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- PDB-5ng1: TUBULIN-MTC-zampanolide complex -

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Basic information

Entry
Database: PDB / ID: 5ng1
TitleTUBULIN-MTC-zampanolide 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 / 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 / cytosol / cytoplasm
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. / 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; / 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. / Dna Ligase; domain 1 / 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-8WB / Chem-8WE / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Chem-ZPN / 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: 2.2 Å
AuthorsField, J.J. / Pera, B. / Estevez Gallego, J. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Prota, A.E. / Menchon, G. ...Field, J.J. / Pera, B. / Estevez Gallego, J. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Prota, A.E. / Menchon, G. / Miller, J.H. / Altmann, K.-H. / Diaz, J.F.
CitationJournal: J. Nat. Prod. / Year: 2018
Title: Zampanolide Binding to Tubulin Indicates Cross-Talk of Taxane Site with Colchicine and Nucleotide Sites.
Authors: Field, J.J. / Pera, B. / Gallego, J.E. / Calvo, E. / Rodriguez-Salarichs, J. / Saez-Calvo, G. / Zuwerra, D. / Jordi, M. / Andreu, J.M. / Prota, A.E. / Menchon, G. / Miller, J.H. / Altmann, K.H. / Diaz, J.F.
History
DepositionMar 16, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 25, 2017Provider: repository / Type: Initial release
Revision 1.1Apr 4, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.2May 2, 2018Group: Data collection / Category: reflns / Item: _reflns.pdbx_Rpim_I_all
Revision 1.3Jan 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
Revision 1.4Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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)266,16424
Polymers261,6316
Non-polymers4,53318
Water10,269570
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: equilibrium centrifugation
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22800 Å2
ΔGint-147 kcal/mol
Surface area79530 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.237, 157.418, 178.858
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 , 11 types, 588 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-8WB / 2-methoxy-5-(2,3,4-trimethoxyphenyl)cyclohepta-2,4,6-trien-1-one


Mass: 302.322 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H18O5
#10: Chemical ChemComp-8WE / (2~{Z},4~{E})-~{N}-[(~{S})-oxidanyl-[(1~{S},2~{E},5~{S},11~{R},17~{S},19~{R})-3,11,19-trimethyl-7,13-bis(oxidanylidene)-6,21-dioxabicyclo[15.3.1]henicos-2-en-5-yl]methyl]hexa-2,4-dienamide


Mass: 503.671 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H45NO6
#11: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#12: 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
#13: Chemical ChemComp-ZPN / (2Z,4E)-N-[(S)-[(1S,2E,5S,8E,10Z,17S)-3,11-dimethyl-19-methylidene-7,13-dioxo-6,21-dioxabicyclo[15.3.1]henicosa-2,8,10-trien-5-yl](hydroxy)methyl]hexa-2,4-dienamide / (-)-ZAMPANOLIDE (Bound form)


Mass: 497.623 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C29H39NO6
#14: 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
#15: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 570 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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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: 2.8 Å3/Da / Density % sol: 56.14 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 6.7
Details: 5% PEG 4K, 12-14% glycerol, 30 mM MgCl2, 30 mM CaCl2, 100 mM MES/Imidazole, pH 6.7

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.00003 Å
DetectorType: DECTRIS PILATUS 2 / Detector: PIXEL / Date: Oct 18, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00003 Å / Relative weight: 1
ReflectionResolution: 2.2→47.69 Å / Num. obs: 149309 / % possible obs: 100 % / Redundancy: 6.7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.107 / Rpim(I) all: 0.046 / Net I/σ(I): 13.4
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 6.5 % / Rmerge(I) obs: 2.047 / Mean I/σ(I) obs: 0.9 / Num. unique obs: 11007 / CC1/2: 0.291 / Rpim(I) all: 0.922 / % possible all: 99.8

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Processing

Software
NameVersionClassification
PHENIX(dev_2420: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHENIXphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS
Starting model: 4I4T

