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- PDB-6hx8: Tubulin-STX3451 complex -

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Basic information

Entry
Database: PDB / ID: 6hx8
TitleTubulin-STX3451 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 / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / spindle microtubule / structural constituent of cytoskeleton ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / microtubule-based process / cytoplasmic microtubule / cellular response to interleukin-4 / tubulin binding / spindle microtubule / structural constituent of cytoskeleton / protein modification process / microtubule cytoskeleton organization / neuron migration / neuron projection development / mitotic cell cycle / double-stranded RNA binding / growth cone / microtubule cytoskeleton / 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. / 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 / 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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-GXN / 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: 2.402 Å
AuthorsDohle, W. / Prota, A.E. / Menchon, G. / Hamel, E. / Steinmetz, M.O. / Potter, B.V.L.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Swiss National Science Foundation31003A_166608 Switzerland
CitationJournal: ACS Omega / Year: 2019
Title: Tetrahydroisoquinoline Sulfamates as Potent Microtubule Disruptors: Synthesis, Antiproliferative and Antitubulin Activity of Dichlorobenzyl-Based Derivatives, and a Tubulin Cocrystal Structure.
Authors: Dohle, W. / Prota, A.E. / Menchon, G. / Hamel, E. / Steinmetz, M.O. / Potter, B.V.L.
History
DepositionOct 16, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Feb 27, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 24, 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)265,44121
Polymers261,6316
Non-polymers3,81015
Water5,459303
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21790 Å2
ΔGint-134 kcal/mol
Surface area82770 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.670, 159.920, 181.010
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) / 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 (domestic 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 , 8 types, 318 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-GXN / [2-[(3-bromanyl-4,5-dimethoxy-phenyl)methyl]-7-methoxy-3,4-dihydro-1~{H}-isoquinolin-6-yl] sulfamate


Mass: 487.365 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H23BrN2O6S
#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-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.: 303 / 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: 2.92 Å3/Da / Density % sol: 57.92 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 10% PEG 4K, 16% 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 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Jun 9, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→48.4 Å / Num. obs: 115121 / % possible obs: 100 % / Redundancy: 6.8 % / CC1/2: 0.999 / Rmerge(I) obs: 0.093 / Rpim(I) all: 0.042 / Rrim(I) all: 0.101 / Net I/σ(I): 16.7
Reflection shellResolution: 2.4→2.46 Å / Redundancy: 6.6 % / Rmerge(I) obs: 2.66 / Num. unique obs: 8408 / CC1/2: 0.294 / Rpim(I) all: 1.158 / Rrim(I) all: 2.889 / % possible all: 100

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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: 5OSK

