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- PDB-3ksa: Detailed structural insight into the DNA cleavage complex of type... -

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Basic information

Entry
Database: PDB / ID: 3ksa
TitleDetailed structural insight into the DNA cleavage complex of type IIA topoisomerases (cleaved form)
Components
  • (DNA topoisomerase 4 subunit ...) x 2
  • 5'-D(*AP*CP*CP*AP*AP*GP*GP*T*CP*AP*TP*GP*AP*AP*T)-3'
  • 5'-D(*CP*TP*GP*TP*TP*TP*TP*A*CP*GP*TP*GP*CP*AP*T)-3'
  • 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3'
  • 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*GP*TP*AP*AP*AP*AP*CP*AP*G)-3'
KeywordsISOMERASE/DNA / Topoisomerase / protein-DNA cleavage complex / Streptococcus pneumoniae / DNA-binding / nucleotide-binding / quinolone / Cleaved form / ISOMERASE-DNA COMPLEX
Function / homology
Function and homology information


DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity / DNA topoisomerase (ATP-hydrolysing) / extrinsic component of plasma membrane / DNA topological change / chromosome segregation / chromosome / DNA binding / ATP binding / metal ion binding / cytoplasm
Similarity search - Function
DNA topoisomerase IV subunit A, Gram-positive / DNA topoisomerase 4 subunit B, Firmicutes/Mollicutes / Rossmann fold - #670 / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA topoisomerase, type IIA, subunit B / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A ...DNA topoisomerase IV subunit A, Gram-positive / DNA topoisomerase 4 subunit B, Firmicutes/Mollicutes / Rossmann fold - #670 / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal / DNA gyrase C-terminal domain, beta-propeller / Topoisomerase (Topo) IIA-type catalytic domain profile. / DNA topoisomerase, type IIA, subunit B / DNA topoisomerase, type IIA, alpha-helical domain superfamily / DNA topoisomerase, type IIA, domain A / DNA topoisomerase, type IIA, domain A, alpha-beta / DNA gyrase/topoisomerase IV, subunit A / DNA Topoisomerase IV / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus / DNA topoisomerase, type IIA, subunit B, domain 2 / DNA gyrase B / DNA topoisomerase, type IIA / DNA topoisomerase, type IIA, conserved site / DNA topoisomerase II signature. / TopoisomeraseII / DNA topoisomerase, type IIA, subunit B, C-terminal / Toprim domain / DNA topoisomerase, type IIA-like domain superfamily / Toprim domain profile. / TOPRIM domain / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein S5 domain 2-type fold / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
DNA / DNA (> 10) / DNA topoisomerase 4 subunit A / DNA topoisomerase 4 subunit B
Similarity search - Component
Biological speciesStreptococcus pneumoniae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å
AuthorsLaponogov, I. / Pan, X.-S. / Veselkov, D.A. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
Citation
Journal: Plos One / Year: 2010
Title: Structural Basis of Gate-DNA Breakage and Resealing by Type II Topoisomerases
Authors: Laponogov, I. / Pan, X.-S. / Veselkov, D.A. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
#1: Journal: Nat.Struct.Mol.Biol. / Year: 2009
Title: Structural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases
Authors: Laponogov, I. / Sohi, M.K. / Veselkov, D.A. / Pan, X.-S. / Sawhney, R. / Thompson, A.W. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
History
DepositionNov 21, 2009Deposition site: RCSB / Processing site: PDBJ
Revision 1.0May 5, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 1, 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_ncs_dom_lim / 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_label_asym_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.pdbx_leaving_atom_flag / _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_label_seq_id / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_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: DNA topoisomerase 4 subunit A
B: DNA topoisomerase 4 subunit A
C: DNA topoisomerase 4 subunit B
D: DNA topoisomerase 4 subunit B
E: 5'-D(*AP*CP*CP*AP*AP*GP*GP*T*CP*AP*TP*GP*AP*AP*T)-3'
F: 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3'
G: 5'-D(*CP*TP*GP*TP*TP*TP*TP*A*CP*GP*TP*GP*CP*AP*T)-3'
H: 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*GP*TP*AP*AP*AP*AP*CP*AP*G)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)194,61610
Polymers194,5688
Non-polymers492
Water1267
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20900 Å2
ΔGint-105 kcal/mol
Surface area56140 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.911, 116.911, 183.759
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21B
12C
22D

