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- PDB-4i50: Crystal structure of tubulin-stathmin-TTL-Epothilone A complex -

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Basic information

Entry
Database: PDB / ID: 4i50
TitleCrystal structure of tubulin-stathmin-TTL-Epothilone A complex
Components
  • Stathmin-4
  • Tubulin Tyrosine Ligase, TTL
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / alpha-tubulin / beta-tubulin / ligase / GTPase / microtubule / stathmin / epothilone A
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 / 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 / cytoplasm / cytosol
Similarity search - Function
Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family ...Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / 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 / 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. / 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 / Dna Ligase; domain 1 / 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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / EPOTHILONE A / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / 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 / Resolution: 2.3 Å
AuthorsProta, A.E. / Bargsten, K. / Zurwerra, D. / Field, J.J. / Diaz, J.F. / Altmann, K.H. / Steinmetz, M.O.
CitationJournal: Science / Year: 2013
Title: Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents.
Authors: Prota, A.E. / Bargsten, K. / Zurwerra, D. / Field, J.J. / Diaz, J.F. / Altmann, K.H. / Steinmetz, M.O.
History
DepositionNov 28, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 13, 2013Group: Database references
Revision 1.2Nov 15, 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, TTL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,65130
Polymers261,6316
Non-polymers4,02024
Water5,513306
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)103.620, 155.130, 180.410
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 / 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) / Strain (production host): NiCo21 (DE3) / References: UniProt: P63043
#4: Protein Tubulin Tyrosine Ligase, TTL


Mass: 44378.496 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Gallus gallus (chicken) / Gene: TTL / Plasmid: PA23_007_ggTTL_KH6_2-378_NSKn1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: E1BQ43

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Non-polymers , 10 types, 330 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.: 6 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 6 / 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.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#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.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: Chemical ChemComp-EP / EPOTHILONE A


Mass: 493.656 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C26H39NO6S
#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


Mass: 18.015 Da / Num. of mol.: 306 / 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: 2.77 Å3/Da / Density % sol: 55.61 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 3% PEG 4000, 4-6% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 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 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 25, 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: 2.3→77.6 Å / Num. all: 129393 / Num. obs: 129393 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 13.6 % / Biso Wilson estimate: 50.3 Å2 / Rmerge(I) obs: 0.133 / Net I/σ(I): 13.8
Reflection shellResolution: 2.3→2.36 Å / Redundancy: 13.8 % / Mean I/σ(I) obs: 1.17 / Num. unique all: 9467 / % possible all: 100

