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- PDB-3rad: Quinolone(Clinafloxacin)-DNA cleavage complex of type IV topoisom... -

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Basic information

Entry
Database: PDB / ID: 3rad
TitleQuinolone(Clinafloxacin)-DNA cleavage complex of type IV topoisomerase from S. pneumoniae
Components
  • (DNA topoisomerase 4 subunit ...) x 2
  • 5'-D(*CP*AP*TP*GP*AP*AP*T)-3'
  • 5'-D(*CP*GP*TP*GP*CP*AP*T)-3'
  • 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*G)-3'
  • 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*G)-3'
KeywordsISOMERASE/DNA/ANTIBIOTIC / PROTEIN-DNA CLEAVAGE COMPLEX / Topoisomerase IIa / Clinafloxacin / ISOMERASE-DNA-ANTIBIOTIC complex
Function / homology
Function and homology information


DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) complex / DNA negative supercoiling 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 / DNA topoisomerase, type IIA, subunit B / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus ...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 / DNA topoisomerase, type IIA, subunit B / DNA gyrase B subunit, C-terminal / DNA gyrase B subunit, carboxyl terminus / Topoisomerase (Topo) IIA-type catalytic domain profile. / 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 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 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
Chem-NFX / DNA / DNA (> 10) / DNA topoisomerase 4 subunit A / DNA topoisomerase 4 subunit B
Similarity search - Component
Biological speciesStreptococcus pneumoniae (bacteria)
synthetic construct (others)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.35 Å
AuthorsLaponogov, I. / Pan, X.-S. / Veselkov, D.A. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
CitationJournal: Open Biol / Year: 2016
Title: Exploring the active site of the Streptococcus pneumoniae topoisomerase IV-DNA cleavage complex with novel 7,8-bridged fluoroquinolones.
Authors: Laponogov, I. / Pan, X.S. / Veselkov, D.A. / Cirz, R.T. / Wagman, A. / Moser, H.E. / Fisher, L.M. / Sanderson, M.R.
History
DepositionMar 28, 2011Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Apr 25, 2012Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / Database references / Source and taxonomy
Category: citation / citation_author / pdbx_entity_src_syn
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Nov 6, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / 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_entry_details.has_protein_modification / _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_seq_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_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(*CP*AP*TP*GP*AP*AP*T)-3'
F: 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*G)-3'
G: 5'-D(*CP*GP*TP*GP*CP*AP*T)-3'
H: 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*G)-3'
hetero molecules


Theoretical massNumber of molelcules
Total (without water)185,56116
Polymers184,6848
Non-polymers8778
Water61334
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19370 Å2
ΔGint-116 kcal/mol
Surface area57280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)157.128, 157.128, 211.091
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 3:245 OR RESSEQ 247:249 OR RESSEQ...
211CHAIN B AND (RESSEQ 3:245 OR RESSEQ 247:249 OR RESSEQ...
112CHAIN C AND (RESSEQ 415:544 OR RESSEQ 557:569 OR RESSEQ 577:640 ) AND (NOT ELEMENT H)
212CHAIN D AND (RESSEQ 415:544 OR RESSEQ 557:569 OR RESSEQ 577:640 ) AND (NOT ELEMENT H)

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 IV subunit A


Mass: 56455.434 Da / Num. of mol.: 2 / Fragment: UNP residues 1-488
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: 7785 / Gene: parC, SP_0855 / Plasmid: pET29A / Production host: Escherichia coli (E. coli)
References: UniProt: P72525, Isomerases; Other isomerases; Sole sub-subclass for isomerases that do not belong in the other subclasses
#2: Protein DNA topoisomerase 4 subunit B / Topoisomerase IV subunit B


Mass: 30415.703 Da / Num. of mol.: 2 / Fragment: UNP residues 404-647
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Streptococcus pneumoniae (bacteria) / Strain: 7785 / Gene: parE, SP_0852 / Plasmid: pET19B / Production host: Escherichia coli (E. coli)
References: UniProt: Q59961, Isomerases; Other isomerases; Sole sub-subclass for isomerases that do not belong in the other subclasses

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DNA chain , 4 types, 4 molecules EFGH

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


Mass: 2121.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#4: DNA chain 5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*G)-3'


Mass: 3348.209 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#5: DNA chain 5'-D(*CP*GP*TP*GP*CP*AP*T)-3'


Mass: 2113.410 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)
#6: DNA chain 5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*G)-3'


Mass: 3358.211 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others)

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Non-polymers , 3 types, 42 molecules

#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-NFX / 7-[(3R)-3-aminopyrrolidin-1-yl]-8-chloro-1-cyclopropyl-6-fluoro-4-oxo-1,4-dihydroquinoline-3-carboxylic acid / Clinafloxacin


Mass: 365.787 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H17ClFN3O3 / Comment: antibiotic*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 34 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsTHE SEQUENCE DIFFERENCES ARE CONSERVED MUTATIONS.

