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- PDB-4o4j: Tubulin-Peloruside A complex -

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Basic information

Entry
Database: PDB / ID: 4o4j
TitleTubulin-Peloruside A complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligase
KeywordsCELL CYCLE/INHIBITOR / ALPHA-TUBULIN / BETA-TUBULIN / LIGASE / GTPASE / MICROTUBULE / STATHMIN / PELORUSIDE A / CELL CYCLE / TUBULIN FOLD / CYTOSKELETON / CELL CYCLE-INHIBITOR complex
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 / 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 / cellular response to interleukin-4 / tubulin binding / 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 / cytoplasm / cytosol
Similarity search - Function
Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Rossmann fold - #11480 / Helix hairpin bin / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / 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 / Helix hairpin bin / 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. / 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; / 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
PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Peloruside A / 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 / DIFFERENCE FOURIER / Resolution: 2.2 Å
AuthorsProta, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Structural basis of microtubule stabilization by laulimalide and peloruside A.
Authors: Prota, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
History
DepositionDec 18, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 26, 2014Provider: repository / Type: Initial release
Revision 1.1Sep 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.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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)265,39619
Polymers261,6316
Non-polymers3,76513
Water15,223845
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.370, 157.840, 180.360
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 / Details: BRAIN / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P81947
#2: Protein Tubulin beta-2B chain


Mass: 49999.887 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: BRAIN / 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 / Fragment: UNP residues 49-189
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / 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) / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 858 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.: 4 / Source method: obtained synthetically / Formula: Mg
#7: Chemical ChemComp-CA / CALCIUM ION


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


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#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-POU / Peloruside A / (1R,3R,4S,7S,9S,11S,13R,14R,15R)-4,11,13,14-tetrahydroxy-7-[(2Z,4R)-4-(hydroxymethyl)hex-2-en-2-yl]-3,9,15-trimethoxy-12,12-dimethyl-6,17-dioxabicyclo[11.3.1]heptadecan-5-one


Mass: 548.663 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H48O11
#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.: 845 / 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: 2.84 Å3/Da / Density % sol: 56.68 %
Crystal growTemperature: 293 K / pH: 6.7
Details: 6% PEG, 16% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M 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: X06DA / Wavelength: 1
DetectorType: PSI PILATUS 2M / Detector: PIXEL / Date: Feb 10, 2013
RadiationMonochromator: VERTICALLY COLLIMATING MIRROR (M1, FOCUS AT INFINITY), FOLLOWED BY A BARTELS MONOCHROMATOR WITH DUAL CHANNEL CUT CRYSTALS (DCCM) IN (+--+) GEOMETRY, AND A TOROIDAL MIRROR (M2) TO ...Monochromator: VERTICALLY COLLIMATING MIRROR (M1, FOCUS AT INFINITY), FOLLOWED BY A BARTELS MONOCHROMATOR WITH DUAL CHANNEL CUT CRYSTALS (DCCM) IN (+--+) GEOMETRY, AND A TOROIDAL MIRROR (M2) TO VERTICALLY AND HORIZONTALLY FOCUS THE BEAM AT THE SAMPLE POSITION (WITH 2:1 HORIZONTAL DEMAGNIFICATION)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.2→72.3 Å / Num. obs: 150728 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6.7 % / Rmerge(I) obs: 0.115 / Net I/σ(I): 13.09
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 6.5 % / Rmerge(I) obs: 1.958 / Mean I/σ(I) obs: 1.1 / % possible all: 96.2

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Processing

Software
NameVersionClassification
DA+data collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 4I4T

