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- PDB-6gze: Tubulin-GDP.BeF complex -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6gze
TitleTubulin-GDP.BeF complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin tyrosine ligase
KeywordsCELL CYCLE / GTPase / cytoskeleton / division
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 / spindle microtubule / protein modification process / 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 / spindle microtubule / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / mitotic cell cycle / nervous system development / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / 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 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Stathmin family / Stathmin, conserved site ...Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin/FtsZ, GTPase domain / 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. / 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 / BERYLLIUM TRIFLUORIDE ION / 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 / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.49 Å
AuthorsOliva, M.A. / Diaz, J.F.
Funding support Spain, 3items
OrganizationGrant numberCountry
Spanish Ministry of Economy and CompetitivenessBFU2013-47014-P Spain
Spanish Ministry of Economy and CompetitivenessRYC-2011-07900 Spain
Spanish Ministry of Economy and CompetitivenessBFU2016-75319-R Spain
CitationJournal: Elife / Year: 2020
Title: Structural model for differential cap maturation at growing microtubule ends.
Authors: Estevez-Gallego, J. / Josa-Prado, F. / Ku, S. / Buey, R.M. / Balaguer, F.A. / Prota, A.E. / Lucena-Agell, D. / Kamma-Lorger, C. / Yagi, T. / Iwamoto, H. / Duchesne, L. / Barasoain, I. / ...Authors: Estevez-Gallego, J. / Josa-Prado, F. / Ku, S. / Buey, R.M. / Balaguer, F.A. / Prota, A.E. / Lucena-Agell, D. / Kamma-Lorger, C. / Yagi, T. / Iwamoto, H. / Duchesne, L. / Barasoain, I. / Steinmetz, M.O. / Chretien, D. / Kamimura, S. / Diaz, J.F. / Oliva, M.A.
History
DepositionJul 4, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 22, 2020Provider: repository / Type: Initial release
Revision 1.1Feb 19, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Mar 18, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.pdbx_database_id_PubMed ..._citation.journal_volume / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Jan 17, 2024Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / 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.ptnr1_symmetry / _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.ptnr3_symmetry / _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_conn.ptnr2_symmetry

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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)266,82521
Polymers263,8846
Non-polymers2,94115
Water90150
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area22120 Å2
ΔGint-137 kcal/mol
Surface area75520 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.176, 156.744, 180.587
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: 48966.324 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (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 / Source: (natural) Bos taurus (cattle) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / / Stathmin-like protein B3 / RB3


Mass: 22125.301 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: 43825.914 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, 65 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-BEF / BERYLLIUM TRIFLUORIDE ION


Mass: 66.007 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: BeF3
#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 / Water


Mass: 18.015 Da / Num. of mol.: 50 / 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: 3.11 Å3/Da / Density % sol: 60.5 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop
Details: 0.1M Mes / 0.1M Imidazole pH 6.5, 0.3M CaCl2 / 0.3M MgCl2, 5mM L-tyrosine, 5.5% glycerol, 8.8% PEG4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9724 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 15, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9724 Å / Relative weight: 1
ReflectionResolution: 2.49→49.46 Å / Num. obs: 104038 / % possible obs: 100 % / Redundancy: 7.1 % / Biso Wilson estimate: 64.7 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.071 / Rpim(I) all: 0.028 / Rrim(I) all: 0.076 / Net I/σ(I): 13.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.49-2.5371.15950990.9930.4731.253100
13.64-49.466.70.0297270.9990.0120.03298.1

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
XDSdata reduction
Aimless0.5.32data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4o2b

