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- PDB-4i55: Crystal structure of tubulin-stathmin-TTL complex -

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Basic information

Entry
Database: PDB / ID: 4i55
TitleCrystal structure of tubulin-stathmin-TTL complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin tyrosine ligase, TTL
KeywordsCELL CYCLE / alpha-tubulin / beta-tubulin / ligase / microtubule / stathmin
Function / homology
Function and homology information


tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement ...tubulin-tyrosine ligase activity / positive regulation of axon guidance / microtubule depolymerization / regulation of microtubule polymerization or depolymerization / cytoplasmic microtubule / microtubule-based process / cellular response to interleukin-4 / tubulin binding / spindle microtubule / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / protein modification process / structural constituent of cytoskeleton / microtubule cytoskeleton organization / neuron projection development / microtubule cytoskeleton / double-stranded RNA binding / mitotic cell cycle / nervous system development / growth cone / microtubule / neuron projection / protein heterodimerization activity / nucleotide binding / GTPase activity / ubiquitin protein ligase binding / GTP binding / Golgi apparatus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / Stathmin family ...Rossmann fold - #11480 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 - #30 / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Helix hairpin bin / Tubulin/FtsZ, C-terminal domain / Tubulin-tyrosine ligase/Tubulin polyglutamylase / Tubulin-tyrosine ligase family / TTL domain profile. / Tubulin/FtsZ, GTPase domain / 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 / ATP-grasp fold, B domain / D-amino Acid Aminotransferase; Chain A, domain 1 / 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 / Dna Ligase; domain 1 / 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 / 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 / Resolution: 2.2 Å
AuthorsProta, A.E. / Bargsten, K. / Zurwerra, D. / Field, J.J. / Diaz, J.F. / Altmann, K.H. / Steinmetz, M.O.
CitationJournal: Science / Year: 2013
Title: Molecular Mechanism of Action of Microtubule-Stabilizing Anticancer Agents.
Authors: Prota, A.E. / Bargsten, K. / Zurwerra, D. / Field, J.J. / Diaz, J.F. / Altmann, K.H. / Steinmetz, M.O.
History
DepositionNov 28, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 23, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 13, 2013Group: Database references
Revision 1.2Nov 15, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.3Sep 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, TTL
hetero molecules


Theoretical massNumber of molelcules
Total (without water)264,49925
Polymers261,3056
Non-polymers3,19419
Water13,781765
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.160, 156.470, 181.490
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: 50041.273 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) / Strain (production host): NiCo21 (DE3) / References: UniProt: P63043
#4: Protein Tubulin tyrosine ligase, TTL


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: PA23_007_ggTTL_KH6_2-378_NSKn1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 (DE3) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 784 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.: 7 / Source method: obtained synthetically / Formula: Mg
#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#9: 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
#10: Chemical ChemComp-MES / 2-(N-MORPHOLINO)-ETHANESULFONIC ACID / MES (buffer)


Mass: 195.237 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C6H13NO4S / Comment: pH buffer*YM
#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.: 765 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsBRAIN TUBULIN PREPARATIONS CONTAIN THREE TUBULIN SUBPOPULATIONS: TYROSINATED (20-30%), DE- ...BRAIN TUBULIN PREPARATIONS CONTAIN THREE TUBULIN SUBPOPULATIONS: TYROSINATED (20-30%), DE-TYROSINATED (30-40%) AND DELTA-2 TUBULIN (ABOUT 40%) (LACKING THE CARBOXYTERMINAL GLUTAMYL-TYROSINE). TUBULIN-TYROSINE LIGASE BINDS ALL THREE VARIANTS, BUT ONLY CAN MODIFY DE-TYROSINATED TUBULIN. ALTHOUGH ALL SUBPOPULATIONS ARE PRESENT IN THE CRYSTAL, ONLY THE DE-TYROSINATED FORM WAS MODELED WITH A TERMINAL CARBOXYLATE TO DESCRIBE THE LIGASE REACTION. IN THE SEQRES RECORD FOR CHAIN A THE TERMINAL TYR WAS OMITTED TO MATCH THE MODELED VARIANT OF ALPHA-TUBULIN.

