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- PDB-4ihj: Crystal structure of tubulin-stathmin-TTL-ADP complex -

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Basic information

Entry
Database: PDB / ID: 4ihj
TitleCrystal structure of tubulin-stathmin-TTL-ADP 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
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / double-stranded RNA binding / mitotic cell cycle / nervous system development / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
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-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / 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-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / 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; / 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 / 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
ADENOSINE-5'-DIPHOSPHATE / 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 / Difference Fourier / Resolution: 2 Å
AuthorsProta, A.E. / Magiera, M.M. / Kuijpers, M. / Bargsten, K. / Frey, D. / Wieser, M. / Jaussi, R. / Hoogenraad, C.C. / Kammerer, R.A. / Janke, C. / Steinmetz, M.O.
CitationJournal: J.Cell Biol. / Year: 2013
Title: Structural basis of tubulin tyrosination by tubulin tyrosine ligase.
Authors: Prota, A.E. / Magiera, M.M. / Kuijpers, M. / Bargsten, K. / Frey, D. / Wieser, M. / Jaussi, R. / Hoogenraad, C.C. / Kammerer, R.A. / Janke, C. / Steinmetz, M.O.
History
DepositionDec 18, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 13, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 20, 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)264,51326
Polymers261,3056
Non-polymers3,20820
Water18,6091033
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.520, 157.310, 180.990
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: 50041.273 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 / Plasmid: pET3d / 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 , 9 types, 1053 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-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 7 / 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 / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: 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
#10: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#11: Chemical ChemComp-ADP / ADENOSINE-5'-DIPHOSPHATE / Adenosine diphosphate


Mass: 427.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O10P2 / Comment: ADP, energy-carrying molecule*YM
#12: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#13: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1033 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsBRAIN TUBULIN PREPARATIONS CONTAIN THREE TUBULIN SUBPOPULATIONS: TYROSINATED (20-30%), DE- ...BRAIN TUBULIN PREPARATIONS CONTAIN THREE TUBULIN SUBPOPULATIONS: TYROSINATED (20-30%), DE-TYROSINATED (30-40%) AND DELTA-2 TUBULIN (ABOUT 40%) (LACKING THE CARBOXYTERMINAL GLUTAMYL-TYROSINE). TUBULIN-TYROSINE LIGASE BINDS ALL THREE VARIANTS, BUT ONLY CAN MODIFY DE-TYROSINATED TUBULIN. ALTHOUGH ALL SUBPOPULATIONS ARE PRESENT IN THE CRYSTAL, ONLY THE DE-TYROSINATED FORM WAS MODELED WITH A TERMINAL CARBOXYLATE TO DESCRIBE THE LIGASE REACTION. IN THE SEQRES RECORD FOR CHAIN A THE TERMINAL TYR WAS OMITTED TO MATCH THE MODELED VARIANT OF ALPHA-TUBULIN.

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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: 2.85 Å3/Da / Density % sol: 56.8 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 4-10% 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: 0.99995 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Dec 15, 2011
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: 0.99995 Å / Relative weight: 1
ReflectionResolution: 2→72.137 Å / Num. all: 200646 / Num. obs: 198918 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 26.8 % / Biso Wilson estimate: 36.2 Å2 / Net I/σ(I): 13.3
Reflection shellResolution: 2→2.05 Å / Redundancy: 25.2 % / Mean I/σ(I) obs: 1.17 / Num. unique all: 13684 / % possible all: 92.5

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHENIX(phenix.refine: 1.7.3_928)model building
PHENIX(phenix.refine: 1.7.3_928)refinement
XDSdata reduction
XDSdata scaling
PHENIX1.7.3_928phasing
RefinementMethod to determine structure: Difference Fourier
Starting model: PDB entry 4I4T

