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- PDB-5iyz: Tubulin-MMAE complex -

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Basic information

Entry
Database: PDB / ID: 5iyz
TitleTubulin-MMAE complex
Components
  • Stathmin-4
  • TUBULIN-TYROSINE LIGASE
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
KeywordsCELL CYCLE / CYTOSKELETON / TUBULIN FOLD / MICROTUBULE
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 / tubulin binding / cellular response to interleukin-4 / 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 / tubulin binding / cellular response to interleukin-4 / 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 / cytosol / cytoplasm
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / 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 / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Helix hairpin bin / 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; / 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 / Dna Ligase; domain 1 / 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
N-methyl-L-valyl-N-[(3R,4S,5S)-1-{(2S)-2-[(1R,2R)-3-{[(1S,2R)-1-hydroxy-1-phenylpropan-2-yl]amino}-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1-yl}-3-methoxy-5-methyl-1-oxoheptan-4-yl]-N-methyl-L-valinamide / Chem-4Q5 / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 1.8 Å
AuthorsWaight, A.B. / Bargsten, K. / Doronina, S. / Steinmetz, M.O. / Sussman, D. / Prota, A.E.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation310030B_138659 Switzerland
CitationJournal: Plos One / Year: 2016
Title: Structural Basis of Microtubule Destabilization by Potent Auristatin Anti-Mitotics.
Authors: Waight, A.B. / Bargsten, K. / Doronina, S. / Steinmetz, M.O. / Sussman, D. / Prota, A.E.
History
DepositionMar 24, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Aug 17, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2016Group: Database references
Revision 1.2Oct 19, 2016Group: Database references
Revision 1.3Dec 21, 2016Group: Non-polymer description
Revision 1.4Jan 10, 2024Group: 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
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

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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)265,90221
Polymers261,6316
Non-polymers4,27115
Water24,3741353
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23140 Å2
ΔGint-155 kcal/mol
Surface area79750 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.510, 156.610, 182.420
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 (domestic cattle) / Tissue: 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 (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 , 8 types, 1368 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.: 2 / 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-4Q5 / N-methyl-L-valyl-N-[(3R,4S,5S)-1-{(2S)-2-[(1R,2R)-3-{[(1S,2R)-1-hydroxy-1-phenylpropan-2-yl]amino}-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1-yl}-3-methoxy-5-methyl-1-oxoheptan-4-yl]-N-methyl-L-valinamide


Type: peptide-like, Peptide-like / Class: Inhibitor / Mass: 717.979 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C39H67N5O7
References: N-methyl-L-valyl-N-[(3R,4S,5S)-1-{(2S)-2-[(1R,2R)-3-{[(1S,2R)-1-hydroxy-1-phenylpropan-2-yl]amino}-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1-yl}-3-methoxy-5-methyl-1-oxoheptan-4-yl]-N-methyl-L-valinamide
Comment: antineoplastic*YM
#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.: 1353 / 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: 2.85 Å3/Da / Density % sol: 56.89 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.7
Details: 5% PEG, 12% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M imidazole

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.98 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Sep 4, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.98 Å / Relative weight: 1
ReflectionResolution: 1.8→71.956 Å / Num. obs: 275542 / % possible obs: 99.9 % / Redundancy: 6.7 % / Rsym value: 0.056 / Net I/σ(I): 17.3
Reflection shellResolution: 1.8→1.85 Å / Redundancy: 6.2 % / Mean I/σ(I) obs: 0.84 / Rsym value: 2.45 / % possible all: 99.5