4i4t


Resolution: 2.2→72.3 Å / SU ML: 0.31 / σ(F): 1.99 / Phase error: 25.01 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.239 7568 5.02 %
Rwork0.201 --
obs0.203 150719 99.7 %
all-151188 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.2→72.3 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16813 0 238 845 17896
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00517700
X-RAY DIFFRACTIONf_angle_d0.97424088
X-RAY DIFFRACTIONf_dihedral_angle_d16.1616658
X-RAY DIFFRACTIONf_chiral_restr0.0662652
X-RAY DIFFRACTIONf_plane_restr0.0043121
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2001-2.22510.37692370.34154319X-RAY DIFFRACTION92
2.2251-2.25130.32642370.29744746X-RAY DIFFRACTION100
2.2513-2.27870.30382580.28754723X-RAY DIFFRACTION100
2.2787-2.30760.34472530.28434729X-RAY DIFFRACTION100
2.3076-2.33790.29712590.2734728X-RAY DIFFRACTION100
2.3379-2.370.30562430.26244763X-RAY DIFFRACTION100
2.37-2.40380.30852480.25794717X-RAY DIFFRACTION100
2.4038-2.43970.29872370.2564778X-RAY DIFFRACTION100
2.4397-2.47780.29412560.23734718X-RAY DIFFRACTION100
2.4778-2.51840.27742530.23424744X-RAY DIFFRACTION100
2.5184-2.56190.28992430.24024781X-RAY DIFFRACTION100
2.5619-2.60850.27012450.22594773X-RAY DIFFRACTION100
2.6085-2.65860.27362300.22544733X-RAY DIFFRACTION100
2.6586-2.71290.2852610.22614759X-RAY DIFFRACTION100
2.7129-2.77190.26082450.22054776X-RAY DIFFRACTION100
2.7719-2.83640.272570.22464755X-RAY DIFFRACTION100
2.8364-2.90730.28152620.22614790X-RAY DIFFRACTION100
2.9073-2.98590.27342550.23064736X-RAY DIFFRACTION100
2.9859-3.07380.26252350.20524796X-RAY DIFFRACTION100
3.0738-3.1730.2332530.20484775X-RAY DIFFRACTION100
3.173-3.28640.24832720.20064764X-RAY DIFFRACTION100
3.2864-3.4180.23462630.19084766X-RAY DIFFRACTION100
3.418-3.57350.24322580.18594809X-RAY DIFFRACTION100
3.5735-3.76190.22452590.17444788X-RAY DIFFRACTION100
3.7619-3.99760.17512380.16074840X-RAY DIFFRACTION100
3.9976-4.30620.1962520.16174823X-RAY DIFFRACTION100
4.3062-4.73950.1892840.15444855X-RAY DIFFRACTION100
4.7395-5.42510.21712530.16874848X-RAY DIFFRACTION100
5.4251-6.83430.2332590.19874913X-RAY DIFFRACTION100
6.8343-72.34030.21242630.19975106X-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)
10.79970.068-0.04481.92610.71051.10350.19580.07950.3765-0.2990.0293-0.2256-0.77560.1587-0.07240.5229-0.070.10120.2757-0.07980.312228.243299.069254.6109
20.25350.10460.25250.80420.32910.657-0.03090.16410.1582-0.23270.346-0.3487-0.38440.4028-0.07090.2921-0.0160.14040.2043-0.36140.207234.28183.515248.3641
30.44630.0544-0.22521.70730.73211.67990.0430.0070.08190.27990.0622-0.08110.00270.1121-0.08510.23880.03310.00660.1749-0.08510.203224.244480.930262.7376
40.37660.1471-0.19611.48570.54352.56790.1234-0.0102-0.03250.2897-0.19090.50690.0888-0.43820.12620.3833-0.00710.14860.3021-0.17690.3129.402384.072671.9111