4o2b


Resolution: 2.49→49.458 Å / SU ML: 0.34 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 27.62
RfactorNum. reflection% reflection
Rfree0.2565 5223 5.03 %
Rwork0.2121 --
obs0.2143 103915 99.96 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 179.9 Å2 / Biso mean: 80.6096 Å2 / Biso min: 30 Å2
Refinement stepCycle: final / Resolution: 2.49→49.458 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16542 0 242 52 16836
Biso mean--72.64 67.72 -
Num. residues----2090
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00317114
X-RAY DIFFRACTIONf_angle_d0.55723208
X-RAY DIFFRACTIONf_chiral_restr0.042537
X-RAY DIFFRACTIONf_plane_restr0.0032999
X-RAY DIFFRACTIONf_dihedral_angle_d17.6810241
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
2.49-2.51830.34541650.322132283393
2.5183-2.54790.36041740.316432693443
2.5479-2.5790.33391670.296832663433
2.579-2.61160.33791750.305132733448
2.6116-2.6460.29561860.292631763362
2.646-2.68220.36731600.290932783438
2.6822-2.72060.34621810.281232493430
2.7206-2.76120.311720.279932373409
2.7612-2.80430.29111820.28532893471
2.8043-2.85030.32891530.274432753428
2.8503-2.89940.30781680.268732853453
2.8994-2.95210.29061850.272632283413
2.9521-3.00890.33231640.279432763440
3.0089-3.07030.37741780.27332963474
3.0703-3.13710.30211750.261632603435
3.1371-3.210.30281790.26532273406
3.21-3.29030.24891660.252132733439
3.2903-3.37920.32931680.250832893457
3.3792-3.47870.26531930.239333133506
3.4787-3.59090.27811730.230832473420
3.5909-3.71920.23741730.216832883461
3.7192-3.86810.22841960.202732653461
3.8681-4.0440.25471850.192532673452
4.044-4.25710.22441570.182133393496
4.2571-4.52370.22211840.162433353519
4.5237-4.87270.20831630.158233063469
4.8727-5.36250.23821560.173933643520
5.3625-6.13720.25471830.202233653548
6.1372-7.72750.28571860.20433773563
7.7275-49.46740.19621760.186135523728
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)
13.3929-0.23490.23565.84551.00923.3479-0.08770.08670.3394-0.74080.2699-0.3843-0.97890.4448-0.15540.9367-0.12560.18250.64-0.14240.572228.600898.433754.97
26.608-2.44610.79826.38324.91139.8886-0.49880.74050.1306-1.45820.27720.236-1.7044-0.19060.26421.0043-0.12350.02150.733-0.05940.645226.718889.237743.5689
32.0843-0.10780.71595.72191.02293.3461-0.01730.40470.056-0.45270.3717-0.6731-0.48720.7521-0.40410.545-0.14050.15110.8322-0.28950.6837.182480.501150.4583
43.43950.2632-0.37137.17111.13933.24570.167-0.2165-0.09960.50140.0591-0.23380.1060.6133-0.18970.59440.02850.0240.6259-0.1980.532130.135373.528359.1636
54.26430.21642.15043.76681.60945.27610.13140.0681-0.04470.1915-0.06550.0216-0.31790.03490.02690.59950.0510.09450.5218-0.09590.557819.486385.079763.1823
61.10180.41320.97355.5038-0.49243.86540.1561-0.0333-0.09010.614-0.13970.53420.2089-0.2661-0.15840.6062-0.01320.06080.5109-0.19520.568414.712682.84171.1785
70.9584-0.93320.65126.53221.7852.7242-0.1088-0.46990.15021.11630.16430.6036-0.2375-0.26080.04960.80940.09450.1490.7233-0.17160.630116.623486.599980.6545
82.09450.2601-0.06264.90462.10224.55490.1157-0.08670.03180.43050.03490.3605-0.11310.03780.00380.5887-0.05770.12230.5404-0.20220.565918.056888.174473.7715
90.9301-0.16780.01734.68132.8094.8926-0.01640.0182-0.25760.96420.2366-0.36680.81640.8477-0.34840.6060.1371-0.05860.5963-0.14530.641629.496161.655762.029