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 1.8→71.956 Å / SU ML: 0.23 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 22.56
RfactorNum. reflection% reflection
Rfree0.2015 13781 5 %
Rwork0.1669 --
obs0.1686 275542 99.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 1.8→71.956 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17294 0 272 1353 18919
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00918216
X-RAY DIFFRACTIONf_angle_d1.15724777
X-RAY DIFFRACTIONf_dihedral_angle_d15.5026835
X-RAY DIFFRACTIONf_chiral_restr0.0542728
X-RAY DIFFRACTIONf_plane_restr0.0053205
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.82040.39764520.35218581X-RAY DIFFRACTION99
1.8204-1.84190.33034540.32128633X-RAY DIFFRACTION100
1.8419-1.86430.32854570.30978694X-RAY DIFFRACTION100
1.8643-1.88790.33924530.29938606X-RAY DIFFRACTION100
1.8879-1.91280.30284540.28398631X-RAY DIFFRACTION100
1.9128-1.9390.31184580.28388691X-RAY DIFFRACTION100
1.939-1.96670.29964570.26888668X-RAY DIFFRACTION100
1.9667-1.9960.28484540.25188633X-RAY DIFFRACTION100
1.996-2.02720.2514590.23388711X-RAY DIFFRACTION100
2.0272-2.06050.2524540.22088634X-RAY DIFFRACTION100
2.0605-2.0960.23584600.21068712X-RAY DIFFRACTION100
2.096-2.13410.23744560.20158676X-RAY DIFFRACTION100
2.1341-2.17520.21834560.19468672X-RAY DIFFRACTION100
2.1752-2.21960.21884590.18548708X-RAY DIFFRACTION100
2.2196-2.26780.2294570.18488688X-RAY DIFFRACTION100
2.2678-2.32060.21784570.1848667X-RAY DIFFRACTION100
2.3206-2.37860.23514580.17898715X-RAY DIFFRACTION100
2.3786-2.44290.20854580.17568694X-RAY DIFFRACTION100
2.4429-2.51480.20644570.17188684X-RAY DIFFRACTION100
2.5148-2.5960.21184600.16848738X-RAY DIFFRACTION100
2.596-2.68880.20724600.17418734X-RAY DIFFRACTION100
2.6888-2.79640.21244600.17218741X-RAY DIFFRACTION100
2.7964-2.92370.21584610.17348745X-RAY DIFFRACTION100
2.9237-3.07790.21534620.16888780X-RAY DIFFRACTION100
3.0779-3.27070.21184610.16548751X-RAY DIFFRACTION100
3.2707-3.52320.18464610.1558768X-RAY DIFFRACTION100
3.5232-3.87780.17284660.14288837X-RAY DIFFRACTION100
3.8778-4.43880.15814660.12648848X-RAY DIFFRACTION100
4.4388-5.59210.16024710.13068931X-RAY DIFFRACTION100
5.5921-72.01330.19464830.16089190X-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)
12.1496-0.1685-0.41383.79420.31510.12340.09090.10510.5374-0.61590.2299-0.4011-1.06010.3594-0.25080.9663-0.19050.16930.4784-0.12320.464728.91298.616755.2612
23.9896-0.98980.61816.88810.59923.3544-0.25610.53390.3209-1.38860.50420.2803-0.74440.129-0.20090.849-0.23910.09740.452-0.06960.382727.117589.330243.8292
31.12270.240.34970.87150.55340.62740.02760.18820.1256-0.36420.5346-0.5712-0.72580.731-0.40590.5303-0.22020.17790.6185-0.27060.516737.234680.613550.7734
40.7551-0.3241-0.20262.42320.91722.53450.01030.0579-0.02320.03350.15060.014-0.16630.1685-0.14460.3293-0.01390.03710.3198-0.10030.287622.073178.704159.8242
51.30010.0682-0.02392.82940.94283.51790.0445-0.0430.09120.18620.07240.1236-0.2257-0.0069-0.11390.42060.01140.06290.3105-0.09520.334218.508484.521472.1736
60.61540.32070.32893.28731.70422.733-0.0308-0.07150.14420.46650.0670.1134-0.1558-0.0137-0.03830.42250.00860.07240.3642-0.07420.362318.925682.872873.8172
