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- PDB-8bdf: Tubulin-taxane-2a complex -

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Basic information

Entry
Database: PDB / ID: 8bdf
TitleTubulin-taxane-2a 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 / microtubule-based process / regulation of microtubule polymerization or depolymerization / 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 / microtubule-based process / regulation of microtubule polymerization or depolymerization / 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 / microtubule cytoskeleton / neuron projection development / 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 / cytoplasm / cytosol
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-R42 / 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 / FOURIER SYNTHESIS / Resolution: 1.95 Å
AuthorsProta, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muehlethaler, T. ...Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muehlethaler, T. / Gago, F. / Oliva, M.A. / Steinmetz, M.O. / Fang, W.S. / Diaz, J.F.
Funding support Switzerland, Spain, European Union, 4items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
Spanish Ministry of Science, Innovation, and Universities2019-104545RB-I00 Spain
Spanish Ministry of Science, Innovation, and UniversitiesCOV20/01007 Spain
H2020 Marie Curie Actions of the European Commission2019 860070European Union
CitationJournal: Elife / Year: 2023
Title: Structural insight into the stabilization of microtubules by taxanes.
Authors: Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Josa-Prado, F. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muhlethaler, T. / Gago, F. / Oliva, M.A. ...Authors: Prota, A.E. / Lucena-Agell, D. / Ma, Y. / Estevez-Gallego, J. / Li, S. / Bargsten, K. / Josa-Prado, F. / Altmann, K.H. / Gaillard, N. / Kamimura, S. / Muhlethaler, T. / Gago, F. / Oliva, M.A. / Steinmetz, M.O. / Fang, W.S. / Diaz, J.F.
History
DepositionOct 19, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 22, 2023Provider: repository / Type: Initial release
Revision 1.1Feb 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)266,09420
Polymers261,6316
Non-polymers4,46314
Water15,907883
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22860 Å2
ΔGint-133 kcal/mol
Surface area78810 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.840, 157.890, 179.090
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))
21(chain C and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))
12(chain B and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))
22(chain D and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))A1 - 164
121(chain A and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))A166 - 360
131(chain A and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))A362 - 438
211(chain C and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))C1 - 164
221(chain C and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))C166 - 360
231(chain C and (resid 1 through 164 or resid 166 through 360 or resid 362 through 438))C362 - 438
112(chain B and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))B1 - 278
122(chain B and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))B286 - 310
132(chain B and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))B312 - 438
142(chain B and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))B504
212(chain D and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))D1 - 278
222(chain D and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))D286 - 310
232(chain D and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))D312 - 438
242(chain D and (resid 1 through 278 or resid 286 through 310 or resid 312 through 438 or resid 504))D504

NCS ensembles :
ID
1
2

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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 (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 (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 , 8 types, 897 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.: 1 / 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-R42 / [(1~{S},2~{S},3~{R},4~{S},7~{R},9~{S},10~{S},12~{R},15~{S})-4-acetyloxy-15-[(2~{R},3~{S})-3-[(4-methoxy-2-methylidene-4-oxidanylidene-butanoyl)amino]-2-oxidanyl-3-phenyl-propanoyl]oxy-10,14,16,16-tetramethyl-1,9,12-tris(oxidanyl)-11-oxidanylidene-6-oxatetracyclo[11.3.1.0^{3,10}.0^{4,7}]heptadec-13-en-2-yl] benzoate


Mass: 833.873 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C44H51NO15 / Feature type: SUBJECT OF INVESTIGATION
#11: 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
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 883 / 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: 2.83 Å3/Da / Density % sol: 56.58 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 2-4% PEG 4K, 2-10% glycerol, 30 mM MgCl2, 524 30 mM CaCl2, 0.1 M MES/Imidazole

