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- PDB-4i4t: Crystal structure of tubulin-RB3-TTL-Zampanolide complex -

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Basic information

Entry
Database: PDB / ID: 4i4t
TitleCrystal structure of tubulin-RB3-TTL-Zampanolide complex
Components
  • Stathmin-4
  • Tubulin Tyrosine ligase, TTL
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / Alpha-tubulin / beta-tubulin / ligase / GTPase / stathmin / zamanolide
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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / TYROSINE / Chem-ZPN / 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: 1.8 Å
AuthorsProta, A.E. / Steinmetz, M.O.
Citation
Journal: 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.
#1: Journal: 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
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 1.2Feb 20, 2013Group: Database references
Revision 1.3Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Sep 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.pdbx_leaving_atom_flag / _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)265,60332
Polymers261,3056
Non-polymers4,29826
Water27,4191522
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.770, 158.640, 179.240
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 / Production host: Escherichia coli (E. coli) / 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 / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 11 types, 1548 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.: 6 / 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-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C3H8O3
#10: 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
#11: Chemical ChemComp-TYR / TYROSINE / Tyrosine


Type: L-peptide linking / Mass: 181.189 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C9H11NO3
#12: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#13: Chemical ChemComp-ZPN / (2Z,4E)-N-[(S)-[(1S,2E,5S,8E,10Z,17S)-3,11-dimethyl-19-methylidene-7,13-dioxo-6,21-dioxabicyclo[15.3.1]henicosa-2,8,10-trien-5-yl](hydroxy)methyl]hexa-2,4-dienamide / (-)-ZAMPANOLIDE (Bound form)


Mass: 497.623 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H39NO6
#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 / Water


Mass: 18.015 Da / Num. of mol.: 1522 / 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: 56.86 %
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: 0.99995 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jan 29, 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: 0.99995 Å / Relative weight: 1
ReflectionResolution: 1.8→79.4 Å / Num. all: 275149 / Num. obs: 274535 / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 13.5 % / Biso Wilson estimate: 33.12 Å2 / Rmerge(I) obs: 0.103 / Net I/σ(I): 13.35
Reflection shellResolution: 1.8→1.85 Å / Redundancy: 13.1 % / Mean I/σ(I) obs: 1 / % possible all: 99

