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- PDB-4o2a: Tubulin-BAL27862 complex -

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Basic information

Entry
Database: PDB / ID: 4o2a
TitleTubulin-BAL27862 complex
Components
  • Stathmin-4
  • TUBULIN-TYROSINE LIGASE
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE/INHIBITOR / ALPHA-TUBULIN / BETA-TUBULIN / LIGASE / GTPASE / MICROTUBULE / STATHMIN / BAL27862 / CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / 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 / 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 / cytoplasm / cytosol
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 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 ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 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. / ATP-grasp fold, A domain / 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. / Dna Ligase; domain 1 / 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 non-globular / Special / Helix Hairpins / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-2RR / ADENOSINE-5'-DIPHOSPHATE / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / DIFFERENCE FOURIER / Resolution: 2.5 Å
AuthorsProta, A.E. / Franck, D. / Bachmann, F. / Bargsten, K. / Buey, R.M. / Pohlmann, J. / Reinelt, S. / Lane, H. / Steinmetz, M.O.
CitationJournal: J.Mol.Biol. / Year: 2014
Title: The Novel Microtubule-Destabilizing Drug BAL27862 Binds to the Colchicine Site of Tubulin with Distinct Effects on Microtubule Organization.
Authors: Prota, A.E. / Danel, F. / Bachmann, F. / Bargsten, K. / Buey, R.M. / Pohlmann, J. / Reinelt, S. / Lane, H. / Steinmetz, M.O.
History
DepositionDec 17, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 5, 2014Provider: repository / Type: Initial release
Revision 1.1Apr 16, 2014Group: Database references
Revision 1.2Nov 22, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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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)265,44026
Polymers261,6316
Non-polymers3,80820
Water6,017334
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.530, 158.120, 179.730
Angle α, β, γ (deg.)90.00, 90.00, 90.00
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 / Details: BRAIN / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: BRAIN / Source: (natural) Bos taurus (domestic cattle) / 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


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, 354 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.: 4 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


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


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#11: 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
#12: Chemical ChemComp-2RR / 3-[(4-{1-[2-(4-aminophenyl)-2-oxoethyl]-1H-benzimidazol-2-yl}-1,2,5-oxadiazol-3-yl)amino]propanenitrile


Mass: 387.395 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H17N7O2
#13: 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
#14: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#15: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 334 / Source method: isolated from a natural source / Formula: H2O

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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: 2.84 Å3/Da / Density % sol: 56.67 %
Crystal growTemperature: 293 K / pH: 6.7
Details: 6% PEG 4K, 4% glycerol, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES/Imidazole , pH 6.7, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1.00001
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 23, 2012
RadiationMonochromator: LN2 COOLED FIXED-EXIT SI(111) MONOCHROMATOR, SAGITTALLY - HORIZONTALLY FOCUSSED
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00001 Å / Relative weight: 1
ReflectionResolution: 2.5→59.4 Å / Num. obs: 103225 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 13.6 % / Rmerge(I) obs: 0.142 / Net I/σ(I): 13.5
Reflection shellResolution: 2.5→2.56 Å / Redundancy: 14.1 % / Rmerge(I) obs: 2.268 / Mean I/σ(I) obs: 1.2 / % possible all: 99.4

