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- PDB-7zx2: Tubulin-Pelophen B complex -

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Basic information

Entry
Database: PDB / ID: 7zx2
TitleTubulin-Pelophen B complex
Components
  • (Tubulin beta-2B ...) x 2
  • Stathmin-4
  • Tubulin alpha-1B chain
KeywordsCELL CYCLE/INHIBITOR / Tubulin / Pelophen / Peloruside / Laulimalide / 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 / cytoplasmic microtubule / tubulin binding / cellular response to interleukin-4 / 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 / tubulin binding / cellular response to interleukin-4 / 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
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. ...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 / 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 / Chem-K9I / 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: 2.5 Å
AuthorsEstevez-Gallego, J. / Diaz, J.F. / Van der Eycken, J. / Oliva, M.A.
Funding support Spain, European Union, 2items
OrganizationGrant numberCountry
Ministerio de Ciencia e Innovacion (MCIN)PID2019-104545RBI00/AEI/10.13039/501100011033 Spain
H2020 Marie Curie Actions of the European CommissionH2020-MSCA-ITN-2019 860070 TUBINTRAINEuropean Union
CitationJournal: Structure / Year: 2023
Title: Chemical modulation of microtubule structure through the laulimalide/peloruside site.
Authors: Estevez-Gallego, J. / Alvarez-Bernad, B. / Pera, B. / Wullschleger, C. / Raes, O. / Menche, D. / Martinez, J.C. / Lucena-Agell, D. / Prota, A.E. / Bonato, F. / Bargsten, K. / Cornelus, J. / ...Authors: Estevez-Gallego, J. / Alvarez-Bernad, B. / Pera, B. / Wullschleger, C. / Raes, O. / Menche, D. / Martinez, J.C. / Lucena-Agell, D. / Prota, A.E. / Bonato, F. / Bargsten, K. / Cornelus, J. / Gimenez-Abian, J.F. / Northcote, P. / Steinmetz, M.O. / Kamimura, S. / Altmann, K.H. / Paterson, I. / Gago, F. / Van der Eycken, J. / Diaz, J.F. / Oliva, M.A.
History
DepositionMay 20, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 23, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 7, 2023Group: 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
Revision 1.2Feb 7, 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 beta-2B chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)271,07830
Polymers266,9126
Non-polymers4,16624
Water2,522140
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.709, 156.973, 181.043
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 (domestic cattle) / 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 (domestic cattle) / 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 tyrosin 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, 164 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.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C3H8O3
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#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.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: Chemical ChemComp-K9I / (3R,4S,7S,9S,11S)-3,4,11-trihydroxy-7-((R,Z)-4-(hydroxymethyl)hex-2-en-2-yl)-9-methoxy-12,12-dimethyl-6-oxa-1(1,3)-benzenacyclododecaphan-5-one


Mass: 464.592 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C26H40O7
#13: Chemical ChemComp-DMS / 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


Mass: 18.015 Da / Num. of mol.: 140 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 55.87 %
Crystal growTemperature: 293.15 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: ESRF / Beamline: ID30B / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Apr 7, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.5→49.66 Å / Num. obs: 103744 / % possible obs: 100 % / Redundancy: 8.1 % / Biso Wilson estimate: 54.32 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.098 / Rpim(I) all: 0.037 / Rrim(I) all: 0.105 / Net I/σ(I): 13.5 / Num. measured all: 841601 / Scaling rejects: 79
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
2.5-2.548.31.0384222150730.6970.3841.1082100
13.69-49.666.70.07148427280.9940.030.0773498.2