5osk


Resolution: 2.402→48.345 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.88
RfactorNum. reflection% reflection
Rfree0.24 5742 4.99 %
Rwork0.1954 --
obs0.1977 115121 96.06 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.402→48.345 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17082 0 228 303 17613
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00217831
X-RAY DIFFRACTIONf_angle_d0.53524199
X-RAY DIFFRACTIONf_dihedral_angle_d10.64110688
X-RAY DIFFRACTIONf_chiral_restr0.0412627
X-RAY DIFFRACTIONf_plane_restr0.0033131
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4024-2.42970.4229430.3356613X-RAY DIFFRACTION17
2.4297-2.45830.36131290.34432491X-RAY DIFFRACTION66
2.4583-2.48820.39222000.34473669X-RAY DIFFRACTION99
2.4882-2.51970.38041680.32883794X-RAY DIFFRACTION100
2.5197-2.55290.35011890.31943757X-RAY DIFFRACTION100
2.5529-2.58780.36062030.30943772X-RAY DIFFRACTION100
2.5878-2.62480.33871810.30723771X-RAY DIFFRACTION100
2.6248-2.6640.32492120.30363717X-RAY DIFFRACTION100
2.664-2.70560.34192050.29733765X-RAY DIFFRACTION100
2.7056-2.750.3342020.2873754X-RAY DIFFRACTION100
2.75-2.79740.35321820.27173752X-RAY DIFFRACTION100
2.7974-2.84820.31872360.25853752X-RAY DIFFRACTION100
2.8482-2.9030.28051980.25663769X-RAY DIFFRACTION100
2.903-2.96230.30681870.25563790X-RAY DIFFRACTION100
2.9623-3.02670.30571870.25613775X-RAY DIFFRACTION100
3.0267-3.09710.31751920.25213771X-RAY DIFFRACTION100
3.0971-3.17450.29692070.2313786X-RAY DIFFRACTION100
3.1745-3.26030.27812200.23453740X-RAY DIFFRACTION100
3.2603-3.35620.26822100.22583791X-RAY DIFFRACTION100
3.3562-3.46450.29631700.2113790X-RAY DIFFRACTION100
3.4645-3.58830.2442040.2073800X-RAY DIFFRACTION100
3.5883-3.73190.24261800.19353823X-RAY DIFFRACTION100
3.7319-3.90170.22852070.17573818X-RAY DIFFRACTION100
3.9017-4.10730.19871790.16433816X-RAY DIFFRACTION100
4.1073-4.36450.20561890.15643817X-RAY DIFFRACTION100
4.3645-4.70120.19392090.13823829X-RAY DIFFRACTION100
4.7012-5.17380.15942000.14543868X-RAY DIFFRACTION100
5.1738-5.92140.23062320.17373829X-RAY DIFFRACTION100
5.9214-7.45590.24752170.19113885X-RAY DIFFRACTION100
7.4559-48.35520.18852040.16354075X-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)
12.99320.0368-0.81066.43740.6861.70610.08960.0980.5274-1.22020.4787-0.4017-1.38330.2327-0.5361.1103-0.24420.22920.7216-0.16830.666828.982697.98852.8717
22.6182-0.9720.65469.03691.42793.21080.13130.33010.2608-1.638-0.0406-0.0902-1.3060.3593-0.15871.1252-0.17370.22440.8921-0.18040.635429.38889.009643.3824
31.63761.1376-0.45954.53881.14853.7931-0.12760.13570.1409-0.35520.5886-0.7867-0.38651.0408-0.40150.5137-0.07290.10120.897-0.36320.803935.579979.326254.9093
42.3521-1.2035-0.38364.59340.43424.06020.44570.6069-0.7050.0283-0.00810.6004-0.0084-0.3672-0.47870.60750.10550.00330.6418-0.16980.695113.769180.46360.765
51.5653-0.56250.92555.24061.4645.14070.1034-0.25060.23350.38830.09740.1498-0.51740.2564-0.25490.57840.04870.12860.573-0.18020.623419.368187.90568.8796
61.2901-0.06930.68854.36711.60622.8093-0.0894-0.48130.43851.69010.1410.3874-0.0557-0.3146-0.07681.03920.06870.21990.6775-0.17080.674417.749788.303780.9936
72.89620.63941.12814.71091.26836.06870.0484-0.25250.03070.77640.09140.2075-0.220.1642-0.16530.82350.0960.17710.6847-0.20990.715318.952790.292674.1465
81.5629-0.1291-0.26532.33971.00741.5785-0.0292-0.0961-0.30510.40060.7019-0.25620.72151.1605-0.45550.62270.1829-0.02680.7347-0.25710.670727.870561.978457.6062
92.7322-1.7144-3.31455.86584.63435.471-0.2390.0353-0.50531.40910.756-0.67571.36972.7612-0.11480.75820.2986-0.13490.98-0.21670.84533.248564.225868.5185