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 0.99987 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Apr 27, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99987 Å / Relative weight: 1
ReflectionResolution: 1.95→49.284 Å / Num. obs: 215803 / % possible obs: 100 % / Redundancy: 27.315 % / Biso Wilson estimate: 43.11 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.133 / Rrim(I) all: 0.136 / Χ2: 1.009 / Net I/σ(I): 20.05 / Num. measured all: 5894682 / Scaling rejects: 893
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
1.95-227.7615.1660.7343963015843158360.3145.261100
2-2.0627.5943.7451.0542670715470154640.4383.815100
2.06-2.1226.2272.8831.3639183714945149400.5612.94100
2.12-2.1827.5342.121.9340180114596145930.7032.16100
2.18-2.2528.4641.6442.6140313714167141630.8051.674100
2.25-2.3328.3451.2553.4338880313719137170.8721.278100
2.33-2.4228.0060.944.5936895213175131740.9250.957100
2.42-2.5227.6680.6956.1235238412737127360.9560.707100
2.52-2.6326.6870.518.0932790912289122870.9750.52100
2.63-2.7626.0190.39110.3130421111693116920.9830.398100
2.76-2.9127.9580.27914.7731086611119111190.9920.284100
2.91-3.0826.3780.1920.427883910571105710.9960.194100
3.08-3.327.4320.12829.04272620993899380.9980.131100
3.3-3.5628.4420.08741.36263515926592650.9990.089100
3.56-3.927.8460.0655.782385058565856510.061100
3.9-4.3626.9490.04570.652092607765776510.046100
4.36-5.0324.8990.03680.521713796883688310.037100
5.03-6.1726.7620.03979.141573895881588110.039100
6.17-8.7226.2490.03291.231205614593459310.033100
8.72-49.28425.3250.027111.21663772656262110.02898.7

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.13_2998refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5lxt