71.1378-0.0394-0.12892.84842.25743.17960.0262-0.0448-0.17330.57840.4816-0.40890.51450.9185-0.42150.37090.1095-0.0920.4481-0.15840.433932.426861.479761.1753
83.8282-0.93110.19164.40011.20423.0064-0.06670.0640.7413-0.40090.0389-0.0107-0.9371-0.04450.01840.52040.01050.00230.2695-0.01570.418815.854872.725422.6569
92.016-0.5063-0.10115.32730.33982.70660.09960.31620.1585-0.5878-0.06490.033-0.53590.2449-0.04080.3928-0.0460.02830.4332-0.04520.300324.363458.649613.2821
101.36280.2462-0.3442.74371.15112.33120.0215-0.13620.1271-0.0010.0696-0.1326-0.17160.2511-0.08860.18480.00410.01480.2909-0.07880.249823.896752.977526.0545
110.59540.07140.61161.14481.04862.9538-0.0295-0.09060.05680.0169-0.04150.1695-0.1545-0.20520.06870.21160.01840.02650.2919-0.09270.348411.879357.96832.9203
125.0296-2.7558-1.9715.38712.65981.69860.31670.28050.0122-0.6976-0.34410.5834-0.2318-1.20540.02950.49390.1278-0.0430.6796-0.15170.5606-4.22363.205135.1747
130.4164-0.27590.08681.84171.25162.3634-0.0806-0.11330.05060.3813-0.04620.18550.1518-0.25060.10280.2242-0.01170.02250.3241-0.05670.303913.442550.551838.8487
141.09-0.0151-0.0341.73650.32131.5295-0.04180.1640.1492-0.22140.0599-0.0554-0.1420.1269-0.01150.2482-0.05780.01270.3052-0.01910.259519.848232.437-12.1323
150.6695-0.60290.20920.93120.64312.05130.0247-0.005-0.0504-0.0145-0.11860.21160.0959-0.37310.05770.1812-0.05130.00890.274-0.03740.28513.42828.59960.2999
160.8157-0.3531-0.12981.58640.80731.5135-0.0674-0.01430.00130.14430.01910.08870.2136-0.04240.05040.2389-0.06310.01920.2544-0.01810.271310.674823.25685.5072
173.9731-0.74980.33124.24931.09023.2934-0.15130.64260.292-0.44350.10820.2055-0.154-0.27640.04130.4432-0.10210.00830.5979-0.00290.269615.204911.7584-41.5241
181.6324-0.273-0.66282.4425-0.05751.9078-0.13330.4724-0.1729-0.36390.1171-0.19210.41970.1638-0.02190.5789-0.0660.1070.5971-0.19630.40627.7536-2.5571-39.524
192.74210.51942.31621.8441.47532.605-0.0670.4219-0.4707-0.3546-0.03210.1970.8026-0.2862-0.10880.8424-0.28060.05070.6744-0.23830.48788.9916-11.3834-34.1772
201.0341-0.2107-0.15321.89250.53262.0315-0.17160.2333-0.0411-0.26360.15180.08380.0992-0.3006-0.0080.4356-0.09250.02740.4767-0.09040.351615.12642.8292-27.5048
210.0903-0.00230.22331.03370.91121.4031-0.06120.3574-0.4071-0.356-0.29050.56480.6678-0.610.20970.5496-0.20930.05760.646-0.21590.49722.39-6.2604-24.9467
221.972-0.3578-0.44331.68290.24852.0214-0.2330.3824-0.2666-0.04570.04050.22490.3317-0.32570.22130.4415-0.13890.03510.3899-0.1220.31668.3363-2.6553-20.8501
232.2988-0.6933-0.76982.23540.66421.5481-0.24650.1593-0.7167-0.06040.0203-0.27960.6640.2609-0.03060.75780.06030.11690.4286-0.19470.590229.5647-17.5001-24.0925
241.4367-0.09780.37232.0792-0.10581.4292-0.0268-0.03910.16070.94090.1828-0.0881-0.00390.3906-0.14790.9034-0.0665-0.02640.6006-0.1550.546627.482192.541182.1659
250.3794-0.3043-0.50290.28590.28730.5325-0.0509-0.0602-0.00260.31060.3565-0.31790.42940.5636-0.42130.39010.07240.01590.5857-0.18930.492842.323627.21693.9536
262.03151.0034-1.28453.2835-0.01762.574-0.46430.3773-0.4616-0.19730.13350.02081.1524-0.49040.22640.8539-0.09870.10240.4557-0.12780.49336.312754.249170.1955
