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- PDB-4o4l: Tubulin-Peloruside A-Epothilone A complex -

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Basic information

Entry
Database: PDB / ID: 4o4l
TitleTubulin-Peloruside A-Epothilone A complex
Components
  • Stathmin-4
  • Tubulin alpha-1B chain
  • Tubulin beta-2B chain
  • Tubulin-tyrosine ligaseTubulin—tyrosine ligase
KeywordsCELL CYCLE/INHIBITOR / ALPHA-TUBULIN / BETA-TUBULIN / LIGASE / GTPASE / MICROTUBULE / STATHMIN / PELORUSIDE A / EPOTHILONE A / TUBULIN FOLD / CYTOSKELETON / CELL CYCLE-INHIBITOR complex
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
EPOTHILONE A / GUANOSINE-5'-DIPHOSPHATE / GUANOSINE-5'-TRIPHOSPHATE / Peloruside A / 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: 2.2 Å
AuthorsProta, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
CitationJournal: Angew.Chem.Int.Ed.Engl. / Year: 2014
Title: Structural basis of microtubule stabilization by laulimalide and peloruside a.
Authors: Prota, A.E. / Bargsten, K. / Northcote, P.T. / Marsh, M. / Altmann, K.H. / Miller, J.H. / Diaz, J.F. / Steinmetz, M.O.
History
DepositionDec 18, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 26, 2014Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / 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
Revision 1.2Apr 3, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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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)266,06122
Polymers261,6316
Non-polymers4,43016
Water10,106561
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)104.400, 156.330, 180.400
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 / Details: BRAIN / 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 / Details: BRAIN / Source: (natural) Bos taurus (cattle) / References: UniProt: Q6B856
#3: Protein Stathmin-4 / / Stathmin-like protein B3 / RB3


Mass: 16844.162 Da / Num. of mol.: 1 / Fragment: UNP residues 49-189
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / 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) / Production host: Escherichia coli (E. coli) / References: UniProt: E1BQ43

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Non-polymers , 8 types, 577 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.: 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-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-POU / Peloruside A / (1R,3R,4S,7S,9S,11S,13R,14R,15R)-4,11,13,14-tetrahydroxy-7-[(2Z,4R)-4-(hydroxymethyl)hex-2-en-2-yl]-3,9,15-trimethoxy-12,12-dimethyl-6,17-dioxabicyclo[11.3.1]heptadecan-5-one


Mass: 548.663 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H48O11
#10: Chemical ChemComp-EP / EPOTHILONE A


Mass: 493.656 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C26H39NO6S
#11: 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
#12: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 561 / 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: 2.81 Å3/Da / Density % sol: 56.28 %
Crystal growTemperature: 293 K / pH: 6.7
Details: 6% PEG, 16% glycerol, 30 mM magnesium chloride, 30 mM calcium chloride, 0.1M MES/0.1M 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: X10SA / Wavelength: 0.97976
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: May 2, 2013
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: 0.97976 Å / Relative weight: 1
ReflectionResolution: 2.2→59.1 Å / Num. obs: 149698 / % possible obs: 99.9 % / Observed criterion σ(I): 0 / Redundancy: 13.6 % / Rmerge(I) obs: 0.122 / Net I/σ(I): 15.9
Reflection shellResolution: 2.2→2.26 Å / Redundancy: 12.4 % / Rmerge(I) obs: 4.112 / Mean I/σ(I) obs: 0.75 / % possible all: 99

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Processing

Software
NameVersionClassification
DA+data collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
XDSdata scaling
PHENIXphasing
RefinementMethod to determine structure: DIFFERENCE FOURIER
Starting model: 404J