104.5468-1.9067-0.90677.20442.27335.56640.26710.290.7466-0.7951-0.18950.0298-1.2347-0.3875-0.1230.6660.03960.03620.49280.0150.610515.930871.193419.2324
112.0235-0.853-0.59793.47951.28354.22950.06640.1304-0.0389-0.2152-0.058-0.019-0.1585-0.0649-0.0580.30380.03310.02260.454-0.11940.457620.234255.394923.551
124.27850.97651.45960.6995-1.25776.84810.1389-0.0690.46110.3306-0.0882-0.2834-0.4990.2746-0.07380.40480.0610.09960.5008-0.19820.546521.689163.658840.1818
133.5636-3.70791.09049.40460.32672.7172-0.136-0.0106-0.4553-0.05990.08811.3726-0.134-1.06690.04010.625-0.00450.10110.9883-0.22740.83691.019157.405438.6797
149.2404-4.3202-2.4823.19192.64622.5156-0.7917-0.72790.39031.5090.48470.3554-0.6109-0.76390.2790.9210.23890.16970.9491-0.21380.7834.29565.984746.9547
150.6813-0.075-0.28842.30792.04093.4093-0.0201-0.1270.00610.49280.02660.0350.51810.0037-0.05080.4034-0.00330.02510.5113-0.03310.486317.832946.803135.5699
163.6845-1.5145-0.16134.1850.50113.7124-0.11270.18290.4841-0.34560.19560.1441-0.5866-0.192-0.07980.5747-0.077-0.00370.56390.03480.560914.170342.8312-12.9796
175.3327-4.2603-0.7673.27660.59275.13560.28480.91790.059-1.4523-0.1239-0.0154-0.6123-0.2657-0.22880.6451-0.14470.02340.66780.03610.475818.395731.5889-22.4753
180.9415-0.41010.06265.16461.41393.0584-0.11620.12530.1075-0.25430.1262-0.1269-0.01430.3238-0.01160.3535-0.07130.02450.5165-0.0550.453525.256926.5103-7.5749
193.8506-0.97161.25212.6907-0.31054.39510.0378-0.30260.2923-0.08-0.07620.3058-0.1868-0.63190.04810.2889-0.0150.05590.4183-0.02740.41436.928429.5874-1.1149
201.697-0.7239-0.13391.98361.04172.1345-0.1341-0.16830.11920.1565-0.12060.44390.0727-0.41970.22610.3863-0.10440.04390.5157-0.08510.56512.436928.17646.3883
213.4193-2.0545-3.95984.37914.87679.1054-0.1672-0.2634-0.1180.43950.2945-0.27240.69820.8022-0.18110.44660.0767-0.04670.4824-0.06360.524825.711411.21532.4969
225.8441-0.92760.37443.36060.19262.4504-0.2771.05250.6094-0.73810.64030.45280.3911-0.894-0.27540.9845-0.4057-0.09971.2630.10990.64815.66511.2891-41.8636
238.8099-2.304-3.45957.30434.02192.9093-0.49452.21550.53-2.28640.7546-0.05980.6202-1.3327-0.20191.7406-0.5510.16721.8719-0.29820.707422.55831.2888-50.492
241.1501-0.34220.59111.41680.24530.5253-0.85491.8324-0.2402-1.5360.6651-1.45880.76170.4225-0.84251.7345-0.44880.60371.5671-0.59460.89534.3522-1.2722-43.745
251.9533-1.1656-0.01660.6249-0.61924.1349-0.35210.335-0.6542-0.67950.27-0.36850.9065-0.16110.00161.1026-0.23250.17520.9331-0.37650.737924.602-6.3878-32.8104
262.53220.8923.03760.31331.02413.6527-0.87461.6189-0.6523-2.04810.96820.45960.828-2.6180.16211.6552-0.76420.00651.6301-0.26150.877.4802-8.5763-38.8608
274.7586-0.81791.78724.3879-1.06516.5214-0.33110.5784-0.0960.02410.52180.4186-0.0784-0.1285-0.13480.5446-0.14010.08460.7043-0.16330.522618.32866.4942-22.9251
284.6311-1.48810.25685.1595-0.44064.0943-0.35461.1665-0.8285-0.1240.65730.74051.1835-1.3286-0.330.9305-0.38950.03531.0842-0.10910.7045.2324-7.0203-23.5446
296.9695-1.2859-0.54216.1151-1.94588.0762-0.39140.0779-0.0140.72040.71740.975-0.329-2.2442-0.30750.7339-0.13640.04951.06250.03640.78361.66754.2585-18.6612
301.60180.05-0.90892.57920.20964.0992-0.42040.6434-0.3831-0.38570.59110.25260.7687-0.5319-0.03530.8325-0.31770.09590.7723-0.17590.630412.2543-6.3509-21.8906
313.5907-1.9832-1.38484.54271.74431.754-0.50370.501-1.2026-0.00640.1937-0.08141.25050.27460.17721.3554-0.01880.22340.8491-0.3521.088431.027-18.5221-24.1184