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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: 2.83 Å3/Da / Density % sol: 56.48 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.7
Details: 3% PEG 4000, 4-6% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 100 mM MES/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: X06SA / Wavelength: 0.99995 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 3, 2012
RadiationMonochromator: LN2 cooled fixed-exit Si(111) monochromator, Sagittally - horizontally focussed
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99995 Å / Relative weight: 1
ReflectionResolution: 2.2→71.844 Å / Num. all: 149411 / Num. obs: 149411 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 13.2 % / Biso Wilson estimate: 45.7 Å2 / Rmerge(I) obs: 0.094 / Net I/σ(I): 16.2
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 11.9 % / Mean I/σ(I) obs: 2.2 / Num. unique all: 10355 / % possible all: 93.9

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Processing

Software
NameVersionClassification
RemDAqdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3RYC, 3TIN

3ryc

3tin


Resolution: 2.2→71.844 Å / SU ML: 0.33 / Phase error: 20.81 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2077 7514 5.03 %RANDOM
Rwork0.1675 ---
all0.1695 149390 --
obs0.1695 149390 99.23 %-
Solvent computationShrinkage radii: 0.98 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 47.152 Å2 / ksol: 0.337 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-6.9646 Å20 Å2-0 Å2
2--7.1804 Å2-0 Å2
3----0.397 Å2
Refinement stepCycle: LAST / Resolution: 2.2→71.844 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17470 0 187 765 18422
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00818285
X-RAY DIFFRACTIONf_angle_d1.11124845
X-RAY DIFFRACTIONf_dihedral_angle_d16.5656864
X-RAY DIFFRACTIONf_chiral_restr0.0632708
X-RAY DIFFRACTIONf_plane_restr0.0053229
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2-2.2250.28472270.25234223X-RAY DIFFRACTION90
2.225-2.25120.32092390.24774573X-RAY DIFFRACTION97
2.2512-2.27860.3072400.2444669X-RAY DIFFRACTION99
2.2786-2.30750.26612720.23094673X-RAY DIFFRACTION99
2.3075-2.33790.26392480.21794664X-RAY DIFFRACTION99
2.3379-2.36990.26782590.21224695X-RAY DIFFRACTION99
2.3699-2.40370.26842510.20894704X-RAY DIFFRACTION100
2.4037-2.43960.27422560.21174706X-RAY DIFFRACTION99
2.4396-2.47770.27482530.19944674X-RAY DIFFRACTION99
2.4777-2.51840.27662420.20454707X-RAY DIFFRACTION100
2.5184-2.56180.28992530.20954680X-RAY DIFFRACTION99
2.5618-2.60840.25122520.19764740X-RAY DIFFRACTION99
2.6084-2.65860.23152310.19364713X-RAY DIFFRACTION100
2.6586-2.71280.24542420.19444695X-RAY DIFFRACTION99
2.7128-2.77180.23992830.18614673X-RAY DIFFRACTION100
2.7718-2.83630.24562570.17954748X-RAY DIFFRACTION100
2.8363-2.90720.22362170.17794758X-RAY DIFFRACTION100
2.9072-2.98580.23092350.16874769X-RAY DIFFRACTION100
2.9858-3.07370.2042450.16474767X-RAY DIFFRACTION100
3.0737-3.17290.21772450.17294739X-RAY DIFFRACTION100