104.51-1.9282-0.675.79691.9713.25310.05190.35370.6677-0.5575-0.04660.0709-0.7292-0.0484-0.06720.55930.00970.00150.56160.02470.540520.082165.216318.0251
112.2688-0.1716-0.56213.641.50513.86910.0233-0.03610.00430.1357-0.09870.2284-0.0063-0.19780.07660.32640.01030.01790.4767-0.10970.484817.430252.781326.5359
123.7813-0.93450.23093.69390.11333.70190.0519-0.23390.5117-0.025-0.13230.2132-0.262-0.57770.09940.48540.04290.04350.6102-0.20730.58610.858562.148638.2293
133.3567-1.43771.74593.9609-0.6624.6966-0.1813-0.32360.31570.4188-0.1310.602-0.0957-0.92360.26990.52750.03090.12170.8058-0.24250.72876.603860.244744.8943
141.1558-0.0795-0.48463.26372.26243.9925-0.0896-0.2309-0.21090.6590.02070.04830.73890.3318-0.05620.4557-0.0263-0.03420.5729-0.02790.51821.374139.301532.2267
155.4789-3.2001-0.94676.39660.82774.582-0.20860.20480.5176-0.05280.08940.1412-0.60130.01850.10590.4695-0.0836-0.01540.52220.01450.452614.493342.2979-12.989
161.7426-0.96030.01514.44721.13113.7152-0.07250.4194-0.03-0.50890.2553-0.4233-0.26880.321-0.19340.4292-0.11930.09640.6227-0.04990.494524.894130.4648-14.4267
172.4168-0.86060.1682.51630.44723.1035-0.0170.11460.1039-0.00420.06180.1653-0.0239-0.1148-0.04580.3872-0.05460.02970.50410.00550.441711.414526.3306-3.4565
182.1893-1.24161.6921.9587-0.43724.42920.1409-0.1282-0.13-0.0333-0.08630.49070.3507-0.8371-0.0820.4377-0.09330.06580.5186-0.09320.52870.877126.87434.4358
195.0337-3.42673.66733.9983-1.14335.6837-0.0735-0.16240.26040.4523-0.19290.4208-0.1367-0.6510.09210.3839-0.16350.0250.4968-0.10620.5287-0.21236.073611.6339
204.4735-2.0754.24842.2662-1.04587.79560.0639-0.39670.2362-0.03230.0530.28010.1843-0.4586-0.07220.4294-0.1280.07550.4963-0.06050.60331.798333.57366.7946
211.3909-1.0055-1.03082.77211.51052.6756-0.08470.0661-0.10360.44310.0805-0.07950.51560.3202-0.02550.4705-0.0084-0.03810.4529-0.04720.513620.143713.13862.5765
224.87-1.7885-0.17163.15930.4792.2765-0.25540.8753-0.1953-0.79460.175-0.08740.1560.15490.0820.8845-0.19220.10361.0412-0.12310.497922.34846.3526-44.0933
231.9797-0.178-0.70861.04630.05062.5542-0.24110.4947-0.4607-0.23980.16710.02590.5489-0.22010.03610.7316-0.13950.04460.6957-0.23170.566914.4046-3.0371-27.2787
245.1298-2.069-5.13242.8511.92867.6053-0.1680.2988-1.0454-0.0219-0.0924-0.04191.28220.34790.08011.11590.08770.03120.7646-0.29350.867330.8088-17.6017-25.2691
252.3314-1.6236-0.01521.89672.03924.63-0.3013-0.2260.53550.2340.4493-0.7927-0.11430.3344-0.13860.8759-0.1973-0.00940.9234-0.3020.901327.95592.769680.7274
260.3027-0.6982-0.92234.18114.39584.9415-0.1893-0.09470.00060.43470.3906-0.12190.56560.7615-0.30070.54940.02820.05120.8371-0.19910.731542.826129.4816.0533
277.27394.0259-3.96895.39330.21416.5179-0.6611.0717-2.17450.5485-0.0131-0.49161.7272-0.63980.65341.3361-0.15730.21680.6018-0.2710.97942.33948.681171.8622
286.7743-0.3921-2.68313.2088-2.29289.1056-0.250.2635-0.376-0.17830.2595-0.15980.8214-0.2118-0.02160.7164-0.040.12290.5273-0.17020.6368.100856.85668.9727
299.2349-0.32184.0996.0207-3.92864.19630.569-0.3711-0.92620.72650.0075-0.94670.16261.195-0.480.96660.1252-0.06610.99550.06550.708813.699263.161993.6021
308.03190.94823.53396.02433.79276.028-0.1205-0.9217-0.74821.5964-0.32440.12940.03231.38740.45161.00830.2254-0.07521.23740.10380.663710.954762.3381104.9805
312.3577-3.26020.13994.54210.3985.9064-0.4186-0.7732-1.27440.5276-0.547-0.28782.67140.99250.72391.62840.30310.29820.92660.54691.4289-0.854646.7136110.1409
