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- PDB-5mf4: Tubulin-Dictyostatin complex -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5mf4
TitleTubulin-Dictyostatin complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Uncharacterized protein
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 / 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
Chem-7LZ / 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: 2.3 Å
AuthorsTrigili, C. / Barasoain, I. / Sanchez-Murcia, P.A. / Bargsten, K. / Redondo-Horcajo, M. / Nogales, A. / Gardner, N.M. / Meyer, A. / Naylor, G.J. / Gomez-Rubio, E. ...Trigili, C. / Barasoain, I. / Sanchez-Murcia, P.A. / Bargsten, K. / Redondo-Horcajo, M. / Nogales, A. / Gardner, N.M. / Meyer, A. / Naylor, G.J. / Gomez-Rubio, E. / Gago, F. / Steinmetz, M.O. / Paterson, I. / Prota, A.E. / Diaz, J.F.
Funding support Spain, Switzerland, 3items
OrganizationGrant numberCountry
Spanish Ministry of Economy and CompetitivenessBIO2013-42984-R ; SAF2012-39760-C02-02 Spain
Comunidad Autonoma de MadridS2010/BMD-2457 BIPEDD2 Spain
Swiss National Science Foundation310030B_138659 ; 31003A_166608 Switzerland
CitationJournal: ACS Omega / Year: 2016
Title: Structural Determinants of the Dictyostatin Chemotype for Tubulin Binding Affinity and Antitumor Activity Against Taxane- and Epothilone-Resistant Cancer Cells.
Authors: Trigili, C. / Barasoain, I. / Sanchez-Murcia, P.A. / Bargsten, K. / Redondo-Horcajo, M. / Nogales, A. / Gardner, N.M. / Meyer, A. / Naylor, G.J. / Gomez-Rubio, E. / Gago, F. / Steinmetz, M.O. ...Authors: Trigili, C. / Barasoain, I. / Sanchez-Murcia, P.A. / Bargsten, K. / Redondo-Horcajo, M. / Nogales, A. / Gardner, N.M. / Meyer, A. / Naylor, G.J. / Gomez-Rubio, E. / Gago, F. / Steinmetz, M.O. / Paterson, I. / Prota, A.E. / Diaz, J.F.
History
DepositionNov 17, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 20, 2017Provider: repository / Type: Initial release
Revision 1.1Aug 29, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ..._citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 17, 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 / struct_conn_type
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.conn_type_id / _struct_conn.id / _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_conn_type.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: Uncharacterized protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,92724
Polymers261,6316
Non-polymers4,29618
Water2,576143
1


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23440 Å2
ΔGint-160 kcal/mol
Surface area79950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.010, 156.510, 179.060
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 Uncharacterized protein


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, 161 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.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#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-7LZ / (3~{Z},5~{E},7~{R},8~{S},10~{S},11~{Z},13~{S},14~{R},15~{S},17~{S},20~{R},21~{S},22~{S})-22-[(2~{S},3~{Z})-hexa-3,5-dien-2-yl]-7,13,15,17,21-pentamethyl-8,10,14,20-tetrakis(oxidanyl)-1-oxacyclodocosa-3,5,11-trien-2-one


Mass: 532.752 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C32H52O6
#11: 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
#12: 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
#13: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 143 / 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: 2.79 Å3/Da / Density % sol: 55.84 %
Crystal growTemperature: 293 K / Method: vapor diffusion / 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: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Mar 12, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.3→67.854 Å / Num. obs: 129857 / % possible obs: 99.8 % / Redundancy: 13.4 % / CC1/2: 1 / Rmerge(I) obs: 0.111 / Net I/σ(I): 18.7
Reflection shellResolution: 2.3→2.36 Å / Redundancy: 12.6 % / Rmerge(I) obs: 4.25 / Mean I/σ(I) obs: 0.7 / CC1/2: 0.262 / % possible all: 98.9