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: PDB ENTRY 4I4T

4i4t


Resolution: 2.5→59.36 Å / SU ML: 0.37 / σ(F): 1.99 / Phase error: 24.99 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.232 5150 4.99 %
Rwork0.194 --
obs0.196 103200 99.7 %
all-103487 -
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.5→59.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17211 0 238 334 17783
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00218147
X-RAY DIFFRACTIONf_angle_d0.73724687
X-RAY DIFFRACTIONf_dihedral_angle_d12.9726825
X-RAY DIFFRACTIONf_chiral_restr0.0462694
X-RAY DIFFRACTIONf_plane_restr0.0033201
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5-2.52850.35511670.32953233X-RAY DIFFRACTION100
2.5285-2.55820.38861830.31833168X-RAY DIFFRACTION99
2.5582-2.58940.34821650.29493251X-RAY DIFFRACTION100
2.5894-2.62220.33851650.29563200X-RAY DIFFRACTION99
2.6222-2.65670.33971660.28643230X-RAY DIFFRACTION100
2.6567-2.69310.33061640.27783253X-RAY DIFFRACTION99
2.6931-2.73150.30931690.26733234X-RAY DIFFRACTION100
2.7315-2.77230.29961950.26023181X-RAY DIFFRACTION99
2.7723-2.81560.30321790.25753256X-RAY DIFFRACTION100
2.8156-2.86180.29211660.25233202X-RAY DIFFRACTION99
2.8618-2.91110.30671440.25193284X-RAY DIFFRACTION99
2.9111-2.96410.27321620.24283262X-RAY DIFFRACTION100
2.9641-3.02110.25261600.21763224X-RAY DIFFRACTION100
3.0211-3.08270.25141760.21453258X-RAY DIFFRACTION100
3.0827-3.14980.28561580.22623276X-RAY DIFFRACTION100
3.1498-3.2230.32371580.22153255X-RAY DIFFRACTION100
3.223-3.30360.27981570.20793260X-RAY DIFFRACTION100
3.3036-3.3930.24922010.20453226X-RAY DIFFRACTION100
3.393-3.49280.23391820.19743257X-RAY DIFFRACTION100
3.4928-3.60550.22611840.19423247X-RAY DIFFRACTION100
3.6055-3.73430.21831660.17993302X-RAY DIFFRACTION100
3.7343-3.88380.21711730.16773252X-RAY DIFFRACTION100
3.8838-4.06060.20571630.16323297X-RAY DIFFRACTION100
4.0606-4.27460.19821730.1643290X-RAY DIFFRACTION100
4.2746-4.54230.18141720.15153309X-RAY DIFFRACTION100
4.5423-4.89290.17381850.14693286X-RAY DIFFRACTION100
4.8929-5.3850.20761820.16163306X-RAY DIFFRACTION100
5.385-6.16350.2171710.18043374X-RAY DIFFRACTION100
6.1635-7.76260.22051830.18723356X-RAY DIFFRACTION100
7.7626-59.37510.19581810.18373521X-RAY DIFFRACTION100
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)
10.01490.00810.01520.0090.01370.02850.12540.02410.0892-0.01760.0262-0.0868-0.14040.07070.09880.4664-0.15350.18720.1684-0.33150.068728.623498.929954.5988
20.012-0.0157-0.01240.04450.0330.05020.02790.02480.0159-0.18430.1234-0.2074-0.23290.22840.12040.2607-0.1060.2060.1721-0.47740.164334.479183.030348.53
30.0210.0022-0.04140.0867-0.07760.1460.0725-0.0188-0.00880.13530.0727-0.072-0.15870.16070.07180.22070.00170.00810.2608-0.15070.305724.049280.875362.9179
40.0295-0.02780.0260.039-0.02640.04770.1681-0.08270.07770.07720.00330.08660.0003-0.12520.04870.39380.04870.15440.3128-0.13440.33889.091384.550671.6873
50.0185-0.0176-0.01360.02030.01950.0164-0.0011-0.04610.06120.0691-0.02890.0771-0.0287-0.0301-0.02870.53850.07060.18140.3617-0.22930.226816.638390.346780.4947
60.01870.0147-0.01120.0268-0.00850.02090.0588-0.01010.09290.14540.05060.1231-0.05050.03560.00150.463-0.02230.03950.3171-0.08510.27617.655789.741773.7423
70.01380.00910.01720.03210.02350.06150.1304-0.05420.03220.0550.04360.06180.00090.05880.01110.24260.05220.05310.2479-0.10.279722.430669.579766.7995
80.01780.00480.04230.0278-0.01250.108-0.04850.1143-0.16880.10630.0911-0.09510.02750.1279-0.00090.2530.1419-0.03960.2303-0.19460.312431.174861.032562.98
90.2779-0.1015-0.0540.16550.12220.4031-0.00060.2490.2662-0.0468-0.1530.0722-0.2237-0.1556-0.49740.20390.04380.08690.2019-0.25310.28517.353859.603726.1582
100.0403-0.0280.03220.07890.02450.102-0.0532-0.0966-0.00510.18810.00450.10070.0847-0.11980.00620.13560.00990.03390.2916-0.12340.1914.706150.063138.6037
110.04480.01580.00230.0301-0.02720.0333-0.00010.0690.235-0.04540.05170.0495-0.21930.01770.0170.1835-0.0390.01790.14070.0020.189814.570642.6963-13.0121
120.03770.0033-0.01570.0245-0.00150.0177-0.02430.14880.0047-0.21520.0627-0.0189-0.06930.02570.0577-0.0864-0.17530.07820.1431-0.03620.102424.913930.8443-14.496
130.0075-0.02330.01030.0659-0.06090.0616-0.07860.00610.0109-0.0601-0.06750.03610.02390.0548-0.12660.1479-0.0301-0.02040.1022-0.09690.210620.479420.7719-3.7727
