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- PDB-4yj2: Crystal structure of tubulin bound to MI-181 -

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Basic information

Entry
Database: PDB / ID: 4yj2
TitleCrystal structure of tubulin bound to MI-181
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligase
KeywordsCELL CYCLE / alpha-tubulin / beta-tubulin / stathmin / MI-181 / cell cycle inhibitor complex / microtubule / cytoskeleton
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. / 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-4ED / 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 (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.6 Å
AuthorsMcNamara, D.E. / Torres, J.Z. / Yeates, T.O.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Center for Advancing Translational Sciences (NIH/NCATS)UL1TR000124 United States
CitationJournal: Protein Sci. / Year: 2015
Title: Structures of potent anticancer compounds bound to tubulin.
Authors: McNamara, D.E. / Senese, S. / Yeates, T.O. / Torres, J.Z.
History
DepositionMar 3, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 27, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 1, 2015Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Database references ...Author supporting evidence / Database references / Derived calculations / Source and taxonomy
Category: citation / entity_src_gen ...citation / entity_src_gen / entity_src_nat / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag ..._citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _entity_src_nat.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 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
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)265,27327
Polymers261,6706
Non-polymers3,60321
Water2,000111
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23740 Å2
ΔGint-120 kcal/mol
Surface area77590 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.830, 157.650, 181.030
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
DetailsThe tubulin-stathmin-TTL biological assembly contains chains A, B, C, D, E, and F

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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: 16883.197 Da / Num. of mol.: 1 / Fragment: Stathmin-like domain / Mutation: F64W
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Stmn4 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / 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 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: E1BQ43

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Non-polymers , 9 types, 132 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.: 3 / Source method: obtained synthetically / Formula: Ca
#8: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 5 / 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-4ED / 5,6-dimethyl-2-[(E)-2-(pyridin-3-yl)ethenyl]-1,3-benzothiazole


Mass: 266.361 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H14N2S
#11: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#12: Chemical ChemComp-IMD / IMIDAZOLE


Mass: 69.085 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H5N2
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 111 / 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: 2.86 Å3/Da / Density % sol: 56.97 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 100 mM MES/imidazole, 30 mM CaCl2, 30 mM MgCl2, 6% (w/v) PEG 4000, 7% glycerol CRYO Paratone-N oil

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 16, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.6→90.72 Å / Num. obs: 92610 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 6.7 % / Biso Wilson estimate: 62.87 Å2 / Rmerge F obs: 0.999 / Rmerge(I) obs: 0.076 / Rrim(I) all: 0.082 / Χ2: 0.973 / Net I/σ(I): 17.79
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.6-2.670.621.1081.6443170683367711.20599.1
2.67-2.740.7340.9212.1145058656665320.99599.5
2.74-2.820.8370.7212.7144798648464810.779100
2.82-2.910.8850.5583.5742852624162350.60399.9
2.91-30.9240.4354.5140776606860620.47299.9
3-3.110.9520.3155.9236940587158620.34399.8
3.11-3.220.9750.2378.1640083568356800.25699.9
3.22-3.360.9860.18110.538186548054780.195100
3.36-3.510.9920.13114.0435956525352500.14299.9
3.51-3.680.9950.10217.7233511500849970.1199.8
3.68-3.880.9970.07522.1430184480447880.08299.7
3.88-4.110.9980.0628.2331647453245270.06599.9
4.11-4.390.9990.04933.3529511428442830.053100
4.39-4.750.9990.0439.2626693399439910.04399.9
4.75-5.20.9990.03938.6123232367336570.04299.6
5.2-5.810.9990.03939.8623480337733760.042100
5.81-6.710.9990.03740.7219947296629620.0499.9
6.71-8.220.9990.02949.6415909254525210.03199.1
8.22-11.630.9990.02463.6113220200120010.026100

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation8.48 Å90.72 Å
Translation8.48 Å90.72 Å

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Processing

Software
NameVersionClassification
PHENIXrefinement
XSCALEJanuary 10, 2014data scaling
PHASER2.5.6phasing
PDB_EXTRACT3.15data extraction
XDSJanuary 10, 2014data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4O2B

