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- PDB-6qqn: Tubulin-TH588 complex -

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Basic information

Entry
Database: PDB / ID: 6qqn
TitleTubulin-TH588 complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine Ligase
KeywordsCELL CYCLE / TUBULIN FOLD / CYTOSKELETON / MICROTUBULE
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
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 ...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. / 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 / 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-2GE / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.301 Å
AuthorsPatterson, J.C. / Joughin, B.A. / Prota, A.E. / Muehlethaler, T. / Jonas, O.H. / Whitman, M.A. / Varmeh, S. / Chen, S. / Balk, S.P. / Steinmetz, M.O. ...Patterson, J.C. / Joughin, B.A. / Prota, A.E. / Muehlethaler, T. / Jonas, O.H. / Whitman, M.A. / Varmeh, S. / Chen, S. / Balk, S.P. / Steinmetz, M.O. / Lauffenburger, D.A. / Yaffe, M.B.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM104047 United States
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)R01-ES015339 United States
CitationJournal: Cell Syst / Year: 2019
Title: VISAGE Reveals a Targetable Mitotic Spindle Vulnerability in Cancer Cells.
Authors: Patterson, J.C. / Joughin, B.A. / Prota, A.E. / Muhlethaler, T. / Jonas, O.H. / Whitman, M.A. / Varmeh, S. / Chen, S. / Balk, S.P. / Steinmetz, M.O. / Lauffenburger, D.A. / Yaffe, M.B.
History
DepositionFeb 18, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 24, 2019Provider: repository / Type: Initial release
Revision 1.1Aug 7, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Mar 30, 2022Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Refinement description
Category: database_2 / pdbx_audit_support ...database_2 / pdbx_audit_support / pdbx_struct_conn_angle / refine / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_audit_support.funding_organization / _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 / _refine.pdbx_diffrn_id / _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.ptnr1_symmetry / _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_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry
Revision 1.3Jan 24, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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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)264,90423
Polymers261,6316
Non-polymers3,27217
Water4,666259
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23020 Å2
ΔGint-147 kcal/mol
Surface area79700 Å2
MethodPISA
Unit cell
Length a, b, c (Å)103.832, 156.186, 179.432
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) / 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 , 9 types, 276 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-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6O2
#9: 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
#10: 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
#11: Chemical ChemComp-2GE / N~4~-cyclopropyl-6-(2,3-dichlorophenyl)pyrimidine-2,4-diamine


Mass: 295.167 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C13H12Cl2N4
#12: Chemical ChemComp-ACP / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE


Mass: 505.208 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Formula: C11H18N5O12P3 / Comment: AMP-PCP, energy-carrying molecule analogue*YM
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 259 / 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: 2.78 Å3/Da / Density % sol: 55.76 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 1% PEG 4K, 8% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole pH 6.7

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00002 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Dec 5, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00002 Å / Relative weight: 1
ReflectionResolution: 2.3→47.5 Å / Num. obs: 249775 / % possible obs: 99.9 % / Redundancy: 13.6 % / CC1/2: 0.998 / Rmerge(I) obs: 0.197 / Rpim(I) all: 0.057 / Rrim(I) all: 0.205 / Net I/σ(I): 11.3
Reflection shellResolution: 2.3→2.36 Å / Redundancy: 13.7 % / Rmerge(I) obs: 4.103 / Num. unique obs: 9434 / CC1/2: 0.22 / Rpim(I) all: 1.218 / Rrim(I) all: 4.261 / % possible all: 99.6

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Processing

Software
NameVersionClassification
PHENIX(1.13_2998: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 5lxt