3.1729-3.28630.23942250.17794768X-RAY DIFFRACTION100
3.2863-3.41790.22292850.17434728X-RAY DIFFRACTION100
3.4179-3.57340.21892600.16344779X-RAY DIFFRACTION100
3.5734-3.76180.16942500.1584766X-RAY DIFFRACTION100
3.7618-3.99750.19352490.14994809X-RAY DIFFRACTION100
3.9975-4.30610.17592480.1324801X-RAY DIFFRACTION100
4.3061-4.73940.14552510.11924852X-RAY DIFFRACTION100
4.7394-5.4250.1542730.12994812X-RAY DIFFRACTION100
5.425-6.8340.21762420.17534918X-RAY DIFFRACTION100
6.834-71.88240.19692840.18195073X-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)
11.0822-0.3131-0.08132.15420.69651.3336-0.03910.08560.0643-0.320.2554-0.2756-0.4910.3546-0.13640.4231-0.13260.09380.3462-0.12260.29831.670987.560552.1532
20.2241-0.2439-0.08731.54590.96642.05140.04590.01420.00860.19050.00460.1083-0.1344-0.0407-0.04070.33170.0140.03890.33-0.08090.347319.058581.480466.1553
30.7108-0.0995-0.01311.71760.88491.1106-0.0047-0.08990.06590.3657-0.03710.18170.00160.0024-0.02480.3350.0110.05250.1986-0.08610.20718.626582.485273.6142
40.7326-0.1801-0.28561.6041.36522.65-0.152-0.0445-0.21260.62980.2159-0.30860.45530.7296-0.01510.36880.1288-0.07370.3193-0.14120.355132.56461.123260.8133
50.0094-0.0022-0.013600.00310.01980.431-0.4206-0.24310.4077-0.4262-0.5629-0.03430.05480.07921.3451-0.06410.14810.78190.09480.662417.058156.146186.7654
61.6852-1.0752-0.28062.34980.36481.67470.10090.1630.3296-0.3559-0.1091-0.0305-0.5155-0.14070.01790.33070.04270.01470.2959-0.03050.354716.306869.587919.6941
71.2846-0.1294-0.34781.7594-0.11341.1890.02780.2562-0.0079-0.33990.1443-0.1469-0.26520.2345-0.12360.275-0.03650.03740.4372-0.04070.296629.085455.762814.6906
81.06780.4646-0.09181.95850.62921.33720.0694-0.0299-0.04840.02780.0747-0.2133-0.11220.131-0.11520.1863-0.0080.04340.2809-0.10350.304624.451352.825126.2646
92.0665-0.55360.63730.3749-0.49960.6988-0.23270.0464-0.36820.1993-0.31670.52580.2514-0.78090.04280.0981-0.12470.14320.6761-0.37730.58255.300450.460528.2336
100.4759-0.2316-0.54670.99280.63211.26020.00150.08210.0363-0.0546-0.03310.1348-0.2795-0.29530.0010.26050.032-0.00090.3767-0.11980.39199.798161.217935.4108
111.5915-0.23850.32891.25330.28341.5555-0.1503-0.22940.10590.3283-0.09750.32150.0288-0.77760.16820.25450.02790.04440.4635-0.16210.31696.437860.311144.9223
120.8011-0.9263-0.28081.87761.38071.3533-0.0633-0.2807-0.1040.2209-0.04420.51090.2453-0.10480.07160.3031-0.01030.04980.3349-0.09070.330515.246941.629734.1359
130.3526-0.0379-0.10731.45281.32073.444-0.0683-0.1215-0.21380.37180.0205-0.03410.29460.46460.05020.26340.0052-0.03450.29-0.03160.319225.522837.740631.4652
141.0109-0.22270.01311.90770.27751.026-0.05170.06350.1159-0.18330.0685-0.0958-0.09180.105-0.01130.1914-0.05280.03480.2637-0.01560.239220.353332.5947-12.0666
150.824-0.3683-0.11271.17190.75911.3603-0.0091-0.00090.09540.0673-0.06660.07620.07-0.17280.04980.1871-0.04560.03030.2509-0.03940.25777.79125.58392.9992
162.5081-0.70620.17861.80160.27431.7696-0.13720.82950.1203-0.69960.12080.07760.0739-0.1403-0.0060.5865-0.08380.03380.6371-0.0290.237417.35059.1127-44.2633