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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: 4.07 Å3/Da / Density % sol: 69.8 %
Crystal growTemperature: 304 K / Method: liquid diffusion / pH: 6.5
Details: 50mM sodium cacodylate, 7% isopropanol, pH 6.5, LIQUID DIFFUSION, temperature 304K

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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: Sep 26, 2010
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 3.1→50 Å / Num. all: 55483 / Num. obs: 55095 / % possible obs: 99.3 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Biso Wilson estimate: 90.1 Å2 / Rmerge(I) obs: 0.102 / Rsym value: 0.102 / Net I/σ(I): 13.144
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allRsym value% possible all
3.1-3.214.10.841.4354320.8498.8
3.21-3.344.60.6252.3254550.62599.7
3.34-3.494.70.4533.5654510.45399.6
3.49-3.684.70.2895.5754680.28999.7
3.68-3.914.70.1928.0954900.19299.8
3.91-4.214.60.13311.255280.13399.8
4.21-4.634.60.0916.3655360.0999.9
4.63-5.34.60.07916.7255210.07999.8
5.3-6.674.50.0717.9456160.0799.9
6.67-504.50.03330.7755980.03396.2

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Processing

Software
NameVersionClassification
GDEdata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.35→41.674 Å / SU ML: 0.96 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 22.07 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2279 4348 9.99 %Random
Rwork0.1774 ---
obs0.1825 43537 99.28 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 42.62 Å2 / ksol: 0.266 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-14.2168 Å2-0 Å2-0 Å2
2--14.2168 Å2-0 Å2
3----28.4337 Å2
Refinement stepCycle: LAST / Resolution: 3.35→41.674 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10244 730 56 34 11064
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00911312
X-RAY DIFFRACTIONf_angle_d1.28215517
X-RAY DIFFRACTIONf_dihedral_angle_d18.2424071
X-RAY DIFFRACTIONf_chiral_restr0.0751785
X-RAY DIFFRACTIONf_plane_restr0.0041906
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3373X-RAY DIFFRACTIONPOSITIONAL
12B3373X-RAY DIFFRACTIONPOSITIONAL0.8
21C1392X-RAY DIFFRACTIONPOSITIONAL
22D1392X-RAY DIFFRACTIONPOSITIONAL0.55
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.35-3.38810.29561360.23411242100
3.3881-3.42790.27981560.2191131199
3.4279-3.46970.29831590.2017126099
3.4697-3.51360.27431460.21231322100
3.5136-3.55980.27831280.1987129699
3.5598-3.60850.26581440.20111279100
3.6085-3.66010.23131430.199132099
3.6601-3.71470.24951470.19431268100
3.7147-3.77270.25921240.19491315100
3.7727-3.83450.22751480.17151295100
3.8345-3.90060.24451380.16221300100
3.9006-3.97140.2311290.1541304100
3.9714-4.04770.22951630.15521312100
4.0477-4.13030.21481460.15421302100
4.1303-4.220.20581430.14641275100
4.22-4.31810.18651500.14621322100
4.3181-4.4260.2011360.14631307100
4.426-4.54550.18751440.13151313100
4.5455-4.67910.18141550.12821287100
4.6791-4.82990.20811480.14811312100
4.8299-5.00220.22331400.15641314100
5.0022-5.20220.26921520.18441309100
5.2022-5.43840.25061420.19051345100
5.4384-5.72450.28411450.21561319100
5.7245-6.08210.34871320.23771344100
6.0821-6.55010.29311400.22251333100
6.5501-7.20620.20611530.17961334100
7.2062-8.24190.19061470.1446134299
8.2419-10.35750.1721690.1485130198
10.3575-41.67670.21951450.2256130691
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)
13.22711.719-3.25842.0822-1.17093.4498-0.30390.1383-0.4554-0.02360.0872-0.320.52240.24060.23040.43140.0502-0.09150.5813-0.04380.4813-73.345248.416-44.273
22.86550.1734-0.33812.89640.16543.09-0.13270.0074-1.2733-0.4907-0.12360.15020.3968-0.00730.31610.75220.06290.16380.5367-0.05430.9257-89.271631.7258-26.7523