404j


Resolution: 2.2→59.1 Å / SU ML: 0.33 / σ(F): 1.33 / Phase error: 25.67 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.224 7515 5.02 %
Rwork0.186 --
obs0.188 149671 99.9 %
all-149869 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.2→59.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17498 0 283 561 18342
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00318560
X-RAY DIFFRACTIONf_angle_d0.83725291
X-RAY DIFFRACTIONf_dihedral_angle_d15.4317032
X-RAY DIFFRACTIONf_chiral_restr0.0582794
X-RAY DIFFRACTIONf_plane_restr0.0033279
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2001-2.22510.37462560.38854592X-RAY DIFFRACTION98
2.2251-2.25130.3742310.34254694X-RAY DIFFRACTION100
2.2513-2.27870.38472710.32554648X-RAY DIFFRACTION100
2.2787-2.30760.35432270.3164713X-RAY DIFFRACTION100
2.3076-2.33790.34662580.30764674X-RAY DIFFRACTION100
2.3379-2.370.30732270.29694772X-RAY DIFFRACTION100
2.37-2.40380.3222580.28744622X-RAY DIFFRACTION100
2.4038-2.43970.32492830.2764723X-RAY DIFFRACTION100
2.4397-2.47780.29292520.2634677X-RAY DIFFRACTION100
2.4778-2.51840.32712760.26444636X-RAY DIFFRACTION100
2.5184-2.56190.31542450.2454721X-RAY DIFFRACTION100
2.5619-2.60850.26392520.22924749X-RAY DIFFRACTION100
2.6085-2.65860.29572280.23444714X-RAY DIFFRACTION100
2.6586-2.71290.29582330.22624711X-RAY DIFFRACTION100
2.7129-2.77190.29272680.21734685X-RAY DIFFRACTION100
2.7719-2.83640.24222470.21024726X-RAY DIFFRACTION100
2.8364-2.90730.26842450.20484739X-RAY DIFFRACTION100
2.9073-2.98590.24262380.19914756X-RAY DIFFRACTION100
2.9859-3.07380.24512380.18964737X-RAY DIFFRACTION100
3.0738-3.1730.21282540.18194735X-RAY DIFFRACTION100
3.173-3.28640.22982270.19284736X-RAY DIFFRACTION100
3.2864-3.41790.23652720.18384762X-RAY DIFFRACTION100
3.4179-3.57350.21542510.17564718X-RAY DIFFRACTION100
3.5735-3.76180.19782610.16314770X-RAY DIFFRACTION100
3.7618-3.99750.18582570.15424768X-RAY DIFFRACTION100
3.9975-4.3060.1832300.14774785X-RAY DIFFRACTION100
4.306-4.73920.15992550.13814851X-RAY DIFFRACTION100
4.7392-5.42460.19692500.15294800X-RAY DIFFRACTION100
5.4246-6.83280.22442500.18444885X-RAY DIFFRACTION100
6.8328-59.13720.19872750.1785057X-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)
11.9175-0.4543-0.7563.7795-0.48671.5890.20860.03290.45-0.16460.0324-0.3818-0.80150.0977-0.23580.7182-0.0330.10780.4221-0.12080.441928.139598.439354.6697
21.73380.0217-0.11022.40851.0542.59310.00440.2105-0.0493-0.40950.2762-0.3584-0.40490.3939-0.2590.4019-0.05990.08590.4108-0.16030.375134.406783.0248.3955
31.4025-0.9041-0.80772.75290.66922.54170.0547-0.03380.02990.24280.0634-0.1457-0.01750.0885-0.10460.35290.0626-0.01310.3267-0.09490.324624.163779.978162.684
41.18781.3721-0.42052.45370.53865.04690.0079-0.0802-0.04920.2604-0.15810.93870.1535-0.75240.12820.41890.03730.11530.4591-0.15340.43189.469783.038571.8071