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111ASNASNLYSLYSchain A and (resseq 3:246 or resseq 253:285 or resseq 287:483 )AA3 - 2463 - 246
121GLNGLNALAALAchain A and (resseq 3:246 or resseq 253:285 or resseq 287:483 )AA253 - 285253 - 285
131VALVALGLUGLUchain A and (resseq 3:246 or resseq 253:285 or resseq 287:483 )AA287 - 483287 - 483
211ASNASNLYSLYSchain B and (resseq 3:246 or resseq 253:285 or resseq 287:483 )BB3 - 2463 - 246
221GLNGLNALAALAchain B and (resseq 3:246 or resseq 253:285 or resseq 287:483 )BB253 - 285253 - 285
231VALVALGLUGLUchain B and (resseq 3:246 or resseq 253:285 or resseq 287:483 )BB287 - 483287 - 483
112LYSLYSVALVALchain C and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )CC415 - 48736 - 108
122ASPASPGLUGLUchain C and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )CC490 - 494111 - 115
132ALAALALYSLYSchain C and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )CC496 - 547117 - 168
142GLUGLUTHRTHRchain C and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )CC553 - 640174 - 261
212LYSLYSVALVALchain D and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )DD415 - 48736 - 108
222ASPASPGLUGLUchain D and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )DD490 - 494111 - 115
232ALAALALYSLYSchain D and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )DD496 - 547117 - 168
242GLUGLUTHRTHRchain D and (resseq 415:487 or resseq 490:494 or resseq 496:547 or resseq 553:640 )DD553 - 640174 - 261

NCS ensembles :
ID
1
2

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Components

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DNA topoisomerase 4 subunit ... , 2 types, 4 molecules ABCD

#1: Protein DNA topoisomerase 4 subunit A / ParC55 / Topoisomerase IV subunit A


Mass: 56455.434 Da / Num. of mol.: 2 / Fragment: residues 1-488
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: 7785 / Gene: parC / Plasmid: pET29A / Production host: Escherichia coli (E. coli) / References: UniProt: P72525, EC: 5.99.1.-
#2: Protein DNA topoisomerase 4 subunit B / ParE30 / Topoisomerase IV subunit B


Mass: 30415.703 Da / Num. of mol.: 2 / Fragment: residues 404-647
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: 7785 / Gene: parE / Plasmid: pET19B / Production host: Escherichia coli (E. coli) / References: UniProt: Q59961, EC: 5.99.1.-

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DNA chain , 4 types, 4 molecules EFGH

#3: DNA chain 5'-D(*AP*CP*CP*AP*AP*GP*GP*T*CP*AP*TP*GP*AP*AP*T)-3'


Mass: 4602.024 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site
#4: DNA chain 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3'


Mass: 5810.770 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site
#5: DNA chain 5'-D(*CP*TP*GP*TP*TP*TP*TP*A*CP*GP*TP*GP*CP*AP*T)-3'


Mass: 4565.968 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site
#6: DNA chain 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*GP*TP*AP*AP*AP*AP*CP*AP*G)-3'


Mass: 5846.827 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site

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Non-polymers , 2 types, 9 molecules

#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 7 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsFOR CHAIN A AND B, THE DATABASE REFERENCE SEQUENCE IS REFERRED IN REFERENCES 1 AND 4 OF PARC_STRPN, ...FOR CHAIN A AND B, THE DATABASE REFERENCE SEQUENCE IS REFERRED IN REFERENCES 1 AND 4 OF PARC_STRPN, UNIPROT. THE 257TH RESIDUE IS THR ACCORDING TO THEM. FOR CHAIN C AND D, THE DATABASE REFERENCE SEQUENCE IS REFERRED IN REFERENCES 1 AND 4 OF PARE_STRPN, UNIPROT. THE 460TH AND 644TH RESIDUES ARE ILE AND ALA, RESPECTIVELY, ACCORDING TO THEM.