33.89090.40261.86527.7907-3.62392.00050.2175-0.1330.63110.72931.76730.22010.2498-0.7669-2.01470.6680.16430.05491.6504-0.11260.8202-39.876755.3156-39.032
43.74030.409-0.87331.0431-1.0195.108-0.0852-1.07320.5487-0.35940.8088-0.51661.07030.9298-0.73811.06690.290.00011.0253-0.29150.8563-24.192345.2843-35.3421
52.57481.11640.44551.71710.03922.06120.2241-0.35560.09190.3006-0.2176-0.12030.03780.02910.00130.4504-0.12560.02440.71150.02890.5262-55.571465.0159-31.0738
67.65711.5348-4.05342.7401-0.24594.8719-0.11330.08920.03420.69030.2667-0.14790.8301-0.2708-0.17830.7824-0.1045-0.15660.585-0.08730.578-86.705647.3018-44.1196
71.5585-0.1196-0.21211.9596-0.32561.39150.0397-0.17390.3488-0.1110.20810.026-0.513-0.0391-0.240.8825-0.20650.05810.69440.00220.78-41.400896.3874-43.8291
81.85890.7507-0.02212.58530.76741.8072-0.0519-0.0351-0.15370.0793-0.13420.31950.0905-0.54190.23680.4278-0.1176-0.0010.82250.07540.5392-67.324567.8519-51.8605
90.97170.70620.19521.51130.40242.4671-0.10140.64090.2707-0.28980.2925-0.1861-0.07340.7516-0.24910.4723-0.11850.03550.91350.02260.5638-50.920869.6079-53.2098
105.39523.66363.60952.47132.78693.529-0.45190.07420.37-0.42340.15990.3349-0.65070.01310.26870.64740.1110.09720.43940.15490.6098-75.943449.03626.0138
115.36330.0589-1.17072.86760.46313.6494-0.20610.680.44760.23580.18190.4326-0.1358-0.52050.07750.4890.2118-0.01720.7773-0.00560.7435-96.437140.5519-13.2973
128.20321.2039-1.54282.81621.98387.4680.40690.1255-0.4084-0.59770.2456-0.18310.0636-0.9256-0.5850.8228-0.1370.04260.71840.00940.6763-55.172677.3242.9254
136.3409-0.53091.86335.2698-0.10366.9230.4684-0.77990.475-0.3266-0.5629-0.8141-0.661-0.52180.13270.8608-0.07140.26050.8184-0.00951.2046-57.304595.6087-0.416
142.36111.57730.35592.5911-0.0951.8496-0.06480.32720.1164-0.2120.0984-0.02980.13550.0118-0.04460.4769-0.02960.02360.68040.08120.4767-52.857358.8097-5.3736
153.54070.2742-0.05694.20590.58733.68850.73660.35130.00980.0131-0.193-0.1957-0.3286-0.9853-0.56070.46980.06920.0810.60330.18870.5579-82.073237.43225.0513
162.389-0.04920.54181.9992-0.51562.0810.1424-0.4957-0.5606-0.11550.1535-0.21550.20230.3471-0.35390.60140.07390.01771.09060.16760.9065-19.174256.52239.2785
171.688-0.9402-0.82951.5434-0.24741.8717-0.2821-0.0598-0.5645-0.1378-0.07430.0128-0.09650.46340.39990.8201-0.2948-0.04870.71860.14720.6529-56.234146.428514.455
181.59940.2692-0.05710.6337-0.07521.59540.2928-0.5638-0.03960.30570.0153-0.1411-0.07030.1733-0.30840.6158-0.145-0.04410.79820.04990.4981-48.173260.151417.099
195.12242.906-2.42338.0336-4.59418.28430.81290.8650.44430.21421.02541.58550.40410.5037-1.91750.91770.1226-0.020.9746-0.04061.3175-39.386338.5764-22.2406
201.80060.8784-0.45742.6330.33442.2870.44120.52270.3941-0.0129-0.4532-0.15980.34950.770.01630.90870.32060.22811.9086-0.23451.0312-24.398654.0962-46.3714
210.3474-0.12390.52450.4635-0.36132.01730.05340.2419-0.37350.015-0.0217-0.23450.210.6998-0.03080.73680.335-0.05061.4984-0.06471.0483-21.567753.4876-23.7789
220.6271.78081.01255.85811.37164.2870.84730.86621.0004-0.30360.3192-0.3112-0.5921-0.006-1.24531.0764-0.05140.22231.24550.15741.2997-68.786185.3175-14.1149
230.17430.00950.1624.37830.35380.1731-0.63230.28650.06010.26740.4404-0.29590.0907-0.32920.21192.0319-0.53560.18871.0406-0.31151.234-49.714691.102911.2587
240.6725-0.6139-0.22370.6664-0.36711.9420.02360.08630.30330.231-0.0695-0.121-0.7740.24160.09271.211-0.18150.13840.65580.04140.952-47.689894.5551-10.847
252.7213-0.3031.02242.61110.75181.10320.17340.07070.68440.3190.1561-0.1108-0.79451.0847-0.44421.0167-0.16490.22891.6039-0.00170.7686-35.20970.8977-33.3788
261.4571-0.7619-0.77252.58950.32691.23490.2269-0.3608-0.1028-0.08810.2987-0.8069-0.49991.229-0.62111.0234-0.1511-0.08161.3202-0.13870.7777-38.720974.4124-1.6141
274.02285.8651-2.03698.5487-2.96971.03090.2921-0.908-0.2775-0.2176-0.2701-0.33350.6537-0.4362-0.03621.22760.0047-0.16312.4739-0.07150.8892-34.160968.2038-23.9948