4i4t


Resolution: 2.2→47.686 Å / SU ML: 0.29 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 23.72
RfactorNum. reflection% reflection
Rfree0.2198 7478 5.01 %
Rwork0.1729 --
obs0.1753 149309 99.95 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.2→47.686 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17458 0 292 570 18320
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00818191
X-RAY DIFFRACTIONf_angle_d0.95724662
X-RAY DIFFRACTIONf_dihedral_angle_d21.46777
X-RAY DIFFRACTIONf_chiral_restr0.0792675
X-RAY DIFFRACTIONf_plane_restr0.0053184
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.2250.34192750.31194612X-RAY DIFFRACTION99
2.225-2.25120.37372520.2974665X-RAY DIFFRACTION100
2.2512-2.27860.32512480.27874677X-RAY DIFFRACTION100
2.2786-2.30750.32062450.27354676X-RAY DIFFRACTION100
2.3075-2.33780.32842330.26714689X-RAY DIFFRACTION100
2.3378-2.36990.28522690.25424702X-RAY DIFFRACTION100
2.3699-2.40370.32272240.25284667X-RAY DIFFRACTION100
2.4037-2.43960.31182280.24784709X-RAY DIFFRACTION100
2.4396-2.47770.29882580.23294704X-RAY DIFFRACTION100
2.4777-2.51830.29652620.23544681X-RAY DIFFRACTION100
2.5183-2.56180.27912710.21074655X-RAY DIFFRACTION100
2.5618-2.60830.2632500.19854686X-RAY DIFFRACTION100
2.6083-2.65850.27242200.19664733X-RAY DIFFRACTION100
2.6585-2.71280.2692350.20024709X-RAY DIFFRACTION100
2.7128-2.77170.26642510.19844709X-RAY DIFFRACTION100
2.7717-2.83620.2382340.19224730X-RAY DIFFRACTION100
2.8362-2.90710.25522290.19044721X-RAY DIFFRACTION100
2.9071-2.98570.25172350.18454733X-RAY DIFFRACTION100
2.9857-3.07360.24462630.17574704X-RAY DIFFRACTION100
3.0736-3.17270.22512400.17644715X-RAY DIFFRACTION100
3.1727-3.28610.21952740.17444702X-RAY DIFFRACTION100
3.2861-3.41770.23782500.17054720X-RAY DIFFRACTION100
3.4177-3.57310.20872810.16044734X-RAY DIFFRACTION100
3.5731-3.76150.19212530.15384736X-RAY DIFFRACTION100
3.7615-3.9970.18252690.14174739X-RAY DIFFRACTION100
3.997-4.30540.17472190.1384783X-RAY DIFFRACTION100
4.3054-4.73840.15882480.12054827X-RAY DIFFRACTION100
4.7384-5.42320.17952590.13954796X-RAY DIFFRACTION100
5.4232-6.82940.21372290.17544878X-RAY DIFFRACTION100
6.8294-47.69750.19252740.16685039X-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)
10.1167-0.1527-0.3880.8839-0.28561.01420.18780.13780.1447-0.23620.00660.0505-0.43230.12470.00010.56380.00510.09890.3979-0.07460.437827.864296.229850.7035
20.5642-0.4241-0.38651.33880.09550.84370.08910.0365-0.0049-0.03020.085-0.1674-0.07530.21280.00010.3274-0.03460.05170.3872-0.16140.389534.496578.49852.8857
30.8592-0.33380.11760.99940.18291.4490.19030.1123-0.01090.1687-0.05350.0208-0.1870.0028-0.00010.36260.03730.06010.332-0.10040.387220.776984.410464.0123
40.3520.0476-0.23350.07250.18840.64990.458-0.0741-0.09810.3434-0.32910.62730.2942-0.52440.00880.46620.02030.17570.422-0.15040.58838.85884.521471.0161
50.62330.50010.26621.60350.21880.98230.0494-0.14230.11280.4956-0.00490.1166-0.0787-0.07260.00030.52560.00610.12360.388-0.12770.344218.736383.288972.7817