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.3→67.854 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.15
RfactorNum. reflection% reflection
Rfree0.2325 6488 5 %
Rwork0.1834 --
obs0.1859 129857 99.85 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.3→67.854 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17214 0 270 143 17627
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00817857
X-RAY DIFFRACTIONf_angle_d0.92824191
X-RAY DIFFRACTIONf_dihedral_angle_d16.5610655
X-RAY DIFFRACTIONf_chiral_restr0.0532653
X-RAY DIFFRACTIONf_plane_restr0.0053120
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.32620.41732110.39564028X-RAY DIFFRACTION98
2.3262-2.35350.40222090.36774037X-RAY DIFFRACTION100
2.3535-2.38220.40842140.3524058X-RAY DIFFRACTION99
2.3822-2.41240.33982120.334054X-RAY DIFFRACTION100
2.4124-2.44410.33472160.31274064X-RAY DIFFRACTION100
2.4441-2.47760.34182140.30454083X-RAY DIFFRACTION100
2.4776-2.5130.35882110.29144041X-RAY DIFFRACTION100
2.513-2.55050.35022160.28244099X-RAY DIFFRACTION100
2.5505-2.59040.32432150.26744088X-RAY DIFFRACTION100
2.5904-2.63280.3412140.2674063X-RAY DIFFRACTION100
2.6328-2.67820.30312140.24924081X-RAY DIFFRACTION100
2.6782-2.7270.3212160.23324105X-RAY DIFFRACTION100
2.727-2.77940.27742130.22294037X-RAY DIFFRACTION100
2.7794-2.83610.2672170.21454128X-RAY DIFFRACTION100
2.8361-2.89780.26362160.20594110X-RAY DIFFRACTION100
2.8978-2.96520.26632140.20374068X-RAY DIFFRACTION100
2.9652-3.03940.26732180.20134121X-RAY DIFFRACTION100
3.0394-3.12150.2612140.20134085X-RAY DIFFRACTION100
3.1215-3.21340.27112180.19784103X-RAY DIFFRACTION100
3.2134-3.31710.25812160.18584112X-RAY DIFFRACTION100
3.3171-3.43570.23172160.17494118X-RAY DIFFRACTION100
3.4357-3.57320.21822170.16224128X-RAY DIFFRACTION100
3.5732-3.73580.23232170.16294106X-RAY DIFFRACTION100
3.7358-3.93280.19812180.16314142X-RAY DIFFRACTION100
3.9328-4.17910.21372170.15674157X-RAY DIFFRACTION100
4.1791-4.50180.18222180.14424151X-RAY DIFFRACTION100
4.5018-4.95470.18372210.14234180X-RAY DIFFRACTION100
4.9547-5.67130.21892200.16574176X-RAY DIFFRACTION100
5.6713-7.1440.23322230.19014245X-RAY DIFFRACTION100
7.144-67.88360.19062330.15534401X-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)
12.3249-0.1088-0.91473.46960.77533.15040.09020.11980.3654-0.46180.1601-0.3366-0.69690.3606-0.24660.6169-0.08130.09720.5375-0.1750.549631.797587.549151.5889
22.5763-0.7152-0.56134.00380.97183.72930.0326-0.13260.24990.38290.05110.1665-0.2024-0.0694-0.08330.46890.02690.06460.4302-0.10560.462719.664281.336565.6507
30.8043-1.06170.12185.68132.04623.5135-0.1765-0.34160.25411.02920.18590.1591-0.0917-0.0876-0.03220.57710.04310.15950.5573-0.10510.543318.92882.424273.1449
43.1555-3.7605-4.05397.82797.36417.4058-0.1797-0.0977-0.16670.70490.4211-0.30851.19811.0751-0.32920.48740.1483-0.09860.5005-0.0760.591833.054761.25860.3887
56.7862-1.1977-0.59355.94931.43064.5841-0.07070.28270.8136-0.8557-0.120.4558-1.1617-0.45370.17790.7240.1243-0.06720.4971-0.01880.550416.045869.379818.9881
64.64760.5706-1.57495.43921.40674.72580.03970.48980.0689-0.81690.2161-0.4328-0.62880.2086-0.28360.4694-0.03390.050.5662-0.08780.409829.231355.917614.3338
73.73791.43040.82845.53542.88435.1418-0.1818-0.13910.1498-0.02590.07060.1669-0.1290.07930.11080.33130.07810.02850.3751-0.0870.469524.724752.737425.9581
87.7499-2.6288-0.43672.6512-2.50943.99260.3728-0.771-0.6166-0.0654-0.23540.77290.6689-1.7886-0.03050.4863-0.09430.07820.9395-0.25970.64095.516550.381128.2062
93.0926-0.24250.21152.20750.26983.55190.0471-0.16470.0186-0.1714-0.20110.6935-0.2643-0.85140.1430.47160.11560.02730.5941-0.21440.65278.505460.698934.7374
104.7011-1.8782.17053.1592-1.42274.7057-0.4742-0.2398-0.01220.6688-0.05430.5039-0.3593-1.33220.48640.61810.07490.12590.803-0.2480.66616.467359.960544.4492