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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: 3.73 Å3/Da / Density % sol: 66.99 %
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 4-5% isopropanol, optimised mixture of salts, 50mM Na cacodylate, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 7, 2009
RadiationMonochromator: Double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 3.3→50 Å / Num. obs: 41533 / % possible obs: 98 % / Observed criterion σ(F): -3 / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Biso Wilson estimate: 116.06 Å2 / Rmerge(I) obs: 0.08 / Rsym value: 0.08 / Net I/σ(I): 15.725
Reflection shellResolution: 3.3→3.42 Å / Redundancy: 5.7 % / Rmerge(I) obs: 0.461 / Mean I/σ(I) obs: 3.512 / Num. unique all: 4232 / Rsym value: 0.461 / % possible all: 100

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Processing

Software
NameVersionClassification
GDAdata collection
PHASERphasing
PHENIX(phenix.refine)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3K9F

3k9f


Resolution: 3.3→29.403 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.12 / Isotropic thermal model: Isotropic+TLS / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 22.09 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2181 4164 10.09 %random
Rwork0.1762 37086 --
obs0.1805 41250 97.77 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 115.475 Å2 / ksol: 0.279 e/Å3
Displacement parametersBiso max: 400.19 Å2 / Biso mean: 136.591 Å2 / Biso min: 64.69 Å2
Baniso -1Baniso -2Baniso -3
1-1.332 Å2-0 Å2-0 Å2
2--1.332 Å20 Å2
3----49.123 Å2
Refinement stepCycle: LAST / Resolution: 3.3→29.403 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10079 730 2 7 10818
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02711602
X-RAY DIFFRACTIONf_angle_d1.29515224
X-RAY DIFFRACTIONf_chiral_restr0.0821812
X-RAY DIFFRACTIONf_plane_restr0.0061845
X-RAY DIFFRACTIONf_dihedral_angle_d20.2316429
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3426X-RAY DIFFRACTIONPOSITIONAL0.017
12B3426X-RAY DIFFRACTIONPOSITIONAL0.017
21C1589X-RAY DIFFRACTIONPOSITIONAL0.017
22D1589X-RAY DIFFRACTIONPOSITIONAL0.017
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3-3.33750.35761460.29661268X-RAY DIFFRACTION100
3.3375-3.37670.30951080.25891248X-RAY DIFFRACTION100
3.3767-3.41780.33191350.26331313X-RAY DIFFRACTION99
3.4178-3.4610.35151270.26081248X-RAY DIFFRACTION99
3.461-3.50650.32191350.23541286X-RAY DIFFRACTION99
3.5065-3.55450.27261420.21941241X-RAY DIFFRACTION99
3.5545-3.60510.23481420.22061238X-RAY DIFFRACTION100
3.6051-3.65890.27351240.21261284X-RAY DIFFRACTION99
3.6589-3.71590.23841380.19841247X-RAY DIFFRACTION99
3.7159-3.77670.23021600.17541265X-RAY DIFFRACTION100
3.7767-3.84170.23771480.18031225X-RAY DIFFRACTION100
3.8417-3.91140.20051610.16471289X-RAY DIFFRACTION99
3.9114-3.98650.19941140.16121216X-RAY DIFFRACTION99
3.9865-4.06760.2331430.16141263X-RAY DIFFRACTION99
4.0676-4.15580.22021470.15531275X-RAY DIFFRACTION100
4.1558-4.25220.2091580.15711244X-RAY DIFFRACTION100
4.2522-4.35830.19371540.13291261X-RAY DIFFRACTION100
4.3583-4.47570.17411390.1221262X-RAY DIFFRACTION100
4.4757-4.60690.15031660.1171226X-RAY DIFFRACTION100
4.6069-4.7550.17061400.11971266X-RAY DIFFRACTION100