5lxt


Resolution: 1.95→49.284 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.39 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2157 10794 5 %
Rwork0.1891 204980 -
obs0.1904 215774 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 209.75 Å2 / Biso mean: 62.9404 Å2 / Biso min: 25.14 Å2
Refinement stepCycle: final / Resolution: 1.95→49.284 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17199 0 289 883 18371
Biso mean--78.22 60.31 -
Num. residues----2173
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3980X-RAY DIFFRACTION10.356TORSIONAL
12C3980X-RAY DIFFRACTION10.356TORSIONAL
21B3901X-RAY DIFFRACTION10.356TORSIONAL
22D3901X-RAY DIFFRACTION10.356TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork
1.95-1.97210.38663550.37856797
1.9721-1.99530.36583310.35036771
1.9953-2.01970.34043760.32316773
2.0197-2.04520.34173280.31396780
2.0452-2.07210.33363430.30596761
2.0721-2.10050.33193730.29236785
2.1005-2.13050.28993410.27756773
2.1305-2.16230.30443940.2666737
2.1623-2.19610.28263420.2536785
2.1961-2.23210.26783770.23766817
2.2321-2.27060.2483250.22666772
2.2706-2.31190.25063460.2266810
2.3119-2.35640.26023510.22336804
2.3564-2.40450.23673140.22146816
2.4045-2.45680.24173700.21166793
2.4568-2.51390.26283790.21266798
2.5139-2.57680.233800.20856782
2.5768-2.64640.26533810.20836794
2.6464-2.72430.25233410.21146844
2.7243-2.81220.25013490.2056831
2.8122-2.91270.25453550.20286862
2.9127-3.02930.23883760.19856796
3.0293-3.16720.21623850.19746838
3.1672-3.33410.23483750.19396818
3.3341-3.5430.19093640.18176862
3.543-3.81640.20153600.16946902
3.8164-4.20030.16383890.14996896
4.2003-4.80770.15353710.13836938
4.8077-6.05540.20823430.16337025
6.0554-49.2840.18743800.17297220
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)
12.1699-0.4275-0.53234.49230.44772.55140.12190.12190.4294-0.52810.076-0.2323-1.11210.2184-0.1840.7213-0.07790.10320.4173-0.09420.381428.893997.398153.4786
21.48270.25181.0049.01630.9842.5989-0.19780.28520.2479-1.43730.31610.2114-1.01870.1829-0.06550.9085-0.11670.09470.5149-0.09660.462128.093586.93342.181
31.85470.532-0.03174.10931.60582.6195-0.08120.07610.0182-0.08150.3552-0.4954-0.16150.4728-0.26670.3561-0.01060.03840.4398-0.18120.396635.195278.246654.843
49.0719-2.17092.06445.1401-0.27275.57420.2211-0.1459-0.3843-0.0461-0.1250.91610.2518-0.8393-0.1310.35240.01450.02290.4138-0.1360.456611.78378.992259.645
51.23650.060.00053.00531.21943.34080.1127-0.13390.13640.3989-0.14880.2438-0.1415-0.088-0.02920.44030.02530.08640.3453-0.12550.429218.735986.827568.0732
62.3343-0.16180.41744.30751.45332.68020.0167-0.31030.12670.6963-0.0150.3151-0.0172-0.1019-0.03050.584-0.01230.13620.4816-0.15110.440317.482188.277676.3302
70.9462-0.1741-0.25471.95312.18175.08810.1558-0.0511-0.12710.36810.0749-0.08810.34360.2128-0.27130.43040.05320.00150.339-0.10050.392727.628961.148957.5972
82.88012.26160.37874.7133-1.61031.70950.1614-0.4392-0.20531.0277-0.05780.06590.07240.5550.04770.65560.177-0.08360.4023-0.10.444329.643462.159971.18
93.6156-1.1615-0.42316.29481.8063.55590.15490.23460.5711-0.4661-0.1830.1724-0.9476-0.1540.06470.55260.0567-0.00470.3508-0.02160.425916.398969.802619.2848
101.5820.23910.26612.72341.45392.8618-0.01190.11450.1377-0.12320.0922-0.1568-0.32440.2901-0.0650.2993-0.0020.02180.4024-0.09530.365126.275954.126921.8851
111.31040.10940.2631.66220.72183.2845-0.0539-0.12090.21340.0791-0.21590.3828-0.1907-0.52270.20.2930.03610.07240.429-0.18720.440712.043357.550932.6114
123.4356-1.91831.22585.08120.83851.7025-0.1569-0.1367-0.41540.0144-0.42031.09310.0268-1.01520.37910.4988-0.02750.04640.9359-0.31430.7135-0.451456.666438.2845
134.2786-3.0879-1.92282.3341.39370.9143-0.7816-0.78390.24060.75610.41560.4811-0.818-1.51770.22760.70770.3085-0.0260.9249-0.2830.63254.896965.019947.0273
140.6488-0.29620.30911.72281.63.3108-0.0837-0.09950.15740.4745-0.20330.31690.1836-0.56270.24110.3085-0.05460.08810.4384-0.12680.401612.320352.00739.2152
151.1229-0.9053-0.36854.04642.98862.5566-0.0317-0.2639-0.29090.9637-0.0071-0.18420.94380.5670.00790.4653-0.0387-0.05290.4509-0.02950.36625.980137.793730.8256
161.33370.0794-0.21842.19680.28941.6403-0.04830.16470.1438-0.28790.1308-0.0628-0.16560.1231-0.07750.2806-0.06820.03310.366-0.04190.307120.349233.036-11.8979
171.1005-0.35740.27431.4921.12412.0119-0.0359-0.02510.09540.0088-0.14210.28340.0511-0.37110.16630.2145-0.04870.04740.336-0.05210.35282.844130.91653.2066