51.99590.11020.38161.6496-0.64031.3945-0.1942-0.17280.34570.73340.31470.3454-0.1795-0.3964-0.00090.62980.12630.03740.4456-0.1650.381316.820589.064480.6082
62.42350.02290.5722.35590.12622.110.019-0.00790.03790.3077-0.05850.14440.11270.13950.040.50190.07910.030.396-0.13650.28917.814788.769573.6637
70.5737-0.0453-0.03932.82110.93191.7539-0.10710.0129-0.22130.75090.13930.10710.63520.111-0.0460.38820.0727-0.01010.3805-0.11050.358622.954368.741466.5167
81.7866-0.10610.90842.47441.85394.2937-0.018-0.0123-0.12650.50220.3579-0.38930.51640.7085-0.25240.43350.1466-0.10880.3278-0.10160.41333.275661.54462.0279
91.2684-0.0973-0.21720.85330.66211.81760.01510.07570.2187-0.1366-0.0660.1008-0.3397-0.1577-0.08170.23310.0188-0.00540.2391-0.09380.283716.923959.048425.9655
100.68610.51710.68450.94320.12431.5311-0.1291-0.4013-0.0370.72010.25060.5906-0.0823-0.65840.44530.0132-0.0842-0.0205-0.0238-0.2641-0.006615.686249.750838.4297
112.3352-0.9738-0.20862.9345-0.37281.6916-0.06940.10410.335-0.11520.17040.079-0.35440.0261-0.08090.3027-0.083-0.00140.3206-0.01240.291314.858841.791-13.0193
122.0466-0.74340.02442.5928-0.07492.28150.03810.2231-0.0312-0.32460.1349-0.2539-0.09260.2318-0.13750.2393-0.08790.06790.3312-0.07290.305625.257930.084-14.6326
130.775-0.6796-0.65514.43750.28522.1465-0.06670.0906-0.03140.09070.01560.25210.20190.16950.01310.21340.00890.0130.2756-0.07760.269920.943720.0869-3.8184
142.2522-0.84590.41941.32880.67442.51030.04080.01740.0054-0.0007-0.1170.22770.0104-0.49870.05690.2308-0.04020.02930.3327-0.03420.27634.10428.03220.5709
152.6522-0.40441.29991.693-0.21152.3619-0.0765-0.30160.1068-0.01890.08910.18950.1042-0.5042-0.0380.2577-0.03730.04860.3553-0.05110.31881.864234.27728.8589
161.3009-0.4771-0.30291.38560.77431.4523-0.01460.0595-0.15090.23810.1333-0.11630.37120.1167-0.09160.3239-0.0065-0.05510.2409-0.06150.385720.98712.78512.6027
172.6347-0.2669-1.24215.48911.00972.2743-0.05870.83590.1203-0.24670.20620.32540.1152-0.1083-0.06650.4287-0.1466-0.00430.7005-0.08870.290315.472810.7887-41.1236
181.9981-0.5926-0.96432.95170.40622.8628-0.17241.1578-0.0615-0.43470.3186-0.59810.20460.4299-0.19730.6092-0.06870.13921.0016-0.41030.577629.10071.994-43.2421
191.7307-0.19690.00780.5552-0.87391.4821-0.01350.2765-0.5176-0.0780.1194-0.15860.68830.1125-0.08880.7318-0.02940.00950.6143-0.33450.657122.5769-9.2229-32.135
202.10040.67581.20371.81441.25221.1703-0.10020.7596-0.51-0.03790.07150.37920.9414-0.74260.03280.7709-0.29430.01550.809-0.21140.60367.2287-8.5912-38.2528
212.13170.83740.20141.0015-0.34093.74360.04850.33540.03660.03690.2556-0.2930.0803-0.1049-0.31940.4057-0.04510.05410.4608-0.19680.445718.76615.7626-23.2196
222.07890.0780.43752.68830.86072.36510.2080.5856-0.5909-0.0871-0.02210.49241.0229-0.9248-0.240.6756-0.3181-0.02960.8528-0.12090.58291.6253-6.847-26.3067