60.80820.4465-0.1420.6473-0.18240.06360.05880.0362-0.12240.33710.1671-0.08070.32810.3093-0.00010.44870.0933-0.02410.3024-0.11990.430231.944262.221662.4897
71.0774-0.0595-0.46330.4441-0.620.88880.15190.20860.4165-0.3315-0.21510.1929-0.6948-0.1869-00.56710.0758-0.04320.345-0.07670.48515.756872.247521.7377
80.01980.0088-0.041-0.00720.01560.18940.10720.54790.0022-0.8225-0.22260.1202-0.343-0.0718-0.00040.51090.0703-0.07760.4105-0.07880.465117.566662.408510.882
90.1112-0.1922-0.19850.17910.21020.49970.07350.4011-0.0986-0.33050.0541-0.0841-0.24260.29220.00010.3465-0.06210.04310.3833-0.06610.326729.145256.043414.1803
100.7755-0.5129-0.22431.24250.69192.12020.0165-0.0436-0.056-0.0464-0.11460.0349-0.1684-0.1333-0.00430.22230.01690.01240.3392-0.14620.334917.55153.17626.1598
110.1677-0.1437-0.17510.2164-0.02280.21290.0653-0.21970.31230.3103-0.1184-0.1739-0.25750.0615-0.06420.37380.02770.07330.3088-0.24360.480520.333764.549839.0791
120.12230.01310.330.11670.03350.4059-0.15630.1717-0.26390.4577-0.23150.3850.0958-0.6854-0.01310.4237-0.01450.10850.6351-0.26880.56763.819355.081139.1159
130.353-0.50470.02760.5992-0.19590.0941-0.7274-0.69470.49220.68110.2823-0.2778-0.4796-1.1732-0.33050.59420.27540.02110.8272-0.27450.50944.652664.802746.3789
141.01670.08290.11580.77440.32710.2099-0.0387-0.62530.14750.4197-0.38250.3613-0.3768-0.952-0.24230.31970.20090.06310.4449-0.3410.45169.030662.251644.2726
150.1744-0.41850.28890.25490.04410.87280.211-0.0591-0.01420.2763-0.49770.26860.3599-0.4407-0.06840.3417-0.03070.0910.4301-0.14730.428215.101943.034634.0263
16-0.10050.26360.00060.66330.27190.2601-0.0107-0.1378-0.26860.41040.0788-0.1750.56220.6930.00220.35270.0083-0.03880.4077-0.03870.297325.987238.040830.7469
171.3884-0.1696-0.07851.73950.23931.44180.00150.17550.0562-0.18210.0436-0.0295-0.1060.124-0.00010.2167-0.06530.02530.2904-0.05580.240620.474632.7822-11.9651
181.0433-0.51870.06061.38360.93571.4189-0.0292-0.01060.0360.0969-0.04340.06680.0802-0.1566-0.00030.1998-0.05310.03190.254-0.04140.25568.050225.72013.1181
190.9667-0.1190.1370.409-0.36080.6495-0.18320.44470.2767-0.19270.2665-0.0712-0.2134-0.0332-00.5183-0.13960.02950.6811-0.02240.422815.507112.2064-41.709
200.7781-0.122-0.03180.5822-0.48920.8095-0.24150.5177-0.0534-0.37310.3286-0.25120.03740.3521-0.00420.5122-0.1110.12680.7522-0.23020.445629.32031.0784-42.8473
210.6647-0.4494-0.22060.16170.02110.5717-0.2920.3058-0.1724-0.3330.2743-0.09240.17910.17930.00360.4932-0.05310.04990.5138-0.22750.451221.693-8.5317-32.255
220.8425-0.0772-0.61580.62790.0281.0377-0.14210.39050.0198-0.13640.2475-0.11820.0647-0.1505-0.00020.3797-0.07180.01490.516-0.12210.353313.35771.1965-29.8427
230.1009-0.0074-0.10760.19770.26920.36520.09290.057-0.09220.12950.01240.10870.423-0.49420.00030.4497-0.1446-0.02040.6591-0.15020.4281-0.9904-3.4042-28.3695
240.87670.2688-0.24130.5899-0.11.554-0.1370.1779-0.0674-0.02140.20160.11270.2287-0.23050.0010.4186-0.03380.00580.4045-0.09080.38268.5452-3.103-21.1327
251.0357-0.361-0.21280.86450.07020.5062-0.3797-0.2755-1.00410.45310.0723-0.11010.85310.7115-0.08860.56950.11040.05210.4801-0.26780.690130.2529-17.1454-24.6356