4o2b


Resolution: 2.6→90.718 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 24.92 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2311 9261 10 %RANDOM
Rwork0.1882 83334 --
obs0.1925 92595 99.74 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 189.59 Å2 / Biso mean: 76.1453 Å2 / Biso min: 29.72 Å2
Refinement stepCycle: final / Resolution: 2.6→90.718 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16908 0 224 111 17243
Biso mean--67.81 53.91 -
Num. residues----2137
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00317637
X-RAY DIFFRACTIONf_angle_d0.55123853
X-RAY DIFFRACTIONf_chiral_restr0.0232595
X-RAY DIFFRACTIONf_plane_restr0.0033088
X-RAY DIFFRACTIONf_dihedral_angle_d11.5186513
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.6-2.62950.33933020.31162723302598
2.6295-2.66040.33373040.289227303034100
2.6604-2.69290.3383030.28072732303599
2.6929-2.7270.32223050.268827463051100
2.727-2.76290.32143060.271827573063100
2.7629-2.80070.29853050.264427373042100
2.8007-2.84070.34513070.249427673074100
2.8407-2.88310.31893060.247327523058100
2.8831-2.92820.29493060.242627513057100
2.9282-2.97620.27483070.240627623069100
2.9762-3.02750.27833040.23727403044100
3.0275-3.08260.28013090.231427813090100
3.0826-3.14190.27763040.231827303034100
3.1419-3.2060.26763080.231427753083100
3.206-3.27570.27353100.227127883098100
3.2757-3.35190.23253030.214727313034100
3.3519-3.43570.2693090.214927853094100
3.4357-3.52860.27913080.210227693077100
3.5286-3.63250.24373080.202727733081100
3.6325-3.74970.23893100.185927913101100
3.7497-3.88370.20823060.182927513057100
3.8837-4.03920.22213110.171327973108100
4.0392-4.22310.20643080.163827693077100
4.2231-4.44570.19723110.149228023113100
4.4457-4.72420.17483100.135227953105100
4.7242-5.0890.18213110.14252793310499
5.089-5.6010.21193150.172828333148100
5.601-6.41130.23343140.180928293143100
6.4113-8.07680.19563180.1692863318199
8.0768-90.77280.20263330.16642982331599
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)
11.44260.1124-0.29635.7986-1.28612.77260.0033-0.12940.21690.4150.3830.5971-0.8071-0.5854-0.37320.64850.15790.13370.61260.1970.5169-31.588488.2198-51.872
21.87641.0571-0.48034.4961-1.3934.49450.10430.19840.2181-0.3790.0221-0.141-0.3124-0.0036-0.11270.50580.03320.0660.44620.09860.4618-19.118982.2553-65.9884
31.14790.30490.74115.986-1.53633.1452-0.20450.36660.0711-1.22240.2588-0.2422-0.00940.0226-0.04860.54930.00250.15520.55980.09680.4634-18.899583.0896-73.4226
44.02631.731-1.80556.7832-5.39822.0626-0.22680.4054-0.3202-1.06350.90840.45851.059-1.8495-0.57890.5581-0.1371-0.10450.64910.14790.61-32.664761.8437-60.4603
54.44511.60730.10772.0426-0.53491.4484-0.142-0.9352-0.7188-0.265-0.35310.3387-0.29941.07230.54770.55310.06970.11990.44690.17140.5948-23.083574.4559-54.5546
67.0432.8549-1.78084.5241-1.3286.07230.3934-0.32710.97450.6528-0.24840.1009-1.36390.3961-0.15140.6412-0.03880.03910.4047-0.01050.5014-15.81170.0978-19.1604
73.04580.9051-0.59496.0565-0.59873.29220.1377-0.5512-0.03850.52130.07180.5108-0.4952-0.3784-0.22350.45640.02810.07980.64930.09630.4796-28.770956.319-14.536
83.3407-2.44940.40439.0354-2.95564.9444-0.0370.26120.17820.02910.08610.1712-0.2322-0.3875-0.06430.2688-0.05310.03270.44380.10730.392-24.083253.3022-26.0547
99.7904-0.96331.77242.93570.92164.9243-0.00940.5947-0.23760.1479-0.1543-0.69180.32961.22670.12980.49940.01220.03960.72870.31070.5794-5.018550.926-28.2317
102.6174-0.26320.11922.4994-0.48074.3890.05310.30670.58130.0254-0.1539-0.3986-0.53120.68930.12140.4425-0.08450.03080.51250.17460.5128-10.009762.1691-35.7945