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3RYC, 3TIN

3ryc

3tin


Resolution: 2.3→77.565 Å / SU ML: 0.4 / σ(F): 1.99 / Phase error: 27.14 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2463 6505 5.03 %
Rwork0.1907 --
all0.1935 129393 -
obs0.1935 129379 99.99 %
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 53.763 Å2 / ksol: 0.341 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-1.6336 Å20 Å2-0 Å2
2--11.8387 Å2-0 Å2
3----5.8897 Å2
Refinement stepCycle: LAST / Resolution: 2.3→77.565 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17039 0 240 306 17585
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00517735
X-RAY DIFFRACTIONf_angle_d0.94324055
X-RAY DIFFRACTIONf_dihedral_angle_d15.1846608
X-RAY DIFFRACTIONf_chiral_restr0.0512624
X-RAY DIFFRACTIONf_plane_restr0.0043109
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.32610.40871970.34774010X-RAY DIFFRACTION100
2.3261-2.35350.37422390.31724090X-RAY DIFFRACTION100
2.3535-2.38220.35112410.29733984X-RAY DIFFRACTION100
2.3822-2.41230.32641940.28564091X-RAY DIFFRACTION100
2.4123-2.44410.35012360.284016X-RAY DIFFRACTION100
2.4441-2.47750.35512090.2834089X-RAY DIFFRACTION100
2.4775-2.51290.32792150.26854042X-RAY DIFFRACTION100
2.5129-2.55050.32752050.26424059X-RAY DIFFRACTION100
2.5505-2.59030.3251980.2424138X-RAY DIFFRACTION100
2.5903-2.63280.31752190.2433985X-RAY DIFFRACTION100
2.6328-2.67820.30422050.24844102X-RAY DIFFRACTION100
2.6782-2.72690.30872110.24084096X-RAY DIFFRACTION100
2.7269-2.77930.29952130.22524028X-RAY DIFFRACTION100
2.7793-2.83610.322380.21754036X-RAY DIFFRACTION100
2.8361-2.89770.27472320.20724096X-RAY DIFFRACTION100
2.8977-2.96510.27552230.20794062X-RAY DIFFRACTION100
2.9651-3.03930.25322250.19974050X-RAY DIFFRACTION100
3.0393-3.12150.28332160.19824093X-RAY DIFFRACTION100
3.1215-3.21330.28872150.20544091X-RAY DIFFRACTION100
3.2133-3.3170.27741890.20374115X-RAY DIFFRACTION100
3.317-3.43560.24552130.19374092X-RAY DIFFRACTION100
3.4356-3.57320.24471970.18184127X-RAY DIFFRACTION100
3.5732-3.73580.22872190.18024090X-RAY DIFFRACTION100
3.7358-3.93270.23772050.17034124X-RAY DIFFRACTION100
3.9327-4.17910.21212190.15794136X-RAY DIFFRACTION100
4.1791-4.50170.19732470.14354108X-RAY DIFFRACTION100
4.5017-4.95470.18142150.13364157X-RAY DIFFRACTION100
4.9547-5.67150.21722160.16884169X-RAY DIFFRACTION100
5.6715-7.14470.2622250.19334211X-RAY DIFFRACTION100
7.1447-77.60910.19242290.17924387X-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)
10.164-0.063-0.03470.0577-0.02780.07970.15480.1092-0.0132-0.1492-0.0193-0.085-0.3217-0.04540.01090.4991-0.0090.05740.3271-0.09320.332527.638294.805551.8166
20.031-0.05150.00490.046-0.01170.05250.0483-0.0019-0.1044-0.24930.1641-0.0696-0.1670.17090.00160.4304-0.06290.09940.3988-0.1240.3837.591579.329546.5112
30.1025-0.12740.00090.1322-0.03340.0214-0.0327-0.2334-0.06190.06790.12850.02330.0250.10190.01440.3029-0.00140.03220.3172-0.13330.327532.772775.784858.3307
40.082-0.0826-0.04370.1448-0.05950.19580.172-0.00330.03450.276-0.01920.0548-0.05410.0882-00.38070.01760.02380.3905-0.08530.418820.667182.6165.0644
50.0438-0.00610.04220.0247-0.00470.05370.3065-0.2673-0.02410.0603-0.06920.33510.1908-0.40440.01020.49180.03750.1030.4139-0.13060.4279.613681.861772.4083
60.295-0.00880.12720.012-0.00280.06730.00010.12810.3310.1998-0.04530.2574-0.02480.0464-0.02780.64420.06620.14820.3656-0.15770.418516.279388.964180.7972
70.0711-0.0002-0.00130.12860.05480.07210.19250.00850.11840.1452-0.17790.3333-0.06380.11060.00330.5891-0.00910.08250.3232-0.16120.369817.152687.430874.4604
80.02790.0043-0.00550.0070.02660.02390.0421-0.15930.03950.2173-0.00950.0570.101-0.013100.42780.02360.0450.3176-0.0730.369822.264767.855566.9726
90.11390.06010.09520.05980.00170.19320.02150.1924-0.14090.19370.1153-0.20720.03060.09790.0010.43430.0592-0.03680.2928-0.05240.37332.475260.585862.0884
100.07950.0242-0.01450.0306-0.00750.00010.09530.28960.0022-0.1232-0.1992-0.2063-0.3353-0.2519-00.41760.1005-0.03750.317-0.04810.350815.574171.574222.5713
110.0798-0.0215-0.08310.04850.06830.082-0.08120.302-0.1662-0.26870.0582-0.1607-0.15070.088700.3702-0.0268-0.01470.4187-0.05710.32124.891357.7513.5306