181.2908-0.6162-0.532.84011.77432.01240.02670.0874-0.0910.33930.1115-0.17050.40930.1624-0.15110.2504-0.0019-0.01840.2413-0.03760.274320.26113.34432.4761
192.7636-1.1282-0.12793.30970.68672.1546-0.23790.6860.0598-0.83760.3098-0.1418-0.03910.0751-0.05360.7749-0.21490.07990.8588-0.13120.366622.6146.8536-44.3269
201.48710.20760.07621.73920.00892.276-0.15130.3664-0.2811-0.41550.2486-0.1910.35740.0391-0.12610.5185-0.08510.05910.5351-0.2020.41720.4379-2.5933-32.0994
211.8192-1.48451.31673.1281-0.0262.9758-0.00630.275-0.4177-0.2233-0.0140.43710.7532-0.8547-0.04940.5497-0.2195-0.02260.7673-0.13920.51223.0234-6.0623-25.2563
222.6979-0.772-0.60873.07170.94063.0827-0.19810.2419-0.1803-0.07860.12080.21620.1862-0.23130.0970.4045-0.13410.01040.3803-0.08870.33259.3976-2.5829-21.5166
232.4035-0.579-1.23763.63141.5113.4905-0.40470.1874-0.93430.11670.1614-0.34241.08660.5021-0.07510.73060.08480.04070.5482-0.27840.675430.4283-16.3863-24.6993
242.8112-2.44020.27944.980.86520.9088-0.1501-0.26510.2291.05930.3513-0.4759-0.11280.3937-0.21771.0881-0.0528-0.04990.6544-0.22190.583327.490792.759381.5934
250.40250.0283-0.29880.0130.00470.2153-0.0959-0.0031-0.06320.5080.5614-0.50060.65680.7747-0.55220.47860.09980.00110.7119-0.26760.649143.050928.7344.8629
263.5631.0205-1.55174.39461.26595.5024-0.47030.468-0.6901-0.05640.214-0.0111.2099-0.37460.17420.9094-0.09710.15260.5697-0.15350.58146.33554.621869.714
277.15331.7799-0.01334.8045-4.95815.7443-0.0364-0.73110.02460.7219-0.1768-0.4048-0.12611.00830.16070.70960.0332-0.04840.8160.02760.595511.029766.061197.176
285.86031.05991.94247.7792-0.61094.5204-0.1163-0.6643-0.39710.8649-0.0891-1.73470.17721.71540.21130.8310.1125-0.19891.65340.31430.93720.46157.1547108.219
292.75580.489-0.83832.744-3.00184.189-0.511-0.2204-0.89960.03430.1118-0.13341.2451-0.00120.20930.98380.10840.18590.45690.12530.6811-2.064153.414296.7548
305.08470.05711.96791.48281.10314.3096-1.09680.0917-1.9035-0.7849-0.3049-0.94491.00351.10851.01132.22740.26910.28340.78330.32771.69682.489140.1376103.477
312.5362-0.3273-1.90220.3740.92952.7776-0.3955-0.1474-0.57120.16150.2554-0.00350.6680.07890.09670.84490.05480.11630.43210.08010.5514-2.215558.093894.8473
324.8650.1818-0.33935.2816-0.33246.1568-0.3390.8504-0.8374-0.104-0.02330.21361.5594-0.99290.34810.6575-0.19530.08550.7384-0.1450.6575-7.404955.04678.8126
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 71 )A1 - 71
2X-RAY DIFFRACTION2chain 'A' and (resid 72 through 102 )A72 - 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 306 )A224 - 306
6X-RAY DIFFRACTION6chain 'A' and (resid 307 through 381 )A307 - 381
7X-RAY DIFFRACTION7chain 'A' and (resid 382 through 414 )A382 - 414
8X-RAY DIFFRACTION8chain 'A' and (resid 415 through 450 )A415 - 450
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 88 )B1 - 88
10X-RAY DIFFRACTION10chain 'B' and (resid 89 through 197 )B89 - 197
11X-RAY DIFFRACTION11chain 'B' and (resid 198 through 273 )B198 - 273
12X-RAY DIFFRACTION12chain 'B' and (resid 274 through 311 )B274 - 311
13X-RAY DIFFRACTION13chain 'B' and (resid 312 through 338 )B312 - 338
14X-RAY DIFFRACTION14chain 'B' and (resid 339 through 401 )B339 - 401
15X-RAY DIFFRACTION15chain 'B' and (resid 402 through 438 )B402 - 438
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 199 )C1 - 199
17X-RAY DIFFRACTION17chain 'C' and (resid 200 through 372 )C200 - 372
18X-RAY DIFFRACTION18chain 'C' and (resid 373 through 440 )C373 - 440
19X-RAY DIFFRACTION19chain 'D' and (resid 1 through 127 )D1 - 127
20X-RAY DIFFRACTION20chain 'D' and (resid 128 through 268 )D128 - 268
21X-RAY DIFFRACTION21chain 'D' and (resid 269 through 311 )D269 - 311
22X-RAY DIFFRACTION22chain 'D' and (resid 312 through 401 )D312 - 401
23X-RAY DIFFRACTION23chain 'D' and (resid 402 through 441 )D402 - 441
24X-RAY DIFFRACTION24chain 'E' and (resid 6 through 46 )E6 - 46
25X-RAY DIFFRACTION25chain 'E' and (resid 47 through 141 )E47 - 141
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 66 )F1 - 66
27X-RAY DIFFRACTION27chain 'F' and (resid 67 through 96 )F67 - 96
28X-RAY DIFFRACTION28chain 'F' and (resid 97 through 184 )F97 - 184
29X-RAY DIFFRACTION29chain 'F' and (resid 185 through 223 )F185 - 223
30X-RAY DIFFRACTION30chain 'F' and (resid 224 through 257 )F224 - 257
31X-RAY DIFFRACTION31chain 'F' and (resid 258 through 339 )F258 - 339
32X-RAY DIFFRACTION32chain 'F' and (resid 340 through 378 )F340 - 378

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