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

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Basic information

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


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
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: 3.5 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 / 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 / _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*TP*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*GP*TP*AP*AP*AP*AP*CP*AP*G)-3'
F: 5'-D(*CP*TP*GP*TP*TP*TP*TP*A*CP*GP*TP*GP*CP*AP*TP*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)194,7068
Polymers194,6586
Non-polymers492
Water724
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20010 Å2
ΔGint-110 kcal/mol
Surface area56310 Å2
MethodPISA
Unit cell
Length a, b, c (Å)116.757, 116.757, 182.811
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 287:300 or resseq 304:483 )AA3 - 2463 - 246
121GLNGLNALAALAchain A and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )AA253 - 285253 - 285
131VALVALILEILEchain A and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )AA287 - 300287 - 300
141LYSLYSGLUGLUchain A and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )AA304 - 483304 - 483
211ASNASNLYSLYSchain B and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )BB3 - 2463 - 246
221GLNGLNALAALAchain B and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )BB253 - 285253 - 285
231VALVALILEILEchain B and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )BB287 - 300287 - 300
241LYSLYSGLUGLUchain B and (resseq 3:246 or resseq 253:285 or resseq 287:300 or resseq 304:483 )BB304 - 483304 - 483
112LYSLYSLYSLYSchain C and (resseq 415:464 or resseq 468:487 or resseq...CC415 - 46436 - 85
122ALAALAVALVALchain C and (resseq 415:464 or resseq 468:487 or resseq...CC468 - 48789 - 108
132ASPASPGLUGLUchain C and (resseq 415:464 or resseq 468:487 or resseq...CC490 - 494111 - 115
142ALAALALYSLYSchain C and (resseq 415:464 or resseq 468:487 or resseq...CC496 - 547117 - 168
152LYSLYSPHEPHEchain C and (resseq 415:464 or resseq 468:487 or resseq...CC551 - 571172 - 192
162ALAALATHRTHRchain C and (resseq 415:464 or resseq 468:487 or resseq...CC575 - 640196 - 261
212LYSLYSLYSLYSchain D and (resseq 415:464 or resseq 468:487 or resseq...DD415 - 46436 - 85
222ALAALAVALVALchain D and (resseq 415:464 or resseq 468:487 or resseq...DD468 - 48789 - 108
232ASPASPGLUGLUchain D and (resseq 415:464 or resseq 468:487 or resseq...DD490 - 494111 - 115
242ALAALALYSLYSchain D and (resseq 415:464 or resseq 468:487 or resseq...DD496 - 547117 - 168
252LYSLYSPHEPHEchain D and (resseq 415:464 or resseq 468:487 or resseq...DD551 - 571172 - 192
262ALAALATHRTHRchain D and (resseq 415:464 or resseq 468:487 or resseq...DD575 - 640196 - 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 / Topoisomerase / 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 / Topoisomerase / 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 , 2 types, 2 molecules EF

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


Mass: 10493.806 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site
#4: DNA chain 5'-D(*CP*TP*GP*TP*TP*TP*TP*A*CP*GP*TP*GP*CP*AP*TP*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3'


Mass: 10421.695 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site

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Non-polymers , 2 types, 6 molecules

