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- PDB-3ltn: Inhibitor-stabilized topoisomerase IV-DNA cleavage complex (S. pn... -

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Basic information

Entry
Database: PDB / ID: 3ltn
TitleInhibitor-stabilized topoisomerase IV-DNA cleavage complex (S. pneumoniae)
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 / quinolone / dione / cleaved form / topoisomerase-DNA complex / ISOMERASE-DNA 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-PDQ / 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: 3.1 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
DepositionFeb 16, 2010Deposition 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_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 / _struct_conn.pdbx_leaving_atom_flag / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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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'
F: 3-amino-7-{(3R)-3-[(1S)-1-aminoethyl]pyrrolidin-1-yl}-1-cyclopropyl-6-fluoro-8-methylquinazoline-2,4(1H,3H)-dione
H: 3-amino-7-{(3R)-3-[(1S)-1-aminoethyl]pyrrolidin-1-yl}-1-cyclopropyl-6-fluoro-8-methylquinazoline-2,4(1H,3H)-dione
hetero molecules


Theoretical massNumber of molelcules
Total (without water)195,33912
Polymers194,5688
Non-polymers7714
Water905
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area20410 Å2
ΔGint-101 kcal/mol
Surface area59450 Å2
MethodPISA
Unit cell
Length a, b, c (Å)122.507, 122.507, 178.303
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-IDSelection detailsAuth asym-IDAuth seq-ID
111chain A and (resseq 3:483 ) and (not element H)A0
211chain B and (resseq 3:483 ) and (not element H)B0
112chain C and (resseq 415:487 or resseq 490:494 or resseq...C415 - 487
122chain C and (resseq 415:487 or resseq 490:494 or resseq...C490 - 494
132chain C and (resseq 415:487 or resseq 490:494 or resseq...C496 - 547
142chain C and (resseq 415:487 or resseq 490:494 or resseq...C549 - 640
212chain D and (resseq 415:487 or resseq 490:494 or resseq...D415 - 487
222chain D and (resseq 415:487 or resseq 490:494 or resseq...D490 - 494
232chain D and (resseq 415:487 or resseq 490:494 or resseq...D496 - 547
242chain D and (resseq 415:487 or resseq 490:494 or resseq...D549 - 640

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, Isomerases; Other isomerases; Sole sub-subclass for isomerases that do not belong in the other subclasses
#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, 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(*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 , 3 types, 9 molecules FH

#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#8: Chemical
ChemComp-PDQ / 3-amino-7-{(3R)-3-[(1S)-1-aminoethyl]pyrrolidin-1-yl}-1-cyclopropyl-6-fluoro-8-methylquinazoline-2,4(1H,3H)-dione


Mass: 361.414 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H24FN5O2
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Nonpolymer detailsTHE INHIBITOR CAN BE CALLED AS PD 0305970.

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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: 3.97 Å3/Da / Density % sol: 69.02 %
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: 3.1→50 Å / Num. all: 54325 / Num. obs: 53890 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 5.8 % / Biso Wilson estimate: 98.815 Å2 / Rmerge(I) obs: 0.075 / Rsym value: 0.075 / Net I/σ(I): 17.159
Reflection shellResolution: 3.1→3.21 Å / Redundancy: 5.8 % / Rmerge(I) obs: 0.408 / Mean I/σ(I) obs: 3.563 / Num. unique all: 5435 / Rsym value: 0.408 / % possible all: 100