233.47870.5333-0.67531.977-0.13654.84980.03350.26160.03370.08710.08450.4158-0.352-1.0817-0.13210.419-0.06530.02540.6596-0.07620.44822.49584.2994-18.5376
240.30380.03210.0980.4425-0.10580.67390.08850.1687-0.4544-0.12350.24340.04790.9599-0.3320.91130.8215-0.048-0.0570.2859-0.33940.48118.9409-10.1609-25.5837
254.3463-0.5777-2.422.23930.2594.7622-0.2736-0.2503-0.57950.44430.2058-0.33510.73290.48770.00450.89250.0714-0.11610.4449-0.21470.824127.9563-13.9233-17.0002
261.7895-1.9695-0.4272.820.6040.3734-0.1569-0.20140.0920.86420.3555-0.1957-0.11930.46410.00810.8959-0.0307-0.1180.7046-0.19360.585927.590392.247181.7489
270.2937-0.2212-0.16020.17930.08310.2741-0.07790.0572-0.09230.13660.5094-0.39070.32630.7625-0.54130.46980.04510.05190.6463-0.29540.663743.559727.56233.4293
280.1759-0.2186-0.11230.3726-1.01352.2939-0.1808-0.2309-0.35790.1909-0.08-0.06990.5793-0.02580.19351.095-0.0070.10140.74620.10340.660315.839454.157891.2051
290.35060.04030.02261.5442-0.56141.2325-0.2979-0.2152-0.70590.490.265-0.43060.87510.01590.12251.6750.01520.22811.08330.13151.29825.288941.794100.6125
303.1103-0.0815-0.01371.36540.2942.0275-0.0191-0.6247-0.65760.67610.00340.0360.5832-0.2411-0.05881.384-0.17640.34670.9176-0.010.71851.575855.978690.0531
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 64 )
2X-RAY DIFFRACTION2chain 'A' and (resid 65 through 160 )
3X-RAY DIFFRACTION3chain 'A' and (resid 161 through 273 )
4X-RAY DIFFRACTION4chain 'A' and (resid 274 through 311 )
5X-RAY DIFFRACTION5chain 'A' and (resid 312 through 338 )
6X-RAY DIFFRACTION6chain 'A' and (resid 339 through 372 )
7X-RAY DIFFRACTION7chain 'A' and (resid 373 through 401 )
8X-RAY DIFFRACTION8chain 'A' and (resid 402 through 439 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 311 )
10X-RAY DIFFRACTION10chain 'B' and (resid 312 through 438 )
11X-RAY DIFFRACTION11chain 'C' and (resid 1 through 72 )
12X-RAY DIFFRACTION12chain 'C' and (resid 73 through 161 )
13X-RAY DIFFRACTION13chain 'C' and (resid 162 through 199 )
14X-RAY DIFFRACTION14chain 'C' and (resid 200 through 311 )
15X-RAY DIFFRACTION15chain 'C' and (resid 312 through 372 )
16X-RAY DIFFRACTION16chain 'C' and (resid 373 through 440 )
17X-RAY DIFFRACTION17chain 'D' and (resid 1 through 56 )
18X-RAY DIFFRACTION18chain 'D' and (resid 57 through 160 )
19X-RAY DIFFRACTION19chain 'D' and (resid 161 through 214 )
20X-RAY DIFFRACTION20chain 'D' and (resid 215 through 238 )
21X-RAY DIFFRACTION21chain 'D' and (resid 239 through 268 )
22X-RAY DIFFRACTION22chain 'D' and (resid 269 through 311 )
23X-RAY DIFFRACTION23chain 'D' and (resid 312 through 337 )
24X-RAY DIFFRACTION24chain 'D' and (resid 338 through 415 )
25X-RAY DIFFRACTION25chain 'D' and (resid 416 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 207 )
29X-RAY DIFFRACTION29chain 'F' and (resid 208 through 275 )
30X-RAY DIFFRACTION30chain 'F' and (resid 276 through 378 )

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