#5: Chemical ChemComp-MG / MAGNESIUM ION


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


Mass: 18.015 Da / Num. of mol.: 4 / 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: 3.7 Å3/Da / Density % sol: 66.72 %
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: 3.5→50 Å / Num. obs: 34407 / % possible obs: 97.7 % / Observed criterion σ(F): -3 / Observed criterion σ(I): 0 / Redundancy: 6.1 % / Biso Wilson estimate: 134.28 Å2 / Rmerge(I) obs: 0.065 / Rsym value: 0.065 / Net I/σ(I): 21.958
Reflection shellResolution: 3.5→3.63 Å / Redundancy: 6.5 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 4.325 / Num. unique all: 3529 / Rsym value: 0.4 / % 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: 3.5→29.318 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.74 / Isotropic thermal model: Isotropic+TLS / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 21.33 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2257 3524 10.3 %random
Rwork0.1813 30696 --
obs0.1859 34220 97.53 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 137.375 Å2 / ksol: 0.291 e/Å3
Displacement parametersBiso max: 268.57 Å2 / Biso mean: 147.717 Å2 / Biso min: 71.62 Å2
Baniso -1Baniso -2Baniso -3
1--4.813 Å20 Å2-0 Å2
2---4.813 Å20 Å2
3----25.078 Å2
Refinement stepCycle: LAST / Resolution: 3.5→29.318 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9865 730 2 4 10601
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02711360
X-RAY DIFFRACTIONf_angle_d1.44114939
X-RAY DIFFRACTIONf_chiral_restr0.0951796
X-RAY DIFFRACTIONf_plane_restr0.0061806
X-RAY DIFFRACTIONf_dihedral_angle_d20.0656275
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3379X-RAY DIFFRACTIONPOSITIONAL0.021
12B3379X-RAY DIFFRACTIONPOSITIONAL0.021
21C1521X-RAY DIFFRACTIONPOSITIONAL0.021
22D1521X-RAY DIFFRACTIONPOSITIONAL0.021
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.5001-3.54790.32791580.26291269X-RAY DIFFRACTION99
3.5479-3.59850.27131330.25611215X-RAY DIFFRACTION99
3.5985-3.65210.30551240.2251268X-RAY DIFFRACTION99
3.6521-3.70910.24811380.22071250X-RAY DIFFRACTION100
3.7091-3.76980.26351620.19611281X-RAY DIFFRACTION100
3.7698-3.83470.24651510.19241207X-RAY DIFFRACTION99
3.8347-3.90420.19821510.17041275X-RAY DIFFRACTION100
3.9042-3.97920.21851230.16461257X-RAY DIFFRACTION100
3.9792-4.06020.26341430.16561267X-RAY DIFFRACTION99
4.0602-4.14820.22131440.16021233X-RAY DIFFRACTION100
4.1482-4.24440.2031560.15521245X-RAY DIFFRACTION100
4.2444-4.35030.20771510.13691273X-RAY DIFFRACTION100
4.3503-4.46750.16611380.12381245X-RAY DIFFRACTION100
4.4675-4.59850.15151690.11681236X-RAY DIFFRACTION100
4.5985-4.74630.17571360.12421235X-RAY DIFFRACTION100
4.7463-4.91520.19571510.13291301X-RAY DIFFRACTION100
4.9152-5.1110.20511300.14491248X-RAY DIFFRACTION100
5.111-5.34230.20651370.1571259X-RAY DIFFRACTION100
5.3423-5.6220.24021480.16951276X-RAY DIFFRACTION100
5.622-5.97150.23271530.19261233X-RAY DIFFRACTION100
5.9715-6.42810.26551360.18521280X-RAY DIFFRACTION100
6.4281-7.06680.251340.18121257X-RAY DIFFRACTION100
7.0668-8.07060.20661410.17661270X-RAY DIFFRACTION100
8.0706-10.09860.17221340.18161142X-RAY DIFFRACTION91
10.0986-29.3190.2467830.2492674X-RAY DIFFRACTION54
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)
1-1.2121-1.0628-1.57365.72343.05222.23220.5826-0.46670.0275-0.18660.0078-0.9043-1.08220.94040.10750.78580.09840.08630.78360.37870.9415-13.572229.87385.7479
23.14680.2735-4.60261.5847-2.7847-2.9966-0.62460.21580.39670.07230.0897-0.0598-0.59790.60550.40791.3473-0.6014-0.06971.5549-0.04770.6117-20.836448.957828.1141
37.23860.27525.68116.5882-9.23779.254-1.1106-0.72121.50972.02290.3139-0.3027-1.0558-1.76230.32291.04590.11920.41570.71740.26760.9993-7.478639.839-26.123