5lxt


Resolution: 2.301→47.484 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.18 / Phase error: 28.37 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2442 12447 4.98 %
Rwork0.196 --
obs0.1983 249777 99.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.301→47.484 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17061 0 195 259 17515
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00217664
X-RAY DIFFRACTIONf_angle_d0.51923945
X-RAY DIFFRACTIONf_dihedral_angle_d10.64410552
X-RAY DIFFRACTIONf_chiral_restr0.042610
X-RAY DIFFRACTIONf_plane_restr0.0033097
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3013-2.32750.38364040.38037729X-RAY DIFFRACTION99
2.3275-2.35480.37294190.37127957X-RAY DIFFRACTION100
2.3548-2.38360.41184180.35657915X-RAY DIFFRACTION100
2.3836-2.41370.33024200.33717900X-RAY DIFFRACTION100
2.4137-2.44550.38114160.32837903X-RAY DIFFRACTION100
2.4455-2.4790.3364140.32147956X-RAY DIFFRACTION100
2.479-2.51440.36214090.32657877X-RAY DIFFRACTION100
2.5144-2.55190.34144170.32167887X-RAY DIFFRACTION100
2.5519-2.59180.34764240.3057996X-RAY DIFFRACTION100
2.5918-2.63430.34164110.29567840X-RAY DIFFRACTION100
2.6343-2.67970.34314100.3067981X-RAY DIFFRACTION100
2.6797-2.72840.32754180.29787896X-RAY DIFFRACTION100
2.7284-2.78090.32094180.28387884X-RAY DIFFRACTION100
2.7809-2.83770.31144210.26447962X-RAY DIFFRACTION100
2.8377-2.89940.32374170.25367894X-RAY DIFFRACTION100
2.8994-2.96680.3034190.24617935X-RAY DIFFRACTION100
2.9668-3.0410.27924180.237881X-RAY DIFFRACTION100
3.041-3.12320.24914150.21727957X-RAY DIFFRACTION100
3.1232-3.21510.28494120.22957881X-RAY DIFFRACTION100
3.2151-3.31880.2784180.21227920X-RAY DIFFRACTION100
3.3188-3.43740.23024140.19677920X-RAY DIFFRACTION100
3.4374-3.5750.23384130.18647930X-RAY DIFFRACTION100
3.575-3.73760.24914090.17457901X-RAY DIFFRACTION100
3.7376-3.93460.23644170.16087917X-RAY DIFFRACTION100
3.9346-4.1810.17724140.15027932X-RAY DIFFRACTION100
4.181-4.50360.17944190.13637942X-RAY DIFFRACTION100
4.5036-4.95630.19054100.13487907X-RAY DIFFRACTION100
4.9563-5.67250.22354140.15957903X-RAY DIFFRACTION100
5.6725-7.14290.22864100.17567931X-RAY DIFFRACTION100
7.1429-47.4940.18764090.15287896X-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)
11.6934-0.3542-0.65993.51761.13533.0398-0.0130.0840.2635-0.68710.3462-0.3956-0.90340.4465-0.30950.698-0.1620.13650.5883-0.18260.589432.030388.546750.9995
21.61130.0347-0.66333.22671.26633.61220.0179-0.05380.140.23690.08360.1243-0.15670.0613-0.09740.49540.01380.02340.4572-0.10470.532420.395180.751265.112
32.75990.36520.93813.37511.18682.52440.0525-0.1644-0.0170.66310.01420.4209-0.12160.0678-0.06220.82760.04340.14310.6141-0.14160.601517.220288.718276.7271
41.0161-0.084602.56271.43772.6708-0.0073-0.0559-0.07360.5580.272-0.2230.55790.4214-0.28910.53160.1034-0.02890.507-0.12460.538728.253764.361463.5357