325.7923.4193-5.01274.385-0.14387.6834-0.34640.2551-0.6506-0.8881-0.2571-1.08290.5235-0.38170.58970.77420.04360.17880.5729-0.02910.9274-2.586459.100686.6702
332.398-2.58681.22956.3909-5.88716.4138-0.30750.2283-1.3229-0.223-0.14520.22021.6837-0.23570.17081.4549-0.0060.31630.63790.16581.2002-7.68246.0188100.9626
346.68670.0564-4.73972.2543-0.29823.52980.03930.10360.33620.18220.78010.4267-0.273-0.4291-1.02711.14640.07440.19970.76070.14850.8516-5.884561.716299.0832
355.67981.1009-7.16611.9517-2.3239.1912-0.4608-0.5222-0.64090.27830.1596-0.36650.33240.42420.11230.88560.1118-0.00380.65890.04360.71053.612761.4990.6743
364.18832.5797-3.86876.8401-3.92816.477-0.31380.1684-1.2723-0.17170.82490.78561.9495-0.6301-0.15571.3035-0.31720.21260.7282-0.19261.0647-4.365549.510482.1853
379.2137-0.2611-6.24883.239-1.5418.6332-0.04870.55090.0927-0.15890.7021-0.10330.0841-0.2551-0.45360.8696-0.05620.18940.8037-0.00090.9386-7.784761.692679.1096
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 199 )A161 - 199
5X-RAY DIFFRACTION5chain 'A' and (resid 200 through 259 )A200 - 259
6X-RAY DIFFRACTION6chain 'A' and (resid 260 through 306 )A260 - 306
7X-RAY DIFFRACTION7chain 'A' and (resid 307 through 338 )A307 - 338
8X-RAY DIFFRACTION8chain 'A' and (resid 339 through 381 )A339 - 381
9X-RAY DIFFRACTION9chain 'A' and (resid 382 through 437 )A382 - 437
10X-RAY DIFFRACTION10chain 'B' and (resid 1 through 127 )B1 - 127
11X-RAY DIFFRACTION11chain 'B' and (resid 128 through 238 )B128 - 238
12X-RAY DIFFRACTION12chain 'B' and (resid 239 through 295 )B239 - 295
13X-RAY DIFFRACTION13chain 'B' and (resid 296 through 373 )B296 - 373
14X-RAY DIFFRACTION14chain 'B' and (resid 374 through 438 )B374 - 438
15X-RAY DIFFRACTION15chain 'C' and (resid 1 through 72 )C1 - 72
16X-RAY DIFFRACTION16chain 'C' and (resid 73 through 161 )C73 - 161
17X-RAY DIFFRACTION17chain 'C' and (resid 162 through 259 )C162 - 259
18X-RAY DIFFRACTION18chain 'C' and (resid 260 through 311 )C260 - 311
19X-RAY DIFFRACTION19chain 'C' and (resid 312 through 336 )C312 - 336
20X-RAY DIFFRACTION20chain 'C' and (resid 337 through 372 )C337 - 372
21X-RAY DIFFRACTION21chain 'C' and (resid 373 through 440 )C373 - 440
22X-RAY DIFFRACTION22chain 'D' and (resid 1 through 127 )D1 - 127
23X-RAY DIFFRACTION23chain 'D' and (resid 128 through 399 )D128 - 399
24X-RAY DIFFRACTION24chain 'D' and (resid 400 through 440 )D400 - 440
25X-RAY DIFFRACTION25chain 'E' and (resid 8 through 46 )E8 - 46
26X-RAY DIFFRACTION26chain 'E' and (resid 47 through 139 )E47 - 139
27X-RAY DIFFRACTION27chain 'F' and (resid 1 through 22 )F1 - 22
28X-RAY DIFFRACTION28chain 'F' and (resid 23 through 66 )F23 - 66
29X-RAY DIFFRACTION29chain 'F' and (resid 67 through 83 )F67 - 83
30X-RAY DIFFRACTION30chain 'F' and (resid 84 through 185 )F84 - 185
31X-RAY DIFFRACTION31chain 'F' and (resid 186 through 199 )F186 - 199
32X-RAY DIFFRACTION32chain 'F' and (resid 200 through 216 )F200 - 216
33X-RAY DIFFRACTION33chain 'F' and (resid 217 through 274 )F217 - 274
34X-RAY DIFFRACTION34chain 'F' and (resid 275 through 297 )F275 - 297
35X-RAY DIFFRACTION35chain 'F' and (resid 298 through 333 )F298 - 333
36X-RAY DIFFRACTION36chain 'F' and (resid 334 through 354 )F334 - 354
37X-RAY DIFFRACTION37chain 'F' and (resid 355 through 380 )F355 - 380

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