4i4t


Resolution: 2→72.1 Å / SU ML: 0.31 / σ(F): 2 / Phase error: 22.19 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2174 10028 5.04 %RANDOM
Rwork0.1677 ---
obs0.1702 198893 99.13 %-
all-198918 --
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 38.273 Å2 / ksol: 0.324 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-5.2872 Å20 Å2-0 Å2
2--4.9205 Å2-0 Å2
3----0.3361 Å2
Refinement stepCycle: LAST / Resolution: 2→72.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17356 0 189 1033 18578
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00818119
X-RAY DIFFRACTIONf_angle_d1.1424607
X-RAY DIFFRACTIONf_dihedral_angle_d15.7176771
X-RAY DIFFRACTIONf_chiral_restr0.0632687
X-RAY DIFFRACTIONf_plane_restr0.0053191
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.0240.32472940.31155333X-RAY DIFFRACTION85
2.024-2.04780.32413530.28776215X-RAY DIFFRACTION99
2.0478-2.07280.31193250.27036268X-RAY DIFFRACTION100
2.0728-2.0990.32013520.27346219X-RAY DIFFRACTION99
2.099-2.12660.31753480.26256251X-RAY DIFFRACTION99
2.1266-2.15580.30053110.2456225X-RAY DIFFRACTION99
2.1558-2.18660.29083170.23036245X-RAY DIFFRACTION99
2.1866-2.21920.26123390.21976284X-RAY DIFFRACTION99
2.2192-2.25390.2913170.22516284X-RAY DIFFRACTION100
2.2539-2.29080.28663360.21526247X-RAY DIFFRACTION99
2.2908-2.33030.28263490.20776223X-RAY DIFFRACTION99
2.3303-2.37270.25373370.19336315X-RAY DIFFRACTION100
2.3727-2.41830.24713450.19196266X-RAY DIFFRACTION100
2.4183-2.46770.24523410.1796286X-RAY DIFFRACTION99
2.4677-2.52140.25383220.18116302X-RAY DIFFRACTION100
2.5214-2.580.24833380.17156290X-RAY DIFFRACTION100
2.58-2.64450.22113290.16046284X-RAY DIFFRACTION100
2.6445-2.71610.22993190.16966346X-RAY DIFFRACTION100
2.7161-2.7960.23243760.16886272X-RAY DIFFRACTION100
2.796-2.88620.22063190.15976366X-RAY DIFFRACTION100
2.8862-2.98940.23192930.16336354X-RAY DIFFRACTION100
2.9894-3.10910.21933400.15736362X-RAY DIFFRACTION100
3.1091-3.25060.21663090.16766378X-RAY DIFFRACTION100
3.2506-3.4220.23093580.176355X-RAY DIFFRACTION100
3.422-3.63630.22193470.16076380X-RAY DIFFRACTION100
3.6363-3.91710.17443400.14056376X-RAY DIFFRACTION100
3.9171-4.31120.17123220.12626452X-RAY DIFFRACTION100
4.3112-4.9350.14183510.10426449X-RAY DIFFRACTION100
4.935-6.2170.17513460.14276510X-RAY DIFFRACTION100
6.217-72.18430.22113550.19036728X-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)
10.5101-0.0835-0.09241.58341.10651.30850.00350.06170.1199-0.32940.2287-0.2683-0.50.3-0.01640.4182-0.15870.12970.284-0.22820.218331.65987.93751.9643
20.9079-0.3028-0.15792.59481.27822.98730.0353-0.04360.00930.2395-0.01190.1123-0.0941-0.0432-0.02110.258-0.00830.04820.1777-0.0710.186819.014582.091965.8993
30.5794-0.2653-0.09252.58411.37581.57130.0285-0.11090.04440.3640.01080.13640.0037-0.03780.00210.32770.00610.07160.1529-0.08880.147218.738483.064473.4024
41.3406-0.7103-1.62513.06413.37125.1389-0.1348-0.1605-0.10770.69510.3529-0.23950.74980.822-0.29060.39840.147-0.08460.2961-0.15030.324132.61261.603360.6618
50.1661-0.0926-0.03030.05160.01690.00550.6976-0.22480.18790.1996-0.5256-0.3005-0.28850.4644-0.03131.55480.02550.43710.64540.15250.731715.920255.816286.6999
63.8693-1.5353-0.71135.99131.37292.87210.1340.26650.5636-0.5226-0.14980.1607-0.7958-0.29030.01730.30430.069-0.00220.2391-0.00210.213816.331569.819119.6074
72.4702-0.0183-1.53917.2315-1.07983.92430.1150.35710.0739-0.54820.0418-0.3689-0.41420.2359-0.15130.2039-0.00230.03710.3714-0.05750.154629.069256.020214.6375
81.98921.43720.24244.7821.90772.69580.0347-0.06430.117-0.08010.0229-0.0593-0.16240.1277-0.05790.1270.01240.03940.2173-0.10030.191524.324752.939226.1239