113.55381.91121.83164.00610.98854.4971-0.3450.41450.1368-0.59140.1454-0.4326-0.2640.98680.16840.4239-0.03370.07410.66290.16250.5193-6.208360.8154-44.7688
122.57885.1202-3.87899.7554-8.47457.7674-0.44610.2417-0.3915-0.8383-0.1211-1.11410.887-0.00010.53360.46040.07940.06610.52340.08140.4869-15.170642.178-34.0847
132.63621.8807-2.73267.3017-5.99072.119-0.52740.5982-0.3222-1.45060.21360.22161.5592-1.00650.30860.5692-0.0902-0.0890.589-0.03430.4814-25.498938.1552-31.0032
142.10411.11290.12584.3858-0.10372.2723-0.0087-0.31420.2010.34050.03170.1591-0.2379-0.2259-0.01180.35710.07710.03440.47120.01320.3725-20.109433.183912.125
151.12060.61490.18052.0263-1.05832.5039-0.02970.061-0.0173-0.0964-0.0848-0.27250.08720.39910.12970.28960.07650.0390.35250.03760.3571-7.664626.0459-3.0298
169.10523.1933-2.07468.72680.62764.99280.2473-1.69760.34480.83080.0505-0.13990.08260.4009-0.32570.71490.15550.05411.00410.0220.4325-16.8919.458844.1997
172.23250.2468-0.70172.008-0.30483.6317-0.0896-0.7368-0.35540.58550.08630.15470.46420.0659-0.00780.67990.05990.06230.71230.20120.4854-20.5561-1.546233.227
181.94290.7232-0.46522.9908-0.44313.8496-0.1292-0.4446-0.3790.18020.0503-0.14930.57860.42190.090.55310.1540.04070.56610.1320.461-8.8308-3.901221.1988
195.9430.4265-3.32241.06631.33534.2205-0.3374-0.3068-0.83160.07280.15280.19141.1288-0.52760.1190.8986-0.03510.07320.60780.25430.7697-30.2853-16.256623.9432
205.90195.0827-1.38558.5955-3.80572.5514-0.14340.4960.3837-0.77450.67250.78930.032-0.6103-0.5191.08580.1042-0.04560.69570.1770.5935-27.601792.5199-82.0578
210.30591.157-1.47413.4129-3.53564.5923-0.04410.0890.0272-0.28630.60410.56620.4545-0.924-0.52560.483-0.0640.0450.84720.2460.7655-42.719928.8222-4.9935
226.4394-3.7314-1.12888.9953-1.45988.0777-0.5451-0.5528-1.14550.130.20170.26462.11640.64180.41250.98580.10010.17650.64070.16380.6527-6.13454.7053-69.8233
233.8927-1.4076-1.66434.57751.61254.6935-0.00041.328-0.9165-1.1695-0.56791.27210.3003-1.56290.52861.0847-0.2012-0.10511.4118-0.2710.8746-13.817958.7209-104.7307
243.5702-0.4224-2.69381.8866-0.17745.3959-0.60420.1502-0.9117-0.24080.28520.01741.43730.11850.28621.0893-0.03580.18650.5169-0.06770.70323.043956.2556-91.8723
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:180)A1 - 180
2X-RAY DIFFRACTION2(chain A and resid 181:311)A181 - 311
3X-RAY DIFFRACTION3(chain A and resid 312:401)A312 - 401
4X-RAY DIFFRACTION4(chain A and resid 402:436)A402 - 436
5X-RAY DIFFRACTION5(chain A and resid 437:439)A437 - 439
6X-RAY DIFFRACTION6(chain B and resid 1:88)B1 - 88
7X-RAY DIFFRACTION7(chain B and resid 89:127)B89 - 127
8X-RAY DIFFRACTION8(chain B and resid 128:197)B128 - 197
9X-RAY DIFFRACTION9(chain B and resid 198:223)B198 - 223
10X-RAY DIFFRACTION10(chain B and resid 224:295)B224 - 295
11X-RAY DIFFRACTION11(chain B and resid 296:373)B296 - 373
12X-RAY DIFFRACTION12(chain B and resid 374:401)B374 - 401
13X-RAY DIFFRACTION13(chain B and resid 402:438)B402 - 438
14X-RAY DIFFRACTION14(chain C and resid 1:197)C1 - 197
15X-RAY DIFFRACTION15(chain C and resid 198:440)C198 - 440
16X-RAY DIFFRACTION16(chain D and resid 1:88)D1 - 88
17X-RAY DIFFRACTION17(chain D and resid 89:295)D89 - 295
18X-RAY DIFFRACTION18(chain D and resid 296:401)D296 - 401
19X-RAY DIFFRACTION19(chain D and resid 402:441)D402 - 441
20X-RAY DIFFRACTION20(chain E and resid 5:46)E5 - 46
21X-RAY DIFFRACTION21(chain E and resid 47:141)E47 - 141
22X-RAY DIFFRACTION22(chain F and resid 1:66)F1 - 66
23X-RAY DIFFRACTION23(chain F and resid 67:198)F67 - 198
24X-RAY DIFFRACTION24(chain F and resid 199:378)F199 - 378

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