53.293-0.714-0.27753.61130.42012.68390.15490.10060.7792-0.3232-0.1310.1855-0.875-0.24620.02660.75370.06950.04830.5585-0.03150.792815.492371.872922.4109
61.9121-0.756-0.28313.81961.8182.44960.0840.39870.2032-0.761-0.0164-0.1735-0.67490.1521-0.05190.6441-0.02270.03820.6025-0.03020.519624.690258.294113.5197
70.6853-0.75710.2482.70041.40552.93170.0315-0.216-0.05080.0761-0.0847-0.0583-0.0358-0.11990.03860.37130.01760.05120.4979-0.12060.480521.316251.820827.0188
81.2399-0.229-0.09941.07960.32774.0387-0.0680.12870.06690.1026-0.06190.3629-0.1668-0.78740.12340.50130.07480.05410.6928-0.18330.66478.327158.282936.611
91.9656-0.68571.32061.1649-0.31052.253-0.4777-0.52360.17160.47110.32150.1833-0.4989-1.25290.14560.76330.13380.05580.8054-0.14450.64756.371862.305947.1026
100.39250.34620.08872.8541.99053.67280.0128-0.1746-0.13380.61570.01480.07480.56810.1503-0.04330.5052-0.0231-0.0280.4961-0.0370.488421.67538.928832.2647
111.7616-0.9964-0.44083.1871-0.32312.4845-0.0390.10410.4414-0.20610.07990.0953-0.51830.0615-0.03260.4781-0.1084-0.01710.55470.01490.553914.518342.0761-12.8469
121.632-0.303-0.20063.46240.57972.3212-0.06530.41210.0941-0.51880.1786-0.1589-0.23920.1193-0.09050.4323-0.10850.08870.5802-0.02140.474124.50430.3508-18.5295
130.5235-0.3806-0.03861.60090.02151.7758-0.10490.0093-0.151-0.02870.11020.0740.11880.03090.00520.3888-0.02090.03420.4862-0.04930.495417.211823.3471-5.4582
141.5248-0.99671.21491.68691.04063.51380.018-0.25380.2157-0.0056-0.13210.1994-0.0185-0.64510.06350.3679-0.03840.04280.5274-0.0480.5144.430430.412.5113
153.6889-1.70531.41222.98380.32.256-0.1237-0.29460.08190.4739-0.10240.4725-0.1316-0.45520.20040.4783-0.05750.05080.5368-0.08790.6151-0.572135.045612.3547
162.6457-0.35341.99911.404-0.16963.5662-0.0631-0.19320.1332-0.17830.05760.27220.07-0.2998-0.03460.4799-0.05230.06850.5295-0.08350.57862.559233.7116.2458
171.1767-0.0589-0.14131.43570.86882.1412-0.13570.0045-0.10990.3260.1526-0.1380.4980.2247-0.03610.4704-0.0178-0.00970.4402-0.04070.495720.4112.8442.6073
184.3063-1.24010.13272.8750.1323.0952-0.25130.47130.4649-0.44540.32240.0723-0.1203-0.118-0.06670.71-0.18680.0250.8759-0.0170.514515.749612.1074-41.7528
191.6676-0.4552-0.31432.5109-1.23371.7370.03870.873-0.0774-0.7650.1365-0.24270.38540.4251-0.15710.9515-0.12670.19161.2127-0.29380.64929.61170.3354-46.6947
202.4177-0.0953-0.21390.9031-1.21782.4583-0.12450.3122-0.3832-0.40730.1705-0.2290.6233-0.0242-0.0570.7392-0.08340.07920.6709-0.23390.539821.0638-5.6835-34.4839
211.94670.67620.97091.8585-0.16384.0351-0.07610.60230.0541-0.22670.13340.04950.1073-0.1097-0.04860.5088-0.08860.08920.6931-0.14990.529818.33896.0368-23.1844
222.8839-0.33630.59772.46040.91232.6346-0.17040.5097-0.1876-0.05490.03360.25730.3359-0.49420.13520.6446-0.16150.03460.6911-0.07280.51394.3642-0.2464-20.604
231.79990.3267-1.1740.4574-0.53421.7429-0.31960.5812-0.9213-0.2670.0027-0.10920.75280.09580.32680.9733-0.09840.11880.7081-0.36260.859324.7292-17.2574-29.7763