274.96690.6784-0.61783.3472-4.3615.78770.027-0.49590.070.6928-0.1329-0.3206-0.34970.98840.08350.69310.0175-0.0280.60260.01790.471911.739265.120397.6285
281.5785-0.09421.35492.3948-0.09521.1984-0.376-1.11620.60950.62310.1763-1.15150.01080.85020.15070.94570.0701-0.34881.55340.11611.09823.037561.0042108.9752
294.3723-0.1575-0.50752.513-0.66410.56270.2431-0.4728-0.85050.8345-0.2452-1.20490.41971.4911-0.0141.0330.3201-0.12961.22620.45591.167820.861351.6449109.2954
304.49161.8704-1.69472.5697-0.29214.6218-0.234-0.4883-0.7550.30040.0258-0.17280.89730.84090.1791.05160.270.10280.72580.23770.7717.423349.2391108.4363
310.63060.6621-0.46071.2257-0.79461.0519-0.4122-0.1327-0.70650.14670.1416-0.15431.1025-0.0009-0.07411.16720.10570.24420.44920.14420.7819-2.415547.14599.2907
325.19872.5343-6.48712.4766-3.26158.94130.0542-0.06410.09920.42490.28830.116-0.36060.1019-0.39360.6180.09910.06370.32250.02050.40640.925266.016993.4622
332.18070.475-2.02360.7029-0.14894.4711-0.2598-0.1835-0.3770.19950.147-0.05260.56220.00430.06030.67360.08630.08320.34770.03670.43323.595258.857391.2686
343.9499-1.0463-0.60892.2196-2.39866.3198-0.38270.6025-0.2847-0.13160.23980.27090.759-0.91030.11380.6154-0.20440.03430.5659-0.06660.5217-6.841655.657480.2893
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 88 )
3X-RAY DIFFRACTION3chain 'A' and (resid 89 through 160 )
4X-RAY DIFFRACTION4chain 'A' and (resid 161 through 243 )
5X-RAY DIFFRACTION5chain 'A' and (resid 244 through 311 )
6X-RAY DIFFRACTION6chain 'A' and (resid 312 through 401 )
7X-RAY DIFFRACTION7chain 'A' and (resid 402 through 437 )
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 64 )
9X-RAY DIFFRACTION9chain 'B' and (resid 65 through 127 )
10X-RAY DIFFRACTION10chain 'B' and (resid 128 through 197 )
11X-RAY DIFFRACTION11chain 'B' and (resid 198 through 273 )
12X-RAY DIFFRACTION12chain 'B' and (resid 274 through 295 )
13X-RAY DIFFRACTION13chain 'B' and (resid 296 through 438 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 197 )
15X-RAY DIFFRACTION15chain 'C' and (resid 198 through 311 )
16X-RAY DIFFRACTION16chain 'C' and (resid 312 through 440 )
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 64 )
18X-RAY DIFFRACTION18chain 'D' and (resid 65 through 197 )
19X-RAY DIFFRACTION19chain 'D' and (resid 198 through 223 )
20X-RAY DIFFRACTION20chain 'D' and (resid 224 through 268 )
21X-RAY DIFFRACTION21chain 'D' and (resid 269 through 311 )
22X-RAY DIFFRACTION22chain 'D' and (resid 312 through 400 )
23X-RAY DIFFRACTION23chain 'D' and (resid 401 through 441 )
24X-RAY DIFFRACTION24chain 'E' and (resid 6 through 46 )
25X-RAY DIFFRACTION25chain 'E' and (resid 47 through 143 )
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 66 )
27X-RAY DIFFRACTION27chain 'F' and (resid 67 through 96 )
28X-RAY DIFFRACTION28chain 'F' and (resid 97 through 139 )
29X-RAY DIFFRACTION29chain 'F' and (resid 140 through 174 )
30X-RAY DIFFRACTION30chain 'F' and (resid 175 through 198 )
31X-RAY DIFFRACTION31chain 'F' and (resid 199 through 283 )
32X-RAY DIFFRACTION32chain 'F' and (resid 284 through 302 )
33X-RAY DIFFRACTION33chain 'F' and (resid 303 through 339 )
34X-RAY DIFFRACTION34chain 'F' and (resid 340 through 380 )

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