41.9189-0.94331.9366-0.53550.3726-0.85080.0331-0.4802-0.625-1.05950.36781.1548-0.48430.802-0.31550.6133-0.34480.21971.12470.13321.13175.293251.491-34.088
53.4745-0.50910.2112.77230.59524.2807-0.3328-0.0069-0.5122-0.0704-0.09410.3061-0.64160.02340.2830.9055-0.02220.18580.78210.06680.9489-25.375737.7517-17.325
64.8262-1.6160.2921.6552-0.54361.2560.1134-1.9304-0.80770.6734-0.66080.1814-0.18661.0730.20041.5434-0.4503-0.16591.64220.56211.2347-18.584727.580218.6343
73.6519-1.7740.49562.16571.0720.54370.75960.0366-1.39520.4784-0.8167-0.4696-0.00320.47240.07411.2995-0.05070.17790.9038-0.5411.3081-35.372815.6311-42.9092
80.9864-4.27991.23042.11533.69195.8725-1.7010.1701-1.34940.32111.4711.197-0.33871.20410.57551.66-0.07960.27911.08980.39111.045-20.3516.053-7.7571
91.3187-1.0907-0.9924-0.34681.48443.2150.07450.2479-0.64060.1742-0.33910.30971.01430.07370.24461.22520.07940.24350.61930.06041.3123-14.860718.1312-22.3182
10-1.1378-2.01831.12155.1917-3.18260.29080.3719-0.4780.1629-0.1195-0.12950.59730.6496-0.66760.25091.03780.0413-0.15410.9168-0.36121.1327-44.801771.02696.2386
112.32080.71142.89332.36051.53-0.8633-0.45080.2384-0.5755-0.1728-0.1523-0.07230.369-0.04870.47011.1996-0.60520.03991.5201-0.04230.585-37.42752.093728.2263
126.7839-7.2093-7.96195.5198.03868.2535-1.2915-1.0703-1.16551.14270.38570.17240.98781.85290.48641.19750.0963-0.4220.8323-0.2651.0028-50.897361.2778-26.1272
131.9546-0.6075-2.0937-1.20810.1062-1.1129-0.17170.6980.1327-0.88490.7421-1.58450.3776-0.6894-0.45550.7499-0.3502-0.21481.3046-0.23421.3091-63.674449.6331-34.0973
142.8609-0.33980.92082.1452-1.17774.0267-0.3634-0.11180.5977-0.0904-0.1217-0.27610.4564-0.11940.34650.8745-0.0294-0.20240.7431-0.06760.9593-32.995163.3364-17.1529
152.6473-1.3415-2.27332.88612.37741.98550.339-1.41580.37730.8686-0.53540.44740.4257-1.60250.30981.4117-0.52610.15471.6292-0.59981.1252-39.79773.528618.635
164.21020.4488-0.62090.9101-1.12611.09840.4615-0.05081.380.5207-0.89380.61890.1061-0.49380.26181.22670.0443-0.18180.90040.61411.2977-22.922185.474-42.9537
170.5041-3.7836-1.28931.6174-5.32677.1981-1.55480.35921.19290.38721.2155-1.2764-0.0531-1.16110.55921.81430.0699-0.25480.9653-0.3991.1098-38.030685.0592-7.757
181.7927-1.85391.56070.05-2.29782.5977-0.07950.10440.7190.4323-0.3426-0.35-0.8898-0.04520.37171.28870.0083-0.24380.785-0.07831.4045-43.479382.9662-22.4664
193.7121-1.484-2.1497.23-0.5026-2.10510.8418-2.41220.48620.98390.0526-0.7824-0.10380.5175-0.38711.36480.00080.062.10190.05331.1254-5.604159.2217-14.9115
209.09497.3398-9.42125.5362-3.05876.0279-0.5092-1.2861-1.8287-0.5548-0.411-2.37540.18070.74890.9140.61530.18490.34331.05330.13180.91943.55737.6299-39.1043
213.24180.48580.36092.04990.5985-0.7540.19140.67570.585-0.2849-0.1284-0.17890.07540.37240.02421.0383-0.00010.15971.20330.36640.9292-5.078558.503-39.673
221.1401-1.655-0.60586.4042-1.86511.05720.9184-2.1599-0.23961.2350.23151.1426-0.4905-0.6675-0.56051.39210.0305-0.12242.1118-0.08441.2857-52.969742.0052-15.5252
232.54389.08489.79799.0684.97137.7524-0.619-1.23522.2284-1.033-0.23663.2247-0.0974-1.44390.85960.59180.1429-0.37931.1564-0.11590.9929-61.924763.4727-39.1034
243.48850.9888-0.7332.5034-0.683-0.47750.24750.6865-0.6681-0.4671-0.2260.1038-0.0216-0.33780.03011.0356-0.016-0.16811.1325-0.35480.9107-53.359342.5677-39.6424
254.3977-3.3390.20134.2583-0.2516-1.6283-0.14261.5188-0.0752-0.2031-0.67740.12230.03410.04850.61341.40810.1436-0.00541.15950.00490.9305-29.198850.5555-37.5649
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 - 26
26X-RAY DIFFRACTION25chain E or chain FF9 - 26

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