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- PDB-5sb9: Tubulin-maytansinoid-4a-complex -

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Basic information

Entry
Database: PDB / ID: 5sb9
TitleTubulin-maytansinoid-4a-complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-Tyrosine LigaseTubulin—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 / 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 / regulation of microtubule polymerization or depolymerization / microtubule-based process / 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 / cytosol / cytoplasm
Similarity search - Function
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-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-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
Similarity search - Domain/homology
Chem-5IX / PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / IMIDAZOLE / 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 / DIFFERENCE FOURIER / Resolution: 2.5 Å
AuthorsMarzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. ...Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.-C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Steinmetz, M.O. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
Funding supportEuropean Union, 1items
OrganizationGrant numberCountry
H2020-MSCA-ITN-2019860070 TUBINTRAINEuropean Union
CitationJournal: Chemistry / Year: 2022
Title: Maytansinol Derivatives: Side Reactions as a Chance for New Tubulin Binders.
Authors: Marzullo, P. / Boiarska, Z. / Perez-Pena, H. / Abel, A.C. / Alvarez-Bernad, B. / Lucena-Agell, D. / Vasile, F. / Sironi, M. / Altmann, K.H. / Prota, A.E. / Diaz, J.F. / Pieraccini, S. / Passarella, D.
History
DepositionJul 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 9, 2022Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 2.0Mar 9, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / diffrn_detector / diffrn_radiation_wavelength / diffrn_source / entity / entity_poly / entity_poly_seq / entity_src_gen / entity_src_nat / pdbx_contact_author / pdbx_deposit_group / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_validate_close_contact / pdbx_validate_torsion / refine / refine_hist / refine_ls_shell / reflns / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref_seq_dif
Item: _diffrn_detector.pdbx_collection_date / _diffrn_radiation_wavelength.wavelength ..._diffrn_detector.pdbx_collection_date / _diffrn_radiation_wavelength.wavelength / _diffrn_source.pdbx_wavelength_list / _entity.formula_weight / _entity_poly.pdbx_seq_one_letter_code / _entity_poly.pdbx_seq_one_letter_code_can / _entity_poly_seq.mon_id / _entity_src_gen.gene_src_common_name / _entity_src_nat.common_name / _pdbx_contact_author.address_1 / _pdbx_contact_author.name_last / _pdbx_deposit_group.group_type / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_poly_seq_scheme.auth_mon_id / _pdbx_poly_seq_scheme.mon_id / _pdbx_poly_seq_scheme.pdb_mon_id / _pdbx_refine_tls.L[1][1] / _pdbx_refine_tls.L[1][2] / _pdbx_refine_tls.L[1][3] / _pdbx_refine_tls.L[2][2] / _pdbx_refine_tls.L[2][3] / _pdbx_refine_tls.L[3][3] / _pdbx_refine_tls.S[1][1] / _pdbx_refine_tls.S[1][2] / _pdbx_refine_tls.S[1][3] / _pdbx_refine_tls.S[2][1] / _pdbx_refine_tls.S[2][2] / _pdbx_refine_tls.S[2][3] / _pdbx_refine_tls.S[3][1] / _pdbx_refine_tls.S[3][2] / _pdbx_refine_tls.S[3][3] / _pdbx_refine_tls.T[1][1] / _pdbx_refine_tls.T[1][2] / _pdbx_refine_tls.T[1][3] / _pdbx_refine_tls.T[2][2] / _pdbx_refine_tls.T[2][3] / _pdbx_refine_tls.T[3][3] / _pdbx_refine_tls.origin_x / _pdbx_refine_tls.origin_y / _pdbx_refine_tls.origin_z / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_1_auth_comp_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_comp_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_atom_id_1 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_close_contact.dist / _pdbx_validate_close_contact.label_alt_id_1 / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_number_reflns_R_free / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_overall_phase_error / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_protein / _refine_ls_shell.R_factor_R_free / _refine_ls_shell.R_factor_R_work / _reflns.number_obs / _reflns.pdbx_number_measured_all / _reflns.pdbx_redundancy / _struct_conf.end_auth_comp_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_comp_id / _struct_conf.end_label_seq_id / _struct_conf.pdbx_PDB_helix_length / _struct_conn.pdbx_dist_value / _struct_conn.ptnr2_auth_seq_id / _struct_mon_prot_cis.pdbx_omega_angle
Revision 2.1May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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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)265,25922
Polymers261,6316
Non-polymers3,62716
Water5,044280
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.539, 156.717, 181.697
Angle α, β, γ (deg.)90.000, 90.000, 90.000
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 / 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, 296 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.: 5 / 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-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
#9: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#10: Chemical ChemComp-IMD / IMIDAZOLE / Imidazole