51.1662-0.7562-0.34912.10441.71341.4654-0.1587-0.3693-0.00910.72410.08930.22440.2432-0.28080.28990.53770.02850.10720.2848-0.12740.290516.936889.965980.6808
61.15660.17190.49381.35770.40452.34740.0791-0.03720.00580.3099-0.0080.2140.2898-0.1527-0.00480.45280.00860.05950.2712-0.11130.265717.910889.680273.6932
70.1687-0.1637-0.11440.72440.84121.0787-0.054-0.11620.00270.65310.07390.03440.42910.115-0.07060.38410.07330.01370.1902-0.0850.239222.844569.508566.676
80.30020.10490.08151.30190.79380.94380.0195-0.0318-0.01590.52230.1455-0.20110.18280.2387-0.1330.36520.1843-0.12910.2174-0.15830.296933.069462.229862.1353
90.9185-0.1592-0.04171.2130.88541.59840.02950.0580.1107-0.0442-0.06990.0824-0.2479-0.1109-0.17360.11980.01420.03490.182-0.08390.195416.760459.654226.0442
100.4613-0.2178-0.13441.40280.98341.4488-0.0489-0.1007-0.02850.428-0.05060.17960.2576-0.1541-0.0580.1296-0.00770.04440.1906-0.0770.202615.243450.37238.631
111.2131-0.314-0.11562.64090.92152.1077-0.00470.11520.2426-0.19410.00960.0781-0.3617-0.00090.01680.1533-0.0401-0.00520.17250.0010.168914.619242.4337-13.0886
120.8029-0.0078-0.05871.29150.70211.05670.00180.23820.0012-0.34950.104-0.1927-0.16280.1396-0.08170.1333-0.04320.03110.1882-0.04670.153524.99430.6361-14.6126
130.5599-0.1251-0.21071.4450.21341.3362-0.08270.00810.16560.0962-0.0040.15040.15020.0241-0.07990.111-0.0126-0.00680.1566-0.07060.145720.715720.756-3.7143
140.7993-0.30570.24410.58780.54740.93050.0653-0.03730.0244-0.0272-0.12380.19160.0473-0.33940.09330.1137-0.02790.01580.2239-0.04660.19533.895528.71040.4009
150.9889-0.09350.36590.89670.40391.3918-0.0475-0.09320.1076-0.0698-0.06940.14180.1371-0.35330.11480.131-0.03080.02280.2145-0.0710.20451.357434.66198.7383
160.5997-0.4758-0.28491.25870.88631.376-0.0258-0.0151-0.11690.26750.0913-0.03480.34840.1755-0.05630.16630.0012-0.02710.1276-0.05560.21720.474413.27742.5006
172.2002-0.1829-0.14242.49220.84372.0436-0.06060.41740.2808-0.48490.1460.1435-0.1513-0.36760.03970.2843-0.07070.02790.5668-0.06130.203715.308511.406-41.0667
180.7031-0.3815-0.26661.14220.53011.6424-0.07020.59930.0111-0.36770.1307-0.28820.1450.0791-0.21840.3499-0.06290.08320.6605-0.24190.305528.99822.6421-43.2638
190.5932-0.2122-0.05470.24060.09920.5617-0.09030.2595-0.20950.06560.0207-0.1330.6371-0.0866-0.55740.4947-0.10620.05960.4066-0.37570.40222.3358-8.6848-32.4119
200.44450.33360.35630.42570.63271.0446-0.04370.1286-0.2064-0.1399-0.04820.19020.3828-0.3966-0.09130.4266-0.244-0.03550.6466-0.20110.32367.3295-8.0181-39.0268
210.9350.00160.0551.18550.1372.2877-0.05280.3742-0.0686-0.04260.073-0.10420.0801-0.1152-0.00630.1842-0.0420.04720.2606-0.11570.226518.43426.2822-23.3377
220.393-0.3651-0.20972.0313-0.11941.32980.22160.2832-0.2308-0.3517-0.09730.53240.3928-0.51380.33490.4583-0.2301-0.02390.5991-0.22030.37251.1622-5.8517-26.6458
231.25740.2863-0.16951.14330.76861.9952-0.08920.11170.14310.1876-0.13220.23050.0071-0.79090.10560.1871-0.1005-0.01890.5489-0.11070.2732.16964.9888-18.6907
