.2999-0.33430.26710.141-0.13260.1686-0.47540.35760.0042-0.01630.159-0.04350.6114-0.0947-0.19220.8345-0.12180.1740.5165-0.11570.50275.88854.88969.7496
280.0860.02970.00140.0589-0.02640.0135-0.2187-0.0816-0.2638-0.04580.15630.02360.00340.3880.00020.70050.2470.0120.84030.1130.505511.931963.479899.6263
290.74840.39-0.38060.2397-0.29770.4156-0.41490.0063-0.380.05050.124-0.0770.4385-0.1317-0.17960.91430.12140.23780.42120.14320.677-3.720250.990499.3594
300.3227-0.0001-0.30860.05490.07640.3069-0.32540.0458-0.1490.10430.34460.01560.2860.01420.00040.81740.06370.15070.48120.08750.541-2.527359.988989.0768
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 79 )A1 - 79
2X-RAY DIFFRACTION2chain 'A' and (resid 80 through 102 )A80 - 102
3X-RAY DIFFRACTION3chain 'A' and (resid 103 through 199 )A103 - 199
4X-RAY DIFFRACTION4chain 'A' and (resid 200 through 223 )A200 - 223
5X-RAY DIFFRACTION5chain 'A' and (resid 224 through 259 )A224 - 259
6X-RAY DIFFRACTION6chain 'A' and (resid 260 through 306 )A260 - 306
7X-RAY DIFFRACTION7chain 'A' and (resid 307 through 338 )A307 - 338
8X-RAY DIFFRACTION8chain 'A' and (resid 339 through 414 )A339 - 414
9X-RAY DIFFRACTION9chain 'A' and (resid 415 through 437 )A415 - 437
10X-RAY DIFFRACTION10chain 'B' and (resid 2 through 64 )B2 - 64
11X-RAY DIFFRACTION11chain 'B' and (resid 65 through 215 )B65 - 215
12X-RAY DIFFRACTION12chain 'B' and (resid 216 through 259 )B216 - 259
13X-RAY DIFFRACTION13chain 'B' and (resid 260 through 296 )B260 - 296
14X-RAY DIFFRACTION14chain 'B' and (resid 297 through 338 )B297 - 338
15X-RAY DIFFRACTION15chain 'B' and (resid 339 through 372 )B339 - 372
16X-RAY DIFFRACTION16chain 'B' and (resid 373 through 436 )B373 - 436
17X-RAY DIFFRACTION17chain 'C' and (resid 1 through 199 )C1 - 199
18X-RAY DIFFRACTION18chain 'C' and (resid 200 through 440 )C200 - 440
19X-RAY DIFFRACTION19chain 'D' and (resid 2 through 102 )D2 - 102
20X-RAY DIFFRACTION20chain 'D' and (resid 103 through 128 )D103 - 128
21X-RAY DIFFRACTION21chain 'D' and (resid 129 through 214 )D129 - 214
22X-RAY DIFFRACTION22chain 'D' and (resid 215 through 401 )D215 - 401
23X-RAY DIFFRACTION23chain 'D' and (resid 402 through 441 )D402 - 441
24X-RAY DIFFRACTION24chain 'E' and (resid 6 through 20 )E6 - 20
25X-RAY DIFFRACTION25chain 'E' and (resid 21 through 46 )E21 - 46
26X-RAY DIFFRACTION26chain 'E' and (resid 47 through 139 )E47 - 139
27X-RAY DIFFRACTION27chain 'F' and (resid 1 through 66 )F1 - 66
28X-RAY DIFFRACTION28chain 'F' and (resid 67 through 149 )F67 - 149
29X-RAY DIFFRACTION29chain 'F' and (resid 182 through 274 )F182 - 274
30X-RAY DIFFRACTION30chain 'F' and (resid 275 through 380 )F275 - 380

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