323.52460.3129-1.68274.43761.07132.70760.1287-0.2112-0.1230.87040.10570.3351-0.51551.545-0.35121.2591-0.0847-0.16991.0831-0.16790.850828.692193.854482.3799
330.7867-1.2523-1.69680.40410.1390.5408-0.1644-0.12780.08160.29020.7833-0.64730.541.1654-0.59960.64190.13480.00360.9376-0.29470.919743.531528.21914.0394
345.61441.8749-3.31455.939-0.01535.2096-0.81231.0774-0.9740.03760.4931-0.19962.2143-0.99590.31871.3631-0.20180.23160.9511-0.21260.80346.418555.07469.5955
358.37091.44831.90858.9354-5.6124.5476-0.4394-1.16270.45961.6527-0.24290.0754-0.43740.58070.68891.13940.1520.031.24750.04330.764311.268665.788497.3139
364.1922-1.19163.61766.4728-0.74383.161-0.63140.00591.31750.7163-0.1645-1.1733-0.98550.91010.87941.40440.3168-0.35162.38030.16541.639922.266161.8538109.0261
372.41080.05762.74742.3054-1.20283.3242-0.1245-0.6283-0.44720.3315-0.583-0.41181.74012.05960.70881.48440.49540.26951.77260.4481.24487.620651.5521105.9751
383.6731.2124-2.91752.5735-1.2722.708-0.93090.0511-1.13470.45230.4211-0.18941.3632-0.11640.50471.940.00480.35480.89990.12171.2922-3.737847.624199.2581
394.0077-0.4624-3.71431.271-0.23835.8317-0.49280.0419-0.4860.14710.38770.08031.4757-0.60690.02511.2231-0.07680.14110.75650.03130.8228-1.192360.08387.275
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 79 )
2X-RAY DIFFRACTION2chain 'A' and (resid 80 through 102 )
3X-RAY DIFFRACTION3chain 'A' and (resid 103 through 197 )
4X-RAY DIFFRACTION4chain 'A' and (resid 198 through 223 )
5X-RAY DIFFRACTION5chain 'A' and (resid 224 through 306 )
6X-RAY DIFFRACTION6chain 'A' and (resid 307 through 338 )
7X-RAY DIFFRACTION7chain 'A' and (resid 339 through 381 )
8X-RAY DIFFRACTION8chain 'A' and (resid 382 through 414 )
9X-RAY DIFFRACTION9chain 'A' and (resid 415 through 437 )
10X-RAY DIFFRACTION10chain 'B' and (resid 1 through 88 )
11X-RAY DIFFRACTION11chain 'B' and (resid 89 through 243 )
12X-RAY DIFFRACTION12chain 'B' and (resid 244 through 268 )
13X-RAY DIFFRACTION13chain 'B' and (resid 269 through 311 )
14X-RAY DIFFRACTION14chain 'B' and (resid 312 through 338 )
15X-RAY DIFFRACTION15chain 'B' and (resid 339 through 437 )
16X-RAY DIFFRACTION16chain 'C' and (resid 1 through 72 )
17X-RAY DIFFRACTION17chain 'C' and (resid 73 through 102 )
18X-RAY DIFFRACTION18chain 'C' and (resid 103 through 199 )
19X-RAY DIFFRACTION19chain 'C' and (resid 200 through 277 )
20X-RAY DIFFRACTION20chain 'C' and (resid 278 through 401 )
21X-RAY DIFFRACTION21chain 'C' and (resid 402 through 440 )
22X-RAY DIFFRACTION22chain 'D' and (resid 2 through 64 )
23X-RAY DIFFRACTION23chain 'D' and (resid 65 through 88 )
24X-RAY DIFFRACTION24chain 'D' and (resid 89 through 128 )
25X-RAY DIFFRACTION25chain 'D' and (resid 129 through 215 )
26X-RAY DIFFRACTION26chain 'D' and (resid 216 through 238 )
27X-RAY DIFFRACTION27chain 'D' and (resid 239 through 266 )
28X-RAY DIFFRACTION28chain 'D' and (resid 267 through 311 )
29X-RAY DIFFRACTION29chain 'D' and (resid 312 through 337 )
30X-RAY DIFFRACTION30chain 'D' and (resid 338 through 399 )
31X-RAY DIFFRACTION31chain 'D' and (resid 400 through 441 )
32X-RAY DIFFRACTION32chain 'E' and (resid 6 through 46 )
33X-RAY DIFFRACTION33chain 'E' and (resid 47 through 143 )
34X-RAY DIFFRACTION34chain 'F' and (resid 1 through 66 )
35X-RAY DIFFRACTION35chain 'F' and (resid 67 through 96 )
36X-RAY DIFFRACTION36chain 'F' and (resid 97 through 139 )
37X-RAY DIFFRACTION37chain 'F' and (resid 140 through 207 )
38X-RAY DIFFRACTION38chain 'F' and (resid 208 through 283 )
39X-RAY DIFFRACTION39chain 'F' and (resid 284 through 380 )

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