240.6047-0.1096-0.36580.87920.17421.1168-0.01360.3513-0.403-0.07520.124-0.05440.5811-0.12480.16070.4884-0.0656-0.02760.373-0.19890.394818.4845-9.6956-25.7356
251.9692-0.3876-1.23352.47011.39394.0428-0.144-0.1927-0.25360.42990.144-0.22280.73690.386-0.09770.62160.0608-0.09930.3245-0.12890.471627.3168-13.384-17.1828
261.2176-0.45820.01731.13260.56221.00340.0603-0.10920.08720.45660.2155-0.35310.42320.4921-0.00080.70080.0223-0.07660.378-0.15440.357827.624493.346281.5154
270.268-0.1240.09921.26361.05671.26390.03070.0269-0.09130.06610.3089-0.42430.20.427-0.30150.20010.00070.07460.4195-0.21290.438543.255328.05733.594
281.1201-0.2683-0.43720.17710.21230.9447-0.1678-0.5034-0.54930.26620.043-0.26371.00240.0026-0.01761.156-0.12880.11640.59410.02780.557110.403955.079184.8024
29-0.0010.02550.04180.95360.42940.528-0.0786-0.1845-0.66350.6058-0.2252-0.11910.91570.35250.14091.4743-0.04370.22310.98920.1620.9772.276745.081599.8393
300.5973-0.0521-0.18170.89060.32480.89-0.1887-0.2056-0.5410.3530.21640.1210.5988-0.13440.22441.0563-0.18490.26830.7576-0.07340.53072.845757.45689.0182
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 160 )
3X-RAY DIFFRACTION3chain 'A' and (resid 161 through 273 )
4X-RAY DIFFRACTION4chain 'A' and (resid 274 through 311 )
5X-RAY DIFFRACTION5chain 'A' and (resid 312 through 338 )
6X-RAY DIFFRACTION6chain 'A' and (resid 339 through 372 )
7X-RAY DIFFRACTION7chain 'A' and (resid 373 through 401 )
8X-RAY DIFFRACTION8chain 'A' and (resid 402 through 439 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 311 )
10X-RAY DIFFRACTION10chain 'B' and (resid 312 through 438 )
11X-RAY DIFFRACTION11chain 'C' and (resid 1 through 72 )
12X-RAY DIFFRACTION12chain 'C' and (resid 73 through 161 )
13X-RAY DIFFRACTION13chain 'C' and (resid 162 through 199 )
14X-RAY DIFFRACTION14chain 'C' and (resid 200 through 311 )
15X-RAY DIFFRACTION15chain 'C' and (resid 312 through 372 )
16X-RAY DIFFRACTION16chain 'C' and (resid 373 through 440 )
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 56 )
18X-RAY DIFFRACTION18chain 'D' and (resid 57 through 160 )
19X-RAY DIFFRACTION19chain 'D' and (resid 161 through 214 )
20X-RAY DIFFRACTION20chain 'D' and (resid 215 through 238 )
21X-RAY DIFFRACTION21chain 'D' and (resid 239 through 268 )
22X-RAY DIFFRACTION22chain 'D' and (resid 269 through 311 )
23X-RAY DIFFRACTION23chain 'D' and (resid 312 through 337 )
24X-RAY DIFFRACTION24chain 'D' and (resid 338 through 415 )
25X-RAY DIFFRACTION25chain 'D' and (resid 416 through 441 )
26X-RAY DIFFRACTION26chain 'E' and (resid 6 through 46 )
27X-RAY DIFFRACTION27chain 'E' and (resid 47 through 143 )
28X-RAY DIFFRACTION28chain 'F' and (resid 1 through 207 )
29X-RAY DIFFRACTION29chain 'F' and (resid 208 through 275 )
30X-RAY DIFFRACTION30chain 'F' and (resid 280 through 378 )

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