4.755-4.92420.16481420.12391263X-RAY DIFFRACTION100
4.9242-5.12040.17971350.14071275X-RAY DIFFRACTION100
5.1204-5.35210.21721400.14371282X-RAY DIFFRACTION100
5.3521-5.63240.22341440.15631242X-RAY DIFFRACTION100
5.6324-5.98250.2091580.1731248X-RAY DIFFRACTION100
5.9825-6.440.22711350.1761299X-RAY DIFFRACTION100
6.44-7.07980.23361340.17131251X-RAY DIFFRACTION100
7.0798-8.08560.20271410.17021271X-RAY DIFFRACTION100
8.0856-10.11760.16851350.16781153X-RAY DIFFRACTION92
10.1176-29.40430.2285730.2486637X-RAY DIFFRACTION50
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)
1-0.4297-0.631-0.64233.9893.77742.72570.5931-0.4734-0.1992-0.7719-0.1122-1.0642-1.3040.2176-0.10251.21190.01330.07051.12870.37591.2418-13.625130.07516.5665
23.1095-0.4381-1.11330.6793-1.1483-0.7796-0.381-0.40220.00650.22180.2010.0284-0.28730.10490.08241.0559-0.4104-0.01811.5229-0.00120.886-20.921948.942828.5993
38.426-3.51383.347-4.29042.09755.8114-1.1005-0.87620.74851.38461.27942.0043-1.1896-0.5994-0.28721.05860.12570.3980.80550.28881.5612-7.202139.845-25.722
4-2.9691-0.7742-0.13150.31880.41910.42630.3444-0.12210.0566-0.09260.0705-0.08680.04580.4989-0.36110.714-0.29740.11771.20330.21131.46185.345651.5187-33.8931
52.7855-0.3480.50872.4936-0.22232.5617-0.11580.0064-0.4723-0.0783-0.28510.4863-0.1870.06670.31640.7465-0.07470.14640.56870.05470.9644-25.406237.8148-16.9222
66.8821-1.2153-5.78161.3286-0.79558.57040.4844-1.9013-0.9780.3662-0.80890.2418-0.83222.08990.43051.4063-0.2519-0.09641.56030.56241.2909-18.628927.605518.9548
74.3268-0.51260.43973.07032.68681.24091.19820.371-1.63070.2825-1.0075-0.80360.46410.1728-0.3571.15560.0526-0.05140.6225-0.50681.2677-35.676215.5571-42.9808
82.9883-3.45953.0070.3503-2.60356.862-0.3491-0.164-1.89560.01990.93790.5840.43910.3634-0.22111.3399-0.06410.24330.9070.3111.194-20.518216.1176-7.5034
90.7425-1.6689-0.54481.01311.41860.4840.12860.1597-0.7459-0.0578-0.51580.34290.82230.22570.35991.1950.03940.23470.53170.08021.4171-15.04918.2562-22.1853
100.4627-0.67680.33264.3285-2.68393.75850.604-0.59380.3316-0.662-0.32720.89621.37380.0039-0.07711.0922-0.0306-0.09381.0322-0.39841.224-44.784671.20496.4472
114.4877-0.6733-0.06851.28180.7524-2.0728-0.5185-0.9816-0.33890.58180.06960.02450.6653-0.41840.27491.1107-0.44580.02761.4887-0.01320.7883-37.433552.165328.6185
129.62940.0918-1.9281-0.9361-2.1871.261-1.3336-1.1421-0.76630.641.2693-1.57030.56590.7508-0.12281.19390.0931-0.45690.9154-0.30041.4348-51.249361.4153-25.7286
13-4.2957-1.43040.5204-0.2445-0.4944-0.11460.1986-0.0781-0.8935-0.22140.1305-0.13630.214-0.1753-0.2820.5979-0.2264-0.10371.1044-0.24981.5044-63.799249.7486-33.9002
142.7239-0.1793-0.43822.1546-0.15373.1395-0.1029-0.0790.5870.0171-0.2689-0.47590.05-0.05410.29380.7786-0.0667-0.17620.584-0.04680.9948-33.090563.408-16.9379
156.0689-1.66316.67481.0381-0.02539.26740.1809-1.78891.04780.1319-0.7323-0.19130.5636-2.51770.69261.25-0.22530.08591.5104-0.54241.2622-39.82773.635418.9525
162.2718-0.7973-0.30382.5044-1.77420.4010.78340.18431.29710.2264-1.01550.3301-0.1060.00780.04971.2164-0.0061-0.01560.70390.57411.3191-22.776685.6743-43.0927
172.5634-3.7922-3.13040.67512.39896.3209-0.3281-0.02471.60670.19950.6573-0.8499-0.5002-0.3729-0.18011.3061-0.0033-0.29030.8086-0.2841.1629-37.932385.1298-7.5005