92.2694-0.57960.87870.324-0.14051.145-0.1724-0.2756-0.0323-0.0169-0.17520.37460.2349-0.64020.23030.2303-0.06620.07110.4798-0.26630.39775.390150.718128.3365
100.9353-0.6384-0.49921.01580.49121.274-0.02480.0160.09650.0006-0.13450.2099-0.1694-0.38730.11610.18820.01680.01090.2607-0.14370.281310.857161.485535.9041
112.3272-1.1790.35372.57730.41062.4061-0.214-0.19470.0870.3759-0.10670.37250.0079-0.76540.23130.2494-0.00790.06410.4177-0.1620.31056.526260.673744.8953
121.646-2.9973-2.44096.68935.59334.8287-0.1446-0.0926-0.12350.5487-0.0490.47510.5706-0.04480.2270.2094-0.05820.02880.2149-0.07590.172415.173142.048134.0991
131.6952-1.2002-1.22253.91314.18897.2517-0.1333-0.3087-0.00030.74920.1945-0.07260.75260.6876-0.03010.24260.0146-0.03070.2269-0.04940.212625.467137.93831.0252
141.1251-0.46120.03322.90670.18171.446-0.04780.14970.1052-0.29740.0925-0.0855-0.09770.1606-0.02530.1412-0.05850.01890.206-0.01760.134920.256632.9624-12.0932
151.1614-0.49260.13571.35990.60561.4622-0.0050.01830.02870.0799-0.05140.0920.1206-0.19240.05120.127-0.0510.02930.1492-0.01830.15887.579125.99753.0136
162.505-1.1479-0.08492.57960.7833.18030.08140.50930.0709-0.6448-0.0914-0.0099-0.1524-0.1070.00560.4366-0.0770.03810.4551-0.0820.073617.2319.6929-44.2927
170.6401-0.2454-0.05541.18480.60721.3486-0.04090.3376-0.1586-0.36990.0524-0.10680.2470.0245-0.04510.4389-0.06030.11790.3652-0.3010.165720.7432-2.2113-33.7118
181.4379-0.2283-0.20771.92740.87181.9173-0.13570.3122-0.2664-0.096-0.01270.18260.3507-0.16980.17220.4088-0.1070.03960.303-0.13310.20448.8398-3.8145-21.3748
191.887-0.5884-0.40341.8267-0.02060.3838-0.02940.0992-0.3589-0.02720.0449-0.19680.50350.28790.08680.57960.0820.07060.3122-0.21830.409230.1409-16.3148-24.4583
202.0574-1.4573-0.93283.07042.02772.6405-0.2299-0.2382-0.09930.77040.3029-0.15760.45490.5268-0.07250.5142-0.0123-0.03640.31-0.11590.241927.275792.438582.1073
210.3008-0.089-0.13611.12731.09121.6297-0.0918-0.0202-0.03770.11870.2916-0.3010.32940.5047-0.32790.16810.06140.06380.3981-0.23740.331842.591928.36324.7056
221.36471.30590.33573.8120.94242.3773-0.2160.2448-0.50350.05880.0636-0.15850.8806-0.2237-0.01630.6743-0.06690.15360.319-0.14230.34896.13854.514770.1511
231.4568-0.72380.8712.5608-1.16183.0364-0.1267-0.7654-0.27720.9063-0.3437-0.86110.12561.40650.5450.77340.086-0.11050.9440.26360.563215.007258.5899106.0349
241.47930.673-1.15751.2157-0.30791.7958-0.2557-0.1437-0.49970.2480.1342-0.04710.4027-0.0254-0.02620.66550.05760.15960.16680.08240.3598-1.795654.365394.0289
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 1:180)
2X-RAY DIFFRACTION2CHAIN A AND (RESSEQ 181:311)
3X-RAY DIFFRACTION3CHAIN A AND (RESSEQ 312:401)
4X-RAY DIFFRACTION4CHAIN A AND (RESSEQ 402:436)
5X-RAY DIFFRACTION5CHAIN A AND (RESSEQ 437:450)
6X-RAY DIFFRACTION6CHAIN B AND (RESSEQ 1:88)
7X-RAY DIFFRACTION7CHAIN B AND (RESSEQ 89:127)
8X-RAY DIFFRACTION8CHAIN B AND (RESSEQ 128:197)
9X-RAY DIFFRACTION9CHAIN B AND (RESSEQ 198:223)
10X-RAY DIFFRACTION10CHAIN B AND (RESSEQ 224:295)
11X-RAY DIFFRACTION11CHAIN B AND (RESSEQ 296:373)
12X-RAY DIFFRACTION12CHAIN B AND (RESSEQ 374:401)
13X-RAY DIFFRACTION13CHAIN B AND (RESSEQ 402:438)
14X-RAY DIFFRACTION14CHAIN C AND (RESSEQ 1:197)
15X-RAY DIFFRACTION15CHAIN C AND (RESSEQ 198:440)
16X-RAY DIFFRACTION16CHAIN D AND (RESSEQ 2:88)
17X-RAY DIFFRACTION17CHAIN D AND (RESSEQ 89:295)
18X-RAY DIFFRACTION18CHAIN D AND (RESSEQ 296:401)
19X-RAY DIFFRACTION19CHAIN D AND (RESSEQ 402:441)
20X-RAY DIFFRACTION20CHAIN E AND (RESSEQ 6:46)
21X-RAY DIFFRACTION21CHAIN E AND (RESSEQ 47:141)
22X-RAY DIFFRACTION22CHAIN F AND (RESSEQ 1:66)
23X-RAY DIFFRACTION23CHAIN F AND (RESSEQ 67:198)
24X-RAY DIFFRACTION24CHAIN F AND (RESSEQ 199:384)

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