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#11: Chemical ChemComp-5IX / (1S,2R,3S,5S,6S,16E,18E,20R,21S)-11-chloro-21-hydroxy-12,20-dimethoxy-2,5,9,16-tetramethyl-8,23-dioxo-4,24-dioxa-9,22-diazatetracyclo[19.3.1.1~10,14~.0~3,5~]hexacosa-10(26),11,13,16,18-pentaen-6-yl phenylacetate


Mass: 683.188 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C36H43ClN2O9 / Feature type: SUBJECT OF INVESTIGATION
#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.: 280 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY

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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: 56.6 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 3% PEG 4K, 4% glycerol, 30 mM MgCl2, 30 mM CaCl2, 0.1 M MES/Imidazole, 5 mM L-tyrosine

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Dec 16, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.5→47.92 Å / Num. obs: 103685 / % possible obs: 100 % / Redundancy: 13.636 % / Biso Wilson estimate: 51.58 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.212 / Rrim(I) all: 0.22 / Χ2: 0.772 / Net I/σ(I): 11.52 / Num. measured all: 1413808 / Scaling rejects: 179
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.5-2.5614.1112.4121.14106902757975760.4692.503100
2.56-2.6413.9711.921.46103207739173870.5651.99399.9
2.64-2.7113.8491.731.6499508718671850.6251.796100
2.71-2.813.6411.3962.0595516700370020.721.45100
2.8-2.8912.9151.0572.6487664678967880.8041.101100
2.89-2.9912.990.8743.2485316657065680.8640.91100
2.99-3.114.0290.6654.4888815633263310.9220.69100
3.1-3.2313.7120.5195.6983810611261120.950.539100
3.23-3.3712.910.397.2576089589458940.9690.406100
3.37-3.5413.6750.27810.1876662560656060.9850.289100
3.54-3.7314.2720.21313.4176527536253620.9910.221100
3.73-3.9514.1510.15117.7971833507650760.9960.157100
3.95-4.2313.9640.11921.3466833478647860.9970.124100
4.23-4.5613.720.09126.2760998444644460.9980.095100
4.56-513.2860.07928.9354886413141310.9980.082100
5-5.5912.4690.08925.8746710374637460.9980.092100
5.59-6.4613.6160.09226.1345028330733070.9980.096100
6.46-7.9112.8360.06932.5836673285728570.9990.072100
7.91-11.1814.1330.04747.6431446222522250.9990.049100
11.18-47.9212.4480.04349.1316020130812870.9980.04498.4

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Processing

Software
NameVersionClassificationNB
PHENIX1.19.1_4122refinement
XSCALEdata scaling
PDB_EXTRACT3.28data extraction
XDSdata reduction
PHENIX1.19.1_4122phasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 5LXT