120.0194-0.0303-0.08450.0756-0.00650.2321-0.01980.0035-0.0659-0.0815-0.0185-0.0064-0.1062-0.042800.24070.01350.02120.305-0.10180.319124.706452.085626.4667
130.00320.00620.01050.6455-0.28990.1287-0.1571-0.0128-0.21660.1054-0.0285-0.12530.2148-0.1923-0.16620.2415-0.04150.08460.6017-0.23170.43524.041648.962328.076
140.01370.0122-0.02070.0531-0.04590.0505-0.0179-0.0886-0.09140.0059-0.13170.0701-0.2113-0.1063-0.00250.30690.0771-0.00790.4585-0.13080.392514.70263.214133.6965
150.00280.031-0.00750.3627-0.10150.0327-0.05340.0971-0.05190.115-0.13150.00560.2229-0.2674-0.22180.21230.01540.02790.6192-0.2540.30127.39756.221938.967
160.1291-0.0322-0.03290.0420.05640.0945-0.2672-0.115-0.00070.1843-0.05890.0062-0.0663-0.6907-0.24550.44820.0730.02310.5431-0.19780.40696.663659.210344.9033
170.0688-0.02570.11910.01010.00780.10180.0486-0.22870.0540.0219-0.11680.20960.1464-0.1662-00.3504-0.04650.04470.3631-0.09580.408515.744440.800334.1787
180.04480.1158-0.05110.1244-0.00160.02980.08280.013-0.26110.2327-0.0835-0.05940.24040.2064-0.00150.4172-0.0488-0.05860.3412-0.04050.39225.773737.237432.0743
190.2511-0.0697-0.00440.22170.05520.3825-0.05360.0247-0.0151-0.04430.10240.0001-0.04910.101200.2614-0.05920.02570.3013-0.04540.323120.604432.156-11.9663
200.165-0.1040.11380.38870.48250.6818-0.01-0.01920.08290.0606-0.0415-0.01850.0415-0.1442-0.00230.1948-0.02990.0290.2431-0.06010.27058.260124.92053.1032
210.51190.2643-0.04510.16530.04330.1119-0.2350.66280.1447-0.15090.2358-0.0567-0.060.0817-0.01540.4521-0.08220.1070.6273-0.10780.317122.76055.9162-44.3825
220.2283-0.0425-0.23240.34720.24690.7378-0.08940.1403-0.03280.00930.0912-0.04360.1462-0.10150.03780.3712-0.02320.03560.391-0.11140.337216.2202-5.7442-27.3108
230.05350.03160.05690.02830.02950.05420.0605-0.09340.16210.04460.06640.01270.09210.2660.06371.0212-0.12150.00870.5651-0.19210.423826.976190.944982.4349
240.0774-0.10140.0335-0.06840.1159-0.0421-0.04370.01290.04450.03890.0463-0.04020.04890.1762-0.32590.14660.1830.3410.1519-0.59940.047243.343927.01253.9924
250.1871-0.0165-0.1120.01260.05550.0765-0.2770.211-0.10070.09580.11660.09510.3501-0.0565-0.00470.6308-0.06670.14180.441-0.15450.42446.21352.762369.9951
260.17970.0227-0.06290.18620.02890.0686-0.1192-0.1507-0.2545-0.0988-0.02990.06890.17320.4342-0.02160.43390.08870.04470.57180.19220.49.756855.9078102.8968
270.0459-0.0607-0.06090.08240.10410.12680.00390.0017-0.07070.2304-0.0574-0.02620.0424-0.0725-0.06241.20080.10830.41630.2910.12940.802-1.535440.32697.5473
280.2337-0.1439-0.15660.05760.05380.1832-0.26420.074-0.38060.02750.1449-0.26410.1834-0.1159-0.00120.6142-0.00230.13980.42290.02610.4371-4.007356.242590.3411
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:88)
2X-RAY DIFFRACTION2chain 'A' and (resseq 89:128)
3X-RAY DIFFRACTION3chain 'A' and (resseq 129:199)
4X-RAY DIFFRACTION4chain 'A' and (resseq 200:273)
5X-RAY DIFFRACTION5chain 'A' and (resseq 274:311)
6X-RAY DIFFRACTION6chain 'A' and (resseq 312:337)
7X-RAY DIFFRACTION7chain 'A' and (resseq 338:372)
8X-RAY DIFFRACTION8chain 'A' and (resseq 373:401)
9X-RAY DIFFRACTION9chain 'A' and (resseq 402:438)
10X-RAY DIFFRACTION10chain 'B' and (resseq 2:64)
11X-RAY DIFFRACTION11chain 'B' and (resseq 65:127)
12X-RAY DIFFRACTION12chain 'B' and (resseq 128:199)
13X-RAY DIFFRACTION13chain 'B' and (resseq 200:223)
14X-RAY DIFFRACTION14chain 'B' and (resseq 224:259)
15X-RAY DIFFRACTION15chain 'B' and (resseq 260:295)
16X-RAY DIFFRACTION16chain 'B' and (resseq 296:373)
17X-RAY DIFFRACTION17chain 'B' and (resseq 374:401)
18X-RAY DIFFRACTION18chain 'B' and (resseq 402:440)
19X-RAY DIFFRACTION19chain 'C' and (resseq 1:197)
20X-RAY DIFFRACTION20chain 'C' and (resseq 198:440)
21X-RAY DIFFRACTION21chain 'D' and (resseq 2:128)
22X-RAY DIFFRACTION22chain 'D' and (resseq 129:441)
23X-RAY DIFFRACTION23chain 'E' and (resseq 6:46)
24X-RAY DIFFRACTION24chain 'E' and (resseq 47:143)
25X-RAY DIFFRACTION25chain 'F' and (resseq 1:66)
26X-RAY DIFFRACTION26chain 'F' and (resseq 67:216)
27X-RAY DIFFRACTION27chain 'F' and (resseq 217:263)
28X-RAY DIFFRACTION28chain 'F' and (resseq 264:379)

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