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation8.16 Å49.61 Å
Translation8.16 Å49.61 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: 2.5→49.66 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.19 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2354 5204 5.02 %
Rwork0.1971 98449 -
obs0.199 103653 99.99 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 166.92 Å2 / Biso mean: 67.1093 Å2 / Biso min: 26.27 Å2
Refinement stepCycle: final / Resolution: 2.5→49.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16666 0 256 140 17062
Biso mean--59.43 47.68 -
Num. residues----2105
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.5-2.530.36091610.313332273388
2.53-2.560.33481730.286132333406
2.56-2.590.32371660.26932853451
2.59-2.620.27211750.264232383413
2.62-2.660.29161800.256132363416
2.66-2.690.30241690.26132653434
2.69-2.730.29741750.254432043379
2.73-2.770.32271690.251632793448
2.77-2.820.28861850.256632603445
2.82-2.860.30981530.259132433396
2.86-2.910.29021650.272232763441
2.91-2.960.33781890.283932083397
2.96-3.020.31321620.260332793441
3.02-3.080.29811730.249432753448
3.08-3.150.26361780.229132563434
3.15-3.220.27581830.234132203403
3.22-3.30.21951620.224432843446
3.3-3.390.28551660.222932823448
3.39-3.490.2531910.213532933484
3.49-3.610.2531770.216732353412
3.61-3.730.21111750.191833103485
3.73-3.880.20261920.176332283420
3.88-4.060.24871880.171332813469
4.06-4.270.20011500.162833163466
4.27-4.540.1941870.149833183505
4.54-4.890.18231620.14133063468
4.89-5.380.2011550.160933523507
5.38-6.160.22561810.17933533534
6.16-7.760.20031860.177233623548
7.76-49.660.1891760.173135453721
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)
10.3941-0.3221-0.22990.18530.15580.36850.02630.1265-0.0764-0.34920.14730.027-0.34630.27520.03060.6421-0.09090.09690.386-0.09740.377528.581898.577754.912
20.06540.0331-0.01210.0905-0.09360.0782-0.2784-0.0849-0.1893-0.580.190.0285-0.54780.0515-00.7828-0.13990.07970.4751-0.08850.415327.258489.304243.8378
30.974-0.36440.64550.2368-0.0430.80750.09110.44-0.2499-0.31490.3806-0.1409-0.0860.74580.30730.326-0.20270.18890.5933-0.21850.472337.735680.500846.1307
4-0.0171-0.1175-0.15390.42760.05110.63780.11130.0296-0.01610.15230.1245-0.03170.03590.17490.00330.4011-0.01420.00990.4855-0.18810.495432.862176.900857.6837
50.36530.16550.41891.07010.63721.03950.10910.05450.01180.2694-0.09880.0941-0.0626-0.0555-0.00030.40160.0160.05860.3116-0.09260.350817.998384.173566.521
60.79650.46730.46541.05380.10650.18730.1067-0.08960.06380.2273-0.14410.19530.0079-0.045800.63950.00410.04260.4386-0.12720.427617.490987.887676.6893
7-0.08530.20250.00140.846-0.0480.47190.0780.1957-0.13490.53450.1419-0.07440.48730.22110.00680.49060.1057-0.07530.4211-0.12620.418329.507961.842861.9782
80.9981-0.0947-0.21730.2925-0.07780.63210.02860.24840.1043-0.24130.00390.0653-0.2503-0.045700.45520.05020.02440.387-0.01340.413117.235867.887818.1867
90.3249-0.2223-0.14980.96911.21011.4167-0.01270.055-0.0703-0.0168-0.002-0.0241-0.05490.0219-0.00710.2484-0.0120.02130.3558-0.07470.361520.259953.654124.5203
100.4128-0.22010.05750.75070.58380.6998-0.043-0.05410.0710.1101-0.19630.03120.053-0.2348-0.03140.36930.01040.05230.4582-0.15750.43088.713461.278942.1381
11-0.22270.19930.20870.61950.38250.9172-0.04920.1208-0.04790.31610.00080.03070.34820.018700.38120.0176-0.01590.3489-0.0340.376821.318540.088232.3853
120.783-0.00750.27530.90990.25590.5309-0.03820.0878-0.0066-0.05940.0505-0.0276-0.03580.0654-00.3082-0.04110.01910.3657-0.02970.344318.279131.4187-11.3012
130.478-0.35120.00920.84310.69620.7999-0.00390.01240.08420.0726-0.0590.0050.1172-0.127100.3061-0.0430.02760.3258-0.03870.3558.379126.42964.156
140.07960.0966-0.1350.0779-0.01640.1043-0.32020.30070.0702-0.15170.3819-0.01090.0644-0.32760.00010.6184-0.15970.03610.8671-0.14080.449817.83814.901-40.4819