180.8865-1.55561.29250.5158-1.85210.65430.01150.03160.680.1701-0.5213-0.269-0.5609-0.13790.43681.1970.0333-0.21780.5642-0.08461.4171-43.418983.0897-22.1672
192.1249-3.7267-4.35783.35351.92615.13880.0637-1.7812-0.21970.19980.4873-0.82590.29171.9595-0.37211.029-0.1207-0.01221.59090.14881.2119-5.679359.4467-14.5953
205.59528.0691-6.8023.5986-1.35255.55730.4994-0.2928-1.3103-0.7421-0.7639-1.5587-0.22690.91620.43771.10890.14880.31841.25010.20421.39284.238437.454-38.7818
212.8759-0.10520.39161.3390.9668-0.04920.14030.54940.5937-0.1234-0.09140.06590.00080.4045-0.00521.0669-0.04650.18631.04450.37151.0908-5.143858.2129-39.7635
22-3.2897-4.53215.5083.9144-2.14552.1994-0.0034-1.0939-0.46320.28610.42211.3037-0.2198-3.1491-0.09741.2154-0.11010.0221.9129-0.17741.3949-52.900242.3799-14.8933
235.959.73437.29377.73555.15146.5050.6775-0.15771.2978-0.6728-1.07771.931-0.0841-1.13380.61391.09110.1456-0.36071.3056-0.18031.3748-62.68363.796-38.7855
242.8931-0.0275-0.41111.4398-1.58320.69890.210.3917-0.6314-0.1634-0.1342-0.17810.0798-0.4038-0.04611.0097-0.0658-0.19380.9471-0.35471.0183-53.33843.0245-39.753
252.2758-0.1980.01523.5192-1.46790.14110.43050.7436-0.3258-0.4801-0.8612-0.32430.1851-0.00130.32841.29280.12770.18810.8687-0.17260.9675-20.256738.9713-37.3852
262.84660.33440.8914.5590.55470.10070.49590.87320.2291-0.4365-0.91130.6814-0.39560.07820.28211.13010.1285-0.20180.74370.17840.7427-38.215662.2499-37.3623
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 343:382A343 - 382
2X-RAY DIFFRACTION2chain A and resseq 383:429A383 - 429
3X-RAY DIFFRACTION3chain A and resseq 18:30A18 - 30
4X-RAY DIFFRACTION4chain A and resseq 2:17A2 - 17
5X-RAY DIFFRACTION5chain A and resseq 31:154A31 - 154
6X-RAY DIFFRACTION6chain A and resseq 430:455A430 - 455
7X-RAY DIFFRACTION7chain A and resseq 239:322A239 - 322
8X-RAY DIFFRACTION8chain A and resseq 456:482A456 - 482
9X-RAY DIFFRACTION9chain A and not (resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482)A0
10X-RAY DIFFRACTION10chain B and resseq 343:382B343 - 382
11X-RAY DIFFRACTION11chain B and resseq 383:429B383 - 429
12X-RAY DIFFRACTION12chain B and resseq 18:30B18 - 30
13X-RAY DIFFRACTION13chain B and resseq 2:17B2 - 17
14X-RAY DIFFRACTION14chain B and resseq 31:154B31 - 154
15X-RAY DIFFRACTION15chain B and resseq 430:455B430 - 455
16X-RAY DIFFRACTION16chain B and resseq 239:322B239 - 322
17X-RAY DIFFRACTION17chain B and resseq 456:482B456 - 482
18X-RAY DIFFRACTION18chain B and not (resseq 343:382 or resseq 383:429 or resseq 31:154 or resseq 430:455 or resseq 239:322 or resseq 2:17 or resseq 18:30 or resseq 456:482)B0
19X-RAY DIFFRACTION19chain C and resseq 539:581C539 - 581
20X-RAY DIFFRACTION20chain C and resseq 610:634C610 - 634
21X-RAY DIFFRACTION21chain C and not (resseq 539:581 or resseq 610:634)C0
22X-RAY DIFFRACTION22chain D and resseq 539:581D539 - 581
23X-RAY DIFFRACTION23chain D and resseq 610:634D610 - 634
24X-RAY DIFFRACTION24chain D and not (resseq 539:581 or resseq 610:634)D0
25X-RAY DIFFRACTION25chain E or chain FE9 - 15
26X-RAY DIFFRACTION25chain E or chain FF1 - 11
27X-RAY DIFFRACTION26chain G or chain HG9 - 15
28X-RAY DIFFRACTION26chain G or chain HH1 - 11

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