5lxt


Resolution: 2.5→47.92 Å / SU ML: 0.37 / Cross valid method: THROUGHOUT / σ(F): 1.21 / Phase error: 24.82 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2282 5184 5 %
Rwork0.1942 98501 -
obs0.1959 103685 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 190.99 Å2 / Biso mean: 64.3556 Å2 / Biso min: 30.45 Å2
Refinement stepCycle: final / Resolution: 2.5→47.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17048 0 229 280 17557
Biso mean--67.61 54.38 -
Num. residues----2153
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.5-2.530.35843320.341862916623
2.53-2.560.3763350.324963306665
2.56-2.590.3663380.309863176655
2.59-2.620.323370.309563176654
2.62-2.660.32233280.294662626590
2.66-2.690.33593370.298463826719
2.69-2.730.33193300.297462636593
2.73-2.770.35593330.293462876620
2.77-2.820.3193320.291563746706
2.82-2.860.33723340.28562636597
2.86-2.910.31033330.285163416674
2.91-2.960.33233320.270962966628
2.96-3.020.27543340.245262926626
3.02-3.080.26083340.234664216755
3.08-3.150.26143240.222862826606
3.15-3.220.25933340.229262616595
3.22-3.30.25163380.214663506688
3.3-3.390.26743330.218963056638
3.39-3.490.25243320.208763766708
3.49-3.610.24263260.186662676593
3.61-3.730.22693280.175263756703
3.73-3.880.21743230.159662846607
3.88-4.060.17893330.153862976630
4.06-4.270.17163310.146963166647
4.27-4.540.15663390.131463386677
4.54-4.890.1513250.127663086633
4.89-5.380.1743350.153363126647
5.38-6.160.2033250.179463326657
6.16-7.760.23233300.17963036633
7.76-47.920.17633370.158363016638
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)
10.8026-0.5452-0.41170.52840.09940.5790.01990.18690.2977-0.58850.1484-0.2261-0.93190.323600.9375-0.16540.12680.5802-0.12960.611828.491798.620854.8502
20.0843-0.1597-0.0180.1793-0.01470.1208-0.25630.10120.0613-0.87240.32910.357-0.9685-0.0039-0.00021.0068-0.16250.08950.5939-0.09420.612327.031489.309243.7737
30.6423-0.32920.55190.83680.2350.76360.00580.30510.085-0.3380.4366-0.4345-0.52620.68510.00010.5788-0.14140.12340.7342-0.25170.690337.183280.681950.5193
40.5268-0.6438-0.53611.27580.15480.75020.1153-0.2454-0.08760.32360.1109-0.24320.15080.411900.47140.00850.01980.6211-0.16770.582229.646473.482258.6812
50.8947-0.5106-0.0382.65490.22112.44680.0792-0.0358-0.03780.21420.0723-0.0575-0.23870.050600.49220.02120.05770.4823-0.12430.523121.240283.905864.8568
60.98750.592-0.32311.17750.8841.3010.1406-0.08730.11770.3521-0.12410.4294-0.3769-0.5216-0.00010.64040.05790.15080.5792-0.10810.61399.048784.13671.7964
70.4357-0.17890.07042.33041.472.5751-0.0222-0.1146-0.03480.59810.15320.03820.15770.2282-00.523-0.00170.02010.4864-0.09130.527322.903876.466769.8917
81.835-0.8507-0.20791.0654-0.35730.85460.05540.23630.3675-0.5146-0.05720.116-0.6739-0.205600.65830.07370.01560.5039-0.03330.631115.98969.646919.0854
91.49940.0963-0.29452.38671.38373.0515-0.00910.12320.088-0.0862-0.01520.0649-0.13180.0389-0.00910.33330.02140.0030.4528-0.07380.479120.449153.930723.4322
100.4898-0.1381-0.55571.1412-0.00251.94570.10090.18350.1086-0.2549-0.10770.1134-0.1663-0.385100.4920.0508-0.02030.5286-0.17820.545310.93362.381737.8867
110.2709-0.14760.11231.41211.45042.5407-0.1108-0.14860.0120.4429-0.10650.17340.2783-0.3675-0.00190.4203-0.0020.0480.5709-0.07750.545513.646150.380738.491
121.1294-0.29940.16122.37380.38581.8164-0.05250.1940.0953-0.28610.0806-0.0907-0.20840.136600.3965-0.07750.0560.4703-0.02230.453720.219932.699-11.9335