150.15550.0126-0.09910.13340.05470.0505-0.37690.41510.1136-0.15480.1974-0.1257-0.01590.06760.00020.6164-0.0551-0.02350.79860.04090.48713.9317.6443-42.5049
160.55930.0957-0.05440.4952-0.41050.5314-0.2270.4899-0.0031-0.29830.271-0.24050.06940.1578-0.05460.6267-0.09660.13180.7963-0.2570.492529.49560.8412-42.7684
170.5945-0.2845-0.17460.0916-0.04280.3437-0.30160.3663-0.1408-0.26560.3466-0.16140.32830.0759-0.01840.6598-0.11180.09060.5473-0.24030.538321.8671-8.7355-32.1337
180.1106-0.0427-0.4690.29530.09340.4355-0.08970.24250.0346-0.16160.1348-0.12290.1001-0.2235-0.00190.489-0.12090.01240.5659-0.10590.411813.16410.3953-29.9609
190.39-0.1677-0.0650.5474-0.0821.3502-0.19630.256-0.0662-0.04160.1416-0.01040.2928-0.31730.00250.5014-0.11750.03360.5161-0.14290.45768.0767-3.7552-21.9403
200.368-0.12150.14150.2585-0.15290.0347-0.00760.0503-0.38860.1706-0.0388-0.08260.34830.08770.00940.8210.06380.050.5781-0.24210.654630.4219-16.4921-24.1427
210.9005-0.0341-0.08130.0239-0.00320.01260.00430.53920.4380.35870.1332-0.1193-0.01520.07070.01570.6892-0.09510.01240.4115-0.12880.616424.686598.995582.1465
220.15180.14650.12780.07220.1330.0701-0.14640.1469-0.45010.63190.061-0.4848-0.12840.2967-0.00011.34810.0358-0.09340.8576-0.1290.671631.841882.271882.1935
230.206-0.4198-0.4430.10020.3459-0.0707-0.142-0.07470.04340.28240.11170.04320.48350.3367-0.09560.43510.02750.02880.5808-0.24310.506642.844129.40655.9317
242.2055-0.6076-0.32570.65740.03850.67640.18540.511-0.05070.6405-0.2488-0.05520.9198-0.5624-0.13371.1639-0.31390.1440.4737-0.19110.52046.323954.233569.9883
250.12010.1003-0.10960.0778-0.14190.1385-0.6854-0.4984-0.2337-0.1690.11960.0682-0.43410.872200.96240.0279-0.00570.96170.1120.730313.597663.172199.5685
260.19250.3381-0.39640.2401-0.21420.6132-0.32790.3442-0.46150.0182-0.0235-0.0170.2043-0.0775-0.1171.08070.03920.21030.62080.20550.8776-2.753450.5865101.2518
270.9333-0.1768-0.5567-0.0935-0.12140.4148-0.12070.0447-0.22280.180.53810.10060.1709-0.04950.00011.0382-0.09410.17040.652-0.01020.6851-0.926359.660987.7705
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 64 )A1 - 64
2X-RAY DIFFRACTION2chain 'A' and (resid 65 through 88 )A65 - 88
3X-RAY DIFFRACTION3chain 'A' and (resid 89 through 128 )A89 - 128
4X-RAY DIFFRACTION4chain 'A' and (resid 129 through 197 )A129 - 197
5X-RAY DIFFRACTION5chain 'A' and (resid 198 through 306 )A198 - 306
6X-RAY DIFFRACTION6chain 'A' and (resid 307 through 381 )A307 - 381
7X-RAY DIFFRACTION7chain 'A' and (resid 382 through 437 )A382 - 437
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 102 )B1 - 102
9X-RAY DIFFRACTION9chain 'B' and (resid 103 through 238 )B103 - 238
10X-RAY DIFFRACTION10chain 'B' and (resid 239 through 372 )B239 - 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 1 through 27 )D1 - 27
15X-RAY DIFFRACTION15chain 'D' and (resid 28 through 64 )D28 - 64
16X-RAY DIFFRACTION16chain 'D' and (resid 65 through 160 )D65 - 160
17X-RAY DIFFRACTION17chain 'D' and (resid 161 through 214 )D161 - 214
18X-RAY DIFFRACTION18chain 'D' and (resid 215 through 266 )D215 - 266
19X-RAY DIFFRACTION19chain 'D' and (resid 267 through 401 )D267 - 401
20X-RAY DIFFRACTION20chain 'D' and (resid 402 through 441 )D402 - 441
21X-RAY DIFFRACTION21chain 'E' and (resid 6 through 20 )E6 - 20
22X-RAY DIFFRACTION22chain 'E' and (resid 21 through 46 )E21 - 46
23X-RAY DIFFRACTION23chain 'E' and (resid 47 through 140 )E47 - 140
24X-RAY DIFFRACTION24chain 'F' and (resid 1 through 66 )F1 - 66
25X-RAY DIFFRACTION25chain 'F' and (resid 67 through 147 )F67 - 147
26X-RAY DIFFRACTION26chain 'F' and (resid 148 through 283 )F148 - 283
27X-RAY DIFFRACTION27chain 'F' and (resid 284 through 380 )F284 - 380

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