170.9549-0.3016-0.2381.34490.3031.3118-0.12140.3565-0.1718-0.34320.0867-0.08930.3158-0.04560.0150.4961-0.06140.08720.4395-0.16960.292521.0696-2.687-33.6387
181.22580.0831-0.46680.79240.17581.5586-0.2230.3056-0.2372-0.12880.12270.01680.3668-0.1820.12310.4395-0.09480.04670.3675-0.13450.31168.9761-4.2832-21.3238
192.0879-0.3275-1.33261.00760.33492.1977-0.0357-0.017-0.4330.02230.1236-0.19920.28890.2344-0.19720.69280.04310.11590.4093-0.20420.537630.3901-16.9014-24.1898
201.7707-0.2889-0.94890.62460.43552.1543-0.174-0.0792-0.02880.61580.1494-0.21150.30340.7295-0.05680.7014-0.0137-0.05060.505-0.15710.448227.496591.241982.8936
210.3556-0.0506-0.09980.54850.68640.738-0.1425-0.08450.01480.17610.4708-0.4060.41190.7801-0.14680.3470.06250.06030.5751-0.21040.464442.952226.73333.561
221.3520.6324-0.63622.0464-0.34690.862-0.31110.3421-0.1459-0.0864-0.0256-0.15030.9318-0.2050.10710.7795-0.09940.15370.3934-0.15370.3756.038853.870370.09
230.4193-0.15160.18530.9346-0.27981.5253-0.2008-0.6923-0.55440.4527-0.1431-0.56880.44391.5030.22220.64430.2351-0.07561.02440.34130.548215.947156.9867105.3962
241.77940.2161-1.540.7602-0.13722.3729-0.4596-0.1124-0.5530.31530.2087-0.07150.6212-0.0813-0.02790.63440.05860.17150.17670.06060.3793-1.875353.403294.1484
252.50554.18064.73827.35358.43749.707-0.17150.06380.05990.4961-0.44390.9517-0.0993-0.34740.60750.48770.07440.10050.7397-0.23940.663131.807559.273736.1985
262.06772.07652.182.08582.19012.2995-0.16330.22970.4276-0.3557-0.2011.2292-0.97911.06330.3560.8068-0.42820.13861.2721-0.22090.64912.426651.118245.7007
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 1:180)
2X-RAY DIFFRACTION2chain 'A' and (resseq 181:311)
3X-RAY DIFFRACTION3chain 'A' and (resseq 312:401)
4X-RAY DIFFRACTION4chain 'A' and (resseq 402:436)
5X-RAY DIFFRACTION5chain 'A' and (resseq 437:450)
6X-RAY DIFFRACTION6chain 'B' and (resseq 1:88)
7X-RAY DIFFRACTION7chain 'B' and (resseq 89:127)
8X-RAY DIFFRACTION8chain 'B' and (resseq 128:197)
9X-RAY DIFFRACTION9chain 'B' and (resseq 198:223)
10X-RAY DIFFRACTION10chain 'B' and (resseq 224:295)
11X-RAY DIFFRACTION11chain 'B' and (resseq 296:373)
12X-RAY DIFFRACTION12chain 'B' and (resseq 374:401)
13X-RAY DIFFRACTION13chain 'B' and (resseq 402:438)
14X-RAY DIFFRACTION14chain 'C' and (resseq 1:197)
15X-RAY DIFFRACTION15chain 'C' and (resseq 198:440)
16X-RAY DIFFRACTION16chain 'D' and (resseq 2:88)
17X-RAY DIFFRACTION17chain 'D' and (resseq 89:295)
18X-RAY DIFFRACTION18chain 'D' and (resseq 296:401)
19X-RAY DIFFRACTION19chain 'D' and (resseq 402:441)
20X-RAY DIFFRACTION20chain 'E' and (resseq 6:46)
21X-RAY DIFFRACTION21chain 'E' and (resseq 47:144)
22X-RAY DIFFRACTION22chain 'F' and (resseq 1:66)
23X-RAY DIFFRACTION23chain 'F' and (resseq 67:198)
24X-RAY DIFFRACTION24chain 'F' and (resseq 199:384)
25X-RAY DIFFRACTION25chain 'B' and (resseq 504:504)
26X-RAY DIFFRACTION26chain 'B' and (resseq 505:505)

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