130.8336-0.5002-0.03141.52181.00771.7762-0.0444-0.05350.05090.0484-0.04970.10080.078-0.1945-00.3488-0.07680.0320.4003-0.02530.45597.598225.77663.044
141.91840.26730.66971.0234-0.14591.9132-0.25450.58140.073-0.55640.2342-0.04490.0412-0.07830.00010.8901-0.14970.10010.9816-0.11140.514220.09546.0736-44.11
151.6276-0.0684-0.14491.81-0.07462.316-0.22730.3765-0.2969-0.52690.199-0.20680.43260.027900.7958-0.06340.10680.7093-0.20870.572722.702-4.462-35.1336
161.2971-0.3893-0.67691.49660.58272.5017-0.20120.3397-0.2427-0.13680.09140.15620.3798-0.34750.00160.6306-0.11210.01210.6365-0.12410.53919.7722-1.8591-21.9179
171.0060.37260.17871.2006-0.38070.373-0.59550.0638-0.94310.14670.0562-0.00030.93990.4588-0.02810.96230.04310.16190.6703-0.21630.802630.2389-16.814-23.7969
180.797-0.2153-0.15080.32860.24650.1347-0.12720.06850.04950.6820.161-0.36480.11350.5141-0.01721.0859-0.0252-0.07740.8238-0.15120.677628.794690.799781.9945
190.2695-0.4268-0.84530.02420.29830.89170.0077-0.0384-0.02990.61310.3253-0.4580.83480.41130.00440.58460.119-0.01380.8396-0.24750.762142.614428.29315.1129
201.18340.2216-1.17990.52660.17191.1936-0.36810.3734-0.3831-0.10540.0873-0.07810.852-0.4151-00.951-0.07850.08210.6362-0.11280.71586.013454.41169.7481
210.26280.11950.08610.2367-0.11190.1622-0.041-0.1969-0.16570.6115-0.0673-0.76920.11081.139500.89590.06170.00871.02980.05440.730711.278265.277897.3366
220.3868-0.2814-0.18120.70980.02630.2725-0.0142-1.1435-0.87781.262-0.321-0.81610.67191.59140.00181.29620.1949-0.08861.67810.33061.200516.515654.4385109.0437
232.25810.116-1.87540.94780.81962.1731-0.3872-0.0308-0.55880.29650.15810.13630.8141-0.0888-0.01860.95360.02060.12760.53290.04460.7322-2.946856.223791.5105
240.42670.2038-0.10840.0984-0.05510.03030.2082-0.02850.04430.03420.23820.2510.0596-0.01890.00081.46160.1753-0.09330.95950.00121.2707-6.771770.566688.3753
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 64 )A1 - 64
2X-RAY DIFFRACTION2chain 'A' and (resid 65 through 88 )A65 - 88
3X-RAY DIFFRACTION3chain 'A' and (resid 89 through 160 )A89 - 160
4X-RAY DIFFRACTION4chain 'A' and (resid 161 through 197 )A161 - 197
5X-RAY DIFFRACTION5chain 'A' and (resid 198 through 273 )A198 - 273
6X-RAY DIFFRACTION6chain 'A' and (resid 274 through 311 )A274 - 311
7X-RAY DIFFRACTION7chain 'A' and (resid 312 through 437 )A312 - 437
8X-RAY DIFFRACTION8chain 'B' and (resid 2 through 88 )B2 - 88
9X-RAY DIFFRACTION9chain 'B' and (resid 89 through 238 )B89 - 238
10X-RAY DIFFRACTION10chain 'B' and (resid 239 through 295 )B239 - 295
11X-RAY DIFFRACTION11chain 'B' and (resid 296 through 438 )B296 - 438
12X-RAY DIFFRACTION12chain 'C' and (resid 1 through 199 )C1 - 199
13X-RAY DIFFRACTION13chain 'C' and (resid 200 through 440 )C200 - 440
14X-RAY DIFFRACTION14chain 'D' and (resid 1 through 109 )D1 - 109
15X-RAY DIFFRACTION15chain 'D' and (resid 110 through 238 )D110 - 238
16X-RAY DIFFRACTION16chain 'D' and (resid 239 through 401 )D239 - 401
17X-RAY DIFFRACTION17chain 'D' and (resid 402 through 441 )D402 - 441
18X-RAY DIFFRACTION18chain 'E' and (resid 6 through 46 )E6 - 46
19X-RAY DIFFRACTION19chain 'E' and (resid 47 through 141 )E47 - 141
20X-RAY DIFFRACTION20chain 'F' and (resid 1 through 66 )F1 - 66
21X-RAY DIFFRACTION21chain 'F' and (resid 67 through 96 )F67 - 96
22X-RAY DIFFRACTION22chain 'F' and (resid 97 through 197 )F97 - 197
23X-RAY DIFFRACTION23chain 'F' and (resid 198 through 378 )F198 - 378
24X-RAY DIFFRACTION24chain 'F' and (resid 379 through 380 )F379 - 380

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