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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: 1.8→79.32 Å / SU ML: 0.3 / σ(F): 1.99 / Phase error: 21.04 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2043 13945 5.08 %
Rwork0.1711 --
obs0.1728 274515 99.77 %
all-274535 -
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.35 Å2 / ksol: 0.33 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-3.1254 Å2-0 Å2-0 Å2
2---0.3509 Å2-0 Å2
3----2.1148 Å2
Refinement stepCycle: LAST / Resolution: 1.8→79.32 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17547 0 265 1522 19334
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00818680
X-RAY DIFFRACTIONf_angle_d1.17925453
X-RAY DIFFRACTIONf_dihedral_angle_d14.7037082
X-RAY DIFFRACTIONf_chiral_restr0.0692788
X-RAY DIFFRACTIONf_plane_restr0.0053306
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.82050.34554730.33688477X-RAY DIFFRACTION99
1.8205-1.84190.33274700.32218551X-RAY DIFFRACTION99
1.8419-1.86430.34684910.32028599X-RAY DIFFRACTION100
1.8643-1.88790.3414470.31888600X-RAY DIFFRACTION99
1.8879-1.91280.33964160.29978591X-RAY DIFFRACTION99
1.9128-1.9390.3274900.29548594X-RAY DIFFRACTION100
1.939-1.96670.3034990.27528553X-RAY DIFFRACTION100
1.9667-1.99610.26424780.2518600X-RAY DIFFRACTION100
1.9961-2.02720.26114480.23498642X-RAY DIFFRACTION100
2.0272-2.06050.27575020.2298582X-RAY DIFFRACTION100
2.0605-2.0960.25014480.21678621X-RAY DIFFRACTION100
2.096-2.13410.23514760.19848633X-RAY DIFFRACTION100
2.1341-2.17520.22134370.18088654X-RAY DIFFRACTION100
2.1752-2.21960.21624620.17578633X-RAY DIFFRACTION100
2.2196-2.26790.21134430.17778706X-RAY DIFFRACTION100
2.2679-2.32060.21524830.16698632X-RAY DIFFRACTION100
2.3206-2.37860.20174470.16298692X-RAY DIFFRACTION100
2.3786-2.4430.18984880.15418668X-RAY DIFFRACTION100
2.443-2.51490.20324440.1518668X-RAY DIFFRACTION100
2.5149-2.5960.20364710.16268694X-RAY DIFFRACTION100
2.596-2.68880.20664480.16488736X-RAY DIFFRACTION100
2.6888-2.79650.2174850.16698662X-RAY DIFFRACTION100
2.7965-2.92380.20834360.16178761X-RAY DIFFRACTION100
2.9238-3.07790.18384380.168753X-RAY DIFFRACTION100
3.0779-3.27080.20414360.16868789X-RAY DIFFRACTION100
3.2708-3.52330.20764980.17018759X-RAY DIFFRACTION100
3.5233-3.87780.18524630.15448798X-RAY DIFFRACTION100
3.8778-4.43890.15414460.12658840X-RAY DIFFRACTION100
4.4389-5.59240.15064910.12838903X-RAY DIFFRACTION100
5.5924-79.39710.21394910.18689179X-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)
11.025-0.2207-0.45762.11110.76571.71590.04980.06560.1381-0.17340.0893-0.1241-0.38310.1574-0.12230.3086-0.04490.05690.246-0.07610.224231.606288.552151.3548
20.53850.0947-0.22281.53280.72091.92230.08480.00450.04190.2202-0.09110.1866-0.1016-0.1508-0.00350.2908-0.00570.05780.2485-0.07010.273319.101982.888165.311
30.4634-0.2546-0.03022.97680.99981.2077-0.0007-0.10620.08030.4906-0.00170.1711-0.027-0.07440.00670.3734-0.0170.09250.2741-0.07670.273218.688284.064172.9221
41.4425-0.3184-0.97652.30992.31234.3385-0.0746-0.1325-0.17410.5660.212-0.17290.59290.5441-0.13610.37930.0588-0.02620.2456-0.07220.32732.92562.464260.3998
50.01160.008-0.02450.01230.0050.0334-0.30830.0172-0.7504-0.611-0.1579-0.8191-0.2208-0.11410.32781.3758-0.05270.32850.4929-0.04490.896617.239856.381787.7257
62.6015-0.928-0.50153.83350.83592.16440.06250.11170.5543-0.3058-0.18460.2317-0.7428-0.21460.11980.38040.0634-0.04360.2356-0.03440.349216.171870.05519.2617
71.7306-0.2288-0.16372.86350.01381.93070.05660.27470.0473-0.3012-0.0339-0.1951-0.31190.249-0.02350.2493-0.03940.02980.3323-0.0310.213429.164456.083114.317