140.05050.0455-0.06860.1321-0.01410.29310.09530.00330.17380.0721-0.03830.0644-0.0366-0.36310.09550.08260.01780.05270.1595-0.10380.19323.641728.86250.3348
150.01450.0370.01380.08520.02420.0441-0.0415-0.13270.0725-0.0162-0.10360.13410.0676-0.0998-0.03730.1197-0.01390.02490.1761-0.07070.17781.195734.99478.7602
160.057-0.0264-0.03740.06390.07010.1125-0.0817-0.00170.00170.22150.012-0.02710.170.084-0.01010.16450.0003-0.01350.1422-0.050.187620.59113.44972.3452
170.0910.0051-0.00170.0048-0.0019-0.0008-0.03480.20680.1083-0.03420.12250.0093-0.0875-0.1340.00140.4485-0.137-0.01340.62480.01660.206715.065811.8702-41.1057
180.0517-0.0224-0.05240.03940.00470.0497-0.08990.33810.0523-0.30980.0376-0.12040.0780.0217-0.0820.4887-0.14670.18420.6999-0.22650.205928.66212.9771-43.3471
190.0513-0.0308-0.01410.05520.01090.0313-0.06810.076-0.0053-0.12190.034-0.09920.1617-0.0175-0.03720.3519-0.19410.10280.3514-0.34420.222521.9629-8.2988-32.5288
200.0009-0.0023-0.00270.00210.00540.00460.03780.02540.0347-0.01290.02770.02330.0231-0.0505-00.5911-0.1873-0.10650.7072-0.12630.30237.0338-7.6446-39.077
210.00640.0107-0.00850.0079-0.00870.0148-0.00680.166-0.06250.00710.0926-0.020.0710.04990.00070.220.00130.0550.2145-0.07910.220318.31186.7632-23.3753
220.0023-0.0050.00450.00940.00180.005-0.02520.01050.01-0.0162-0.01030.07610.0614-0.06430.02150.3589-0.1320.02430.4023-0.25820.25834.137-5.8981-23.8356
230.00670.00070.00310.00460.00680.00080.00540.09440.00590.00950.10160.0576-0.0465-0.079300.40110.0225-0.01470.56780.03410.35981.79855.3646-18.8359
240.06420.09180.05710.12260.06110.0621-0.01310.2146-0.1784-0.06530.3007-0.14960.15060.07080.26090.4159-0.10830.17980.2474-0.43740.260118.0872-9.3495-25.9508
250.0055-0.0030.0089-0.0004-0.00010.00670.05640.0526-0.07620.06820.0287-0.04120.03910.0749-00.42470.0330.06470.3048-0.15360.377326.9986-13.103-17.3055
260.0192-0.01180.01780.00250.01570.01960.0588-0.00470.10270.14910.02860.0767-0.04170.14890.00010.6044-0.07020.0040.3969-0.17970.341727.902592.629281.4604
270.1758-0.0690.03060.01350.0240.0033-0.0197-0.09040.028-0.01480.0896-0.02560.11390.10970.08410.13980.06620.20880.4225-0.4290.332143.038227.93963.7485
280.25010.1457-0.24870.1272-0.11290.2916-0.344-0.252-0.5277-0.11050.1075-0.22960.43430.4297-0.06360.42960.13910.08750.36510.10520.31699.799557.033191.0614
290.10920.032-0.01370.0150.00090.0446-0.02660.0461-0.21170.11940.0506-0.05770.1793-0.03470.01290.64780.07480.22660.20810.13010.5328-1.613346.0713100.0894
300.24830.0591-0.060.03410.00820.1423-0.187-0.0038-0.20140.20890.2369-0.03780.1226-0.11760.02940.52830.06840.17210.19850.0580.2838-2.433259.883488.6362
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 64 )
2X-RAY DIFFRACTION2chain 'A' and (resid 65 through 160 )
3X-RAY DIFFRACTION3chain 'A' and (resid 161 through 273 )
4X-RAY DIFFRACTION4chain 'A' and (resid 274 through 311 )
5X-RAY DIFFRACTION5chain 'A' and (resid 312 through 338 )
6X-RAY DIFFRACTION6chain 'A' and (resid 339 through 372 )
7X-RAY DIFFRACTION7chain 'A' and (resid 373 through 401 )
8X-RAY DIFFRACTION8chain 'A' and (resid 402 through 450 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 311 )
10X-RAY DIFFRACTION10chain 'B' and (resid 312 through 438 )
11X-RAY DIFFRACTION11chain 'C' and (resid 1 through 72 )
12X-RAY DIFFRACTION12chain 'C' and (resid 73 through 161 )
13X-RAY DIFFRACTION13chain 'C' and (resid 162 through 199 )
14X-RAY DIFFRACTION14chain 'C' and (resid 200 through 311 )
15X-RAY DIFFRACTION15chain 'C' and (resid 312 through 372 )
16X-RAY DIFFRACTION16chain 'C' and (resid 373 through 440 )
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 56 )
18X-RAY DIFFRACTION18chain 'D' and (resid 57 through 160 )
19X-RAY DIFFRACTION19chain 'D' and (resid 161 through 214 )
20X-RAY DIFFRACTION20chain 'D' and (resid 215 through 238 )
21X-RAY DIFFRACTION21chain 'D' and (resid 239 through 268 )
22X-RAY DIFFRACTION22chain 'D' and (resid 269 through 311 )
23X-RAY DIFFRACTION23chain 'D' and (resid 312 through 337 )
24X-RAY DIFFRACTION24chain 'D' and (resid 338 through 415 )
25X-RAY DIFFRACTION25chain 'D' and (resid 416 through 441 )
26X-RAY DIFFRACTION26chain 'E' and (resid 6 through 46 )
27X-RAY DIFFRACTION27chain 'E' and (resid 47 through 143 )
28X-RAY DIFFRACTION28chain 'F' and (resid 1 through 207 )
29X-RAY DIFFRACTION29chain 'F' and (resid 208 through 275 )
30X-RAY DIFFRACTION30chain 'F' and (resid 276 through 379 )

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