288.79661.2141.3510.16690.18520.2061-0.18650.92440.2592-0.80790.59250.04010.1431-0.3097-0.3961.24690.1127-0.3412.456-0.00950.8505-40.343776.7034-10.9572
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 343:382 )A343 - 382
2X-RAY DIFFRACTION2( CHAIN A AND RESID 383:429 )A383 - 429
3X-RAY DIFFRACTION3( CHAIN A AND RESID 18:30 )A18 - 30
4X-RAY DIFFRACTION4( CHAIN A AND RESID 3:17 )A3 - 17
5X-RAY DIFFRACTION5( CHAIN A AND RESID 31:154 )A31 - 154
6X-RAY DIFFRACTION6( CHAIN A AND RESID 430:455 )A430 - 455
7X-RAY DIFFRACTION7( CHAIN A AND RESID 239:322 )A239 - 322
8X-RAY DIFFRACTION8( CHAIN A AND RESID 456:482 )A456 - 482
9X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:618 ) )A155 - 238
10X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:618 ) )A323 - 342
11X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:618 ) )A483 - 484
12X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:618 ) )A501
13X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:618 ) )A601 - 618
14X-RAY DIFFRACTION10( CHAIN B AND RESID 343:382 )B343 - 382
15X-RAY DIFFRACTION11( CHAIN B AND RESID 383:429 )B383 - 429
16X-RAY DIFFRACTION12( CHAIN B AND RESID 18:30 )B18 - 30
17X-RAY DIFFRACTION13( CHAIN B AND RESID 3:17 )B3 - 17
18X-RAY DIFFRACTION14( CHAIN B AND RESID 31:154 )B31 - 154
19X-RAY DIFFRACTION15( CHAIN B AND RESID 430:455 )B430 - 455
20X-RAY DIFFRACTION16( CHAIN B AND RESID 239:322 )B239 - 322
21X-RAY DIFFRACTION17( CHAIN B AND RESID 456:482 )B456 - 482
22X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:611 ) )B155 - 238
23X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:611 ) )B323 - 342
24X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:611 ) )B483 - 484
25X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:611 ) )B501
26X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 601:611 ) )B601 - 611
27X-RAY DIFFRACTION19( CHAIN C AND RESID 539:581 )C539 - 581
28X-RAY DIFFRACTION20( CHAIN C AND RESID 610:634 )C610 - 634
29X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:802 ) )C414 - 538
30X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:802 ) )C582 - 609
31X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:802 ) )C635 - 640
32X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:802 ) )C701
33X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:802 ) )C801 - 802
34X-RAY DIFFRACTION22( CHAIN D AND RESID 539:581 )D539 - 581
35X-RAY DIFFRACTION23( CHAIN D AND RESID 610:634 )D610 - 634
36X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 ) )D415 - 538
37X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 ) )D582 - 609
38X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 ) )D635 - 640
39X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 ) )D701
40X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:102 ) ) OR ( CHAIN F AND RESID 1:11 )E9 - 15
41X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:102 ) ) OR ( CHAIN F AND RESID 1:11 )E101 - 102
42X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:102 ) ) OR ( CHAIN F AND RESID 1:11 )F1 - 11
43X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 101:101 ) )H1 - 11
44X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 101:101 ) )G9 - 15
45X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 101:101 ) )G101
46X-RAY DIFFRACTION27( CHAIN A AND RESID 502:502 ) OR ( CHAIN F AND RESID 101:101 )A502
47X-RAY DIFFRACTION27( CHAIN A AND RESID 502:502 ) OR ( CHAIN F AND RESID 101:101 )F101
48X-RAY DIFFRACTION28( CHAIN H AND RESID 101:101 ) OR ( CHAIN B AND RESID 502:502 )H101
49X-RAY DIFFRACTION28( CHAIN H AND RESID 101:101 ) OR ( CHAIN B AND RESID 502:502 )B502

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