243.4951-0.1423-1.74871.90850.12034.5206-0.317-0.06330.03960.57580.3289-0.28051.36730.67230.00871.03460.09790.02690.7463-0.17250.82827.5535-14.1854-17.6236
254.6163-1.71812.23066.0551-0.3273.4587-0.6711-0.10570.34650.93980.4595-0.9412-0.54890.42160.19071.1632-0.06570.10680.7961-0.24730.739224.575496.949282.6178
263.86380.5823-4.42621.35130.33657.26140.02370.1023-0.00680.85830.579-0.7745-0.02450.3657-0.50861.46050.1775-0.13751.0646-0.16591.102634.421478.462180.3511
270.5412-0.3166-0.53570.47390.64291.2771-0.1941-0.0673-0.02140.4130.6003-0.33280.64010.9149-0.56120.60930.06180.04040.8675-0.20150.791643.030328.35444.9534
283.2435-0.0545-2.68981.4439-0.18163.8482-0.41490.0822-0.57940.0130.2314-0.09981.07580.14670.12540.9283-0.0090.10280.5352-0.0220.71737.655156.923977.927
292.86460.0271-0.95721.4946-0.27873.2772-0.2998-0.7957-0.78880.4116-0.1033-0.59320.87951.04750.4061.26570.19960.03911.12090.28641.08258.779352.115103.683
303.0516-0.0391-3.00761.2379-0.51934.6689-0.40820.1423-0.48810.23270.26480.09290.9485-0.3310.09251.02410.04010.1080.60740.02330.7551-3.755256.409890.7022
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 160 )
2X-RAY DIFFRACTION2chain 'A' and (resid 161 through 311 )
3X-RAY DIFFRACTION3chain 'A' and (resid 312 through 372 )
4X-RAY DIFFRACTION4chain 'A' and (resid 373 through 437 )
5X-RAY DIFFRACTION5chain 'B' and (resid 1 through 64 )
6X-RAY DIFFRACTION6chain 'B' and (resid 65 through 128 )
7X-RAY DIFFRACTION7chain 'B' and (resid 129 through 214 )
8X-RAY DIFFRACTION8chain 'B' and (resid 215 through 324 )
9X-RAY DIFFRACTION9chain 'B' and (resid 325 through 373 )
10X-RAY DIFFRACTION10chain 'B' and (resid 374 through 438 )
11X-RAY DIFFRACTION11chain 'C' and (resid 1 through 72 )
12X-RAY DIFFRACTION12chain 'C' and (resid 73 through 128 )
13X-RAY DIFFRACTION13chain 'C' and (resid 129 through 223 )
14X-RAY DIFFRACTION14chain 'C' and (resid 224 through 311 )
15X-RAY DIFFRACTION15chain 'C' and (resid 312 through 338 )
16X-RAY DIFFRACTION16chain 'C' and (resid 339 through 372 )
17X-RAY DIFFRACTION17chain 'C' and (resid 373 through 440 )
18X-RAY DIFFRACTION18chain 'D' and (resid 1 through 64 )
19X-RAY DIFFRACTION19chain 'D' and (resid 65 through 127 )
20X-RAY DIFFRACTION20chain 'D' and (resid 128 through 238 )
21X-RAY DIFFRACTION21chain 'D' and (resid 239 through 268 )
22X-RAY DIFFRACTION22chain 'D' and (resid 269 through 372 )
23X-RAY DIFFRACTION23chain 'D' and (resid 373 through 414 )
24X-RAY DIFFRACTION24chain 'D' and (resid 415 through 441 )
25X-RAY DIFFRACTION25chain 'E' and (resid 6 through 23 )
26X-RAY DIFFRACTION26chain 'E' and (resid 24 through 46 )
27X-RAY DIFFRACTION27chain 'E' and (resid 47 through 141 )
28X-RAY DIFFRACTION28chain 'F' and (resid 1 through 96 )
29X-RAY DIFFRACTION29chain 'F' and (resid 97 through 257 )
30X-RAY DIFFRACTION30chain 'F' and (resid 258 through 380 )

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