261.41980.07570.04250.03840.1607-0.0090.0412-0.02310.43250.47920.0472-0.27110.03180.09650.02690.9257-0.09390.03140.4706-0.160.478627.229992.907481.3325
270.092-0.0739-0.10810.16040.0380.0642-0.10060.00880.00290.22810.2948-0.14540.32110.4860.00540.32830.03850.03670.5768-0.26050.487143.066327.8793.9283
281.24640.3451-0.97450.2095-0.27330.6275-0.44650.3234-0.3432-0.1436-0.0555-0.18170.88090.0586-0.13730.7518-0.09970.13220.4474-0.13110.4697.789656.499573.8052
290.4330.3251-0.10590.36620.32970.37530.0496-0.55590.03010.3046-0.0874-0.44290.01060.94160.00230.64290.1114-0.11671.03130.06870.727218.521858.7493105.8574
301.2124-0.0326-0.68760.12220.29170.4728-0.2554-0.0673-0.38530.00240.0682-0.11430.8315-0.1106-0.01430.7579-0.02420.11010.27450.07180.5333-1.825753.442796.3851
310.11410.067-0.07270.0276-0.04310.018-0.29180.3106-0.3105-0.21750.6526-0.61110.1630.195-0.00041.35770.32250.04980.94360.18211.26748.19741.6949105.8333
321.2737-0.2081-0.39980.17030.43221.3647-0.220.0372-0.43550.02810.1397-0.05710.5324-0.0468-0.0130.73280.01550.12510.29540.03130.5151-1.784955.583895.4133
330.08290.03340.0150.0068-0.0050.1861-0.31620.5617-0.53860.04440.37190.13490.8534-0.6245-0.00030.7211-0.2530.07240.7043-0.08990.6898-7.54856.129179.2076
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 88 )
2X-RAY DIFFRACTION2chain 'A' and (resid 89 through 199 )
3X-RAY DIFFRACTION3chain 'A' and (resid 200 through 273 )
4X-RAY DIFFRACTION4chain 'A' and (resid 274 through 311 )
5X-RAY DIFFRACTION5chain 'A' and (resid 312 through 401 )
6X-RAY DIFFRACTION6chain 'A' and (resid 402 through 440 )
7X-RAY DIFFRACTION7chain 'B' and (resid 1 through 64 )
8X-RAY DIFFRACTION8chain 'B' and (resid 65 through 88 )
9X-RAY DIFFRACTION9chain 'B' and (resid 89 through 127 )
10X-RAY DIFFRACTION10chain 'B' and (resid 128 through 238 )
11X-RAY DIFFRACTION11chain 'B' and (resid 239 through 266 )
12X-RAY DIFFRACTION12chain 'B' and (resid 267 through 311 )
13X-RAY DIFFRACTION13chain 'B' and (resid 312 through 338 )
14X-RAY DIFFRACTION14chain 'B' and (resid 339 through 372 )
15X-RAY DIFFRACTION15chain 'B' and (resid 373 through 401 )
16X-RAY DIFFRACTION16chain 'B' and (resid 402 through 438 )
17X-RAY DIFFRACTION17chain 'C' and (resid 1 through 199 )
18X-RAY DIFFRACTION18chain 'C' and (resid 200 through 440 )
19X-RAY DIFFRACTION19chain 'D' and (resid 1 through 64 )
20X-RAY DIFFRACTION20chain 'D' and (resid 65 through 160 )
21X-RAY DIFFRACTION21chain 'D' and (resid 161 through 214 )
22X-RAY DIFFRACTION22chain 'D' and (resid 215 through 266 )
23X-RAY DIFFRACTION23chain 'D' and (resid 267 through 295 )
24X-RAY DIFFRACTION24chain 'D' and (resid 296 through 399 )
25X-RAY DIFFRACTION25chain 'D' and (resid 400 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 83 )
29X-RAY DIFFRACTION29chain 'F' and (resid 84 through 184 )
30X-RAY DIFFRACTION30chain 'F' and (resid 185 through 223 )
31X-RAY DIFFRACTION31chain 'F' and (resid 224 through 248 )
32X-RAY DIFFRACTION32chain 'F' and (resid 249 through 339 )
33X-RAY DIFFRACTION33chain 'F' and (resid 340 through 380 )

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