114.2036-5.7174-3.94569.34667.22985.4332-0.06640.1064-0.26320.3185-0.52480.97990.7298-0.53410.59180.5772-0.06950.07060.4893-0.07310.49615.965341.505734.0748
122.242-1.844-2.26417.9077.65658.8199-0.3165-0.2656-0.35271.17820.24590.06051.60990.65450.02960.5240.0321-0.06480.3971-0.02790.55726.153337.687730.8829
131.6463-0.7446-0.21353.67440.33111.8465-0.03080.23910.1686-0.37450.15230.0677-0.3070.1031-0.11380.4169-0.12410.01540.5089-0.00750.455520.367332.4756-11.8387
140.8359-0.42890.30791.85190.84082.1659-0.0517-0.05840.11580.1130.03680.2317-0.0206-0.2950.02060.4121-0.08250.05440.4626-0.03370.54788.296825.34163.3734
156.0771-3.5764-0.50236.71460.25572.51140.0131.00120.2543-1.33070.23760.044-0.0769-0.186-0.18120.8865-0.37120.02941.1416-0.03690.469517.40589.3687-44.2714
162.70010.0772-0.5791.55630.18673.2614-0.36310.7136-0.5285-0.5990.3718-0.36850.64790.1081-0.0480.8754-0.22470.15370.986-0.31070.612925.1196-4.602-36.9976
172.4484-0.1391-1.8916.0092-0.82252.23280.19080.96090.0966-0.0586-0.12960.49320.1914-0.23350.1650.7161-0.1266-0.0330.8049-0.05580.549410.85452.0955-33.9167
183.17920.03070.55192.4991-0.49543.02490.05360.6335-0.097-0.36030.2760.09630.4217-0.2628-0.33190.5765-0.17390.00910.87-0.17490.483610.3962.0815-24.7202
192.6917-0.8729-0.33963.7025-0.40472.9136-0.27830.6654-0.2885-0.2020.26040.16020.4947-0.44420.04820.617-0.22020.05070.6682-0.1040.47519.2595-4.2571-21.2405
204.1819-2.6223-3.1035.33123.42762.6344-0.62590.2336-1.1483-0.07770.2103-0.37991.10970.64060.08090.94070.02240.12330.8333-0.40360.982730.4256-16.7962-24.3533
214.0844-4.6888-0.75675.31421.51222.0076-0.4628-0.60120.63670.8730.962-0.9978-0.20110.7307-0.42861.283-0.0424-0.15560.8883-0.25120.849427.535991.915781.8667
220.4168-0.1262-0.43712.18882.31223.0111-0.18140.0622-0.04140.48120.8518-0.60220.68331.131-1.03830.5070.0954-0.02930.8327-0.29530.783343.282727.92724.1501
236.83181.5899-2.93855.6372-0.00893.931-0.68690.6639-1.0342-0.18270.2949-0.0881.5706-0.35810.33661.2744-0.08160.19370.7269-0.16230.7166.339153.790469.3423
243.75550.5259-0.06154.5708-2.35735.7401-0.049-1.1878-0.75070.5993-0.3306-0.7730.49211.64650.41930.85850.25510.00961.35930.24110.862214.446157.3171105.4359
253.47020.5323-1.9591.8924-1.2513.5181-0.5663-0.091-0.8770.01020.2188-0.07911.2093-0.1190.12581.14410.03160.20590.57480.07910.7946-2.036753.7392.2727
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 180)
2X-RAY DIFFRACTION2chain 'A' and (resid 181 through 311)
3X-RAY DIFFRACTION3chain 'A' and (resid 312 through 401)
4X-RAY DIFFRACTION4chain 'A' and (resid 402 through 436)
5X-RAY DIFFRACTION5chain 'B' and (resid 2 through 88)
6X-RAY DIFFRACTION6chain 'B' and (resid 89 through 127)
7X-RAY DIFFRACTION7chain 'B' and (resid 128 through 197)
8X-RAY DIFFRACTION8chain 'B' and (resid 198 through 223)
9X-RAY DIFFRACTION9chain 'B' and (resid 224 through 295)
10X-RAY DIFFRACTION10chain 'B' and (resid 296 through 373)
11X-RAY DIFFRACTION11chain 'B' and (resid 374 through 401)
12X-RAY DIFFRACTION12chain 'B' and (resid 402 through 438)
13X-RAY DIFFRACTION13chain 'C' and (resid 1 through 197)
14X-RAY DIFFRACTION14chain 'C' and (resid 198 through 440)
15X-RAY DIFFRACTION15chain 'D' and (resid 2 through 88)
16X-RAY DIFFRACTION16chain 'D' and (resid 89 through 228)
17X-RAY DIFFRACTION17chain 'D' and (resid 230 through 240)
18X-RAY DIFFRACTION18chain 'D' and (resid 242 through 295)
19X-RAY DIFFRACTION19chain 'D' and (resid 296 through 401)
20X-RAY DIFFRACTION20chain 'D' and (resid 402 through 441)
21X-RAY DIFFRACTION21chain 'E' and (resid 6 through 46)
22X-RAY DIFFRACTION22chain 'E' and (resid 47 through 144)
23X-RAY DIFFRACTION23chain 'F' and (resid 1 through 66)
24X-RAY DIFFRACTION24chain 'F' and (resid 67 through 198)
25X-RAY DIFFRACTION25chain 'F' and (resid 199 through 384)

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