81.55240.51680.1473.20190.962.09650.0287-0.12460.11450.0118-0.0133-0.0487-0.160.0123-0.00010.19340.00280.02510.2587-0.07650.238724.517853.403526.1181
94.0159-0.34071.18970.2457-0.33330.8469-0.3573-0.405-0.19730.2645-0.17820.4541-0.0314-0.7690.19460.1514-0.0620.15850.631-0.35510.50095.448651.088228.0721
100.6982-0.32840.38540.43650.69971.3019-0.083-0.1890.1080.0421-0.17960.276-0.2751-0.50660.1590.24790.02980.0210.3515-0.15450.35811.71161.777735.9036
111.5972-0.47390.69041.110.09731.6576-0.1376-0.2080.16770.2779-0.230.2503-0.051-1.0880.26150.3020.05560.05840.5757-0.19970.38356.565261.13644.4904
120.7058-0.7249-0.46121.99461.91981.9214-0.0054-0.1204-0.00310.3426-0.08280.29630.3876-0.11830.10430.2911-0.05740.0450.2894-0.0670.26515.519442.285934.0768
130.4499-0.2030.052.38782.03414.71930.0252-0.1825-0.150.5078-0.0197-0.05740.35590.2785-0.02970.2405-0.0282-0.03930.2754-0.01740.229725.807138.44631.3267
145.57995.0459-1.51074.97981.28561.9999-0.0754-0.5030.0735-0.4028-0.18750.2646-0.1216-0.60480.26950.92680.5284-0.14840.7583-0.39581.000423.099521.657318.1514
150.8195-0.03190.05861.5550.25841.034-0.03720.10060.0855-0.14880.0901-0.0492-0.12550.1532-0.04820.182-0.04280.02980.2455-0.02530.21520.517833.1255-12.0684
160.5952-0.16490.03651.09470.72131.08740.0049-0.030.050.0879-0.05120.08930.0415-0.14550.03580.1211-0.03240.02860.1824-0.02010.18437.85726.3362.9342
173.181-1.2088-0.35823.05430.53031.97910.02880.62510.0779-0.57470.0308-0.0522-0.13850.1098-0.05910.3688-0.07560.04280.4668-0.01960.155917.36439.9907-44.1631
181.0974-0.0025-0.19371.09320.30271.5003-0.06640.2931-0.1355-0.24440.1448-0.1630.17630.103-0.05920.2792-0.00790.03220.3279-0.12540.221819.7457-2.0808-33.9486
191.17540.2044-0.10650.79380.19031.3924-0.06420.2164-0.1634-0.04740.06270.01480.2214-0.0660.03370.2507-0.0149-0.00160.2419-0.07380.21279.2248-3.5944-21.6205
203.2635-1.0024-3.12411.81931.31954.82090.02730.0656-0.42810.04140.1528-0.38530.47020.3824-0.12930.31430.1139-0.00110.303-0.22690.458930.4399-16.0908-24.5724
211.3383-0.1969-0.30731.30540.77762.3137-0.1063-0.3129-0.08110.73120.1135-0.3090.28350.4977-0.09140.7413-0.11810.03120.2747-0.16590.301127.144494.019881.0849
220.20280.0271-0.06741.45281.57561.9677-0.07730.0416-0.04450.29210.5241-0.46590.38990.764-0.41910.23730.06330.02430.4753-0.21340.432243.055327.99143.6479
231.49821.3075-0.24222.73870.51121.3555-0.30110.3201-0.5068-0.40270.0827-0.26150.9753-0.09350.03480.6668-0.09920.09890.2624-0.12830.31236.557555.198369.9406
242.25160.4008-0.44552.3484-0.65342.3896-0.1713-0.5281-0.30250.25660.0442-0.68540.49990.97710.12220.45030.1802-0.0520.530.03280.449715.474159.2142105.16
251.42410.2504-1.28331.31040.00553.047-0.24490.0268-0.39180.12030.12480.00290.55-0.1242-0.01920.437-0.00520.03270.14130.02350.3291-1.830655.235893.8453
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 'B' and (resseq 506:506)
15X-RAY DIFFRACTION15chain 'C' and (resseq 1:197)
16X-RAY DIFFRACTION16chain 'C' and (resseq 198:440)
17X-RAY DIFFRACTION17chain 'D' and (resseq 1:88)
18X-RAY DIFFRACTION18chain 'D' and (resseq 89:295)
19X-RAY DIFFRACTION19chain 'D' and (resseq 296:401)
20X-RAY DIFFRACTION20chain 'D' and (resseq 402:441)
21X-RAY DIFFRACTION21chain 'E' and (resseq 6:46)
22X-RAY DIFFRACTION22chain 'E' and (resseq 47:144)
23X-RAY DIFFRACTION23chain 'F' and (resseq 1:66)
24X-RAY DIFFRACTION24chain 'F' and (resseq 67:198)
25X-RAY DIFFRACTION25chain 'F' and (resseq 199:384)

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