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Processing

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

3fof


Resolution: 3.1→34.127 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.56 / Isotropic thermal model: Isotropic+TLS / Cross valid method: THROUGHOUT / σ(F): 1.97 / Phase error: 22.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2277 5392 10.02 %Random
Rwork0.186 48447 --
obs0.1902 53839 99.15 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 73.472 Å2 / ksol: 0.248 e/Å3
Displacement parametersBiso max: 365 Å2 / Biso mean: 112.623 Å2 / Biso min: 40.72 Å2
Baniso -1Baniso -2Baniso -3
1--13.7173 Å20 Å20 Å2
2---13.7173 Å20 Å2
3---1.8126 Å2
Refinement stepCycle: LAST / Resolution: 3.1→34.127 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10282 730 54 5 11071
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.02511918
X-RAY DIFFRACTIONf_angle_d1.30815681
X-RAY DIFFRACTIONf_dihedral_angle_d20.0946636
X-RAY DIFFRACTIONf_chiral_restr0.0831786
X-RAY DIFFRACTIONf_plane_restr0.0081921
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3523X-RAY DIFFRACTIONPOSITIONAL0.013
12B3523X-RAY DIFFRACTIONPOSITIONAL0.013
21C1615X-RAY DIFFRACTIONPOSITIONAL0.013
22D1615X-RAY DIFFRACTIONPOSITIONAL0.013
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1001-3.13530.33141800.28051665X-RAY DIFFRACTION100
3.1353-3.17220.28831590.26351597X-RAY DIFFRACTION99
3.1722-3.21080.34281680.26761666X-RAY DIFFRACTION100
3.2108-3.25150.34071800.24791583X-RAY DIFFRACTION100
3.2515-3.29420.23021940.21921666X-RAY DIFFRACTION100
3.2942-3.33930.27141640.21061633X-RAY DIFFRACTION100
3.3393-3.3870.26931690.21571642X-RAY DIFFRACTION100
3.387-3.43750.28341850.2161610X-RAY DIFFRACTION100
3.4375-3.49110.25331760.21351685X-RAY DIFFRACTION100
3.4911-3.54830.26741690.2051607X-RAY DIFFRACTION100
3.5483-3.60940.27251700.22281652X-RAY DIFFRACTION100
3.6094-3.6750.32191700.22671605X-RAY DIFFRACTION100
3.675-3.74560.23121690.19591639X-RAY DIFFRACTION100
3.7456-3.82190.22992030.17931608X-RAY DIFFRACTION100
3.8219-3.90490.22831940.15951620X-RAY DIFFRACTION100
3.9049-3.99560.18361900.15051599X-RAY DIFFRACTION100
3.9956-4.09540.20921820.16561654X-RAY DIFFRACTION100
4.0954-4.20590.20911890.16721634X-RAY DIFFRACTION100
4.2059-4.32950.20041940.15621620X-RAY DIFFRACTION100
4.3295-4.46890.18141750.13781597X-RAY DIFFRACTION100
4.4689-4.62830.1511950.12361603X-RAY DIFFRACTION100
4.6283-4.81310.17912110.1331632X-RAY DIFFRACTION100
4.8131-5.03150.19671810.14941612X-RAY DIFFRACTION100
5.0315-5.29580.20831770.16831641X-RAY DIFFRACTION100
5.2958-5.62630.23131800.17671616X-RAY DIFFRACTION100
5.6263-6.05850.21721890.18821633X-RAY DIFFRACTION100
6.0585-6.66410.20171820.18311588X-RAY DIFFRACTION100
6.6641-7.6190.21981640.18361652X-RAY DIFFRACTION100
7.619-9.5640.19542000.17291614X-RAY DIFFRACTION100
9.564-34.12880.26031330.21661274X-RAY DIFFRACTION78
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)
1-0.1099-0.9254-0.1479-1.2882.2030.3445-0.17-0.145-0.38610.435-0.3739-0.35380.3380.09440.57620.951-0.08880.25190.4020.36390.7531-16.42432.26578.0716
22.1877-0.61390.52830.8392-0.0105-0.9372-0.3902-0.3685-0.1212-0.13580.11640.0282-0.452-0.03460.2630.6452-0.461-0.13090.66430.0540.2241-22.20250.696329.356
3-1.9107-9.9384-0.80516.4621-0.56073.36340.1118-1.4578-1.23030.19950.16741.9723-1.0303-2.2193-0.30520.28090.09380.14961.00030.28920.7362-8.121842.6117-24.3738
4-0.5673-1.4021-1.2909-0.4330.66852.462-0.60531.86760.47030.19420.31630.2470.41860.38030.24620.4719-0.11970.04791.53310.13350.44284.18554.6491-31.4611
52.4261-0.9404-0.63571.34110.53752.0211-0.20940.5492-0.35110.0256-0.2350.35930.0513-0.15490.43810.4152-0.18240.18940.73-0.04350.4678-26.712640.5543-16.6498
63.2167-2.5342-3.00331.15464.65266.0011-0.8789-0.5453-0.6670.54870.34790.57161.14980.61780.4981.3056-0.28210.07630.54440.36020.5496-22.434729.724519.9637
7-1.4213-0.46970.50830.6953-1.3184-0.92990.16460.12810.4339-0.2047-0.22680.04690.0352-0.27320.17320.8087-0.20130.22641.4091-0.78380.9384-36.138218.4641-44.7392
80.55540.12180.0252-0.7531.16070.17780.01250.0983-0.76720.9056-0.6160.15521.38390.07670.65961.2312-0.1160.39280.5198-0.15110.8302-23.049918.4417-8.0975
93.7062-0.72132.04232.65472.62532.0947-0.11720.6893-0.71040.5955-0.1463-0.00990.52520.65980.21480.75170.08430.3970.7518-0.19490.6452-15.693520.8097-21.9531
10-0.2144-0.99910.2372-1.0507-2.1006-0.3369-0.0958-0.13840.3670.5525-0.44030.44-0.5035-0.15210.60380.9982-0.0516-0.25060.4141-0.36940.7401-44.840573.83668.0707
112.638-0.4748-0.6011.12390.0367-0.6225-0.5334-0.50350.1385-0.33910.24540.00540.44350.06010.23180.6196-0.440.11920.648-0.050.2066-39.061755.410829.3601
12-3.4886-6.3834-0.46162.98421.15317.17970.0499-1.81851.15450.068-0.0621-1.29030.80192.0006-0.02050.29220.0871-0.19710.9701-0.29630.7912-53.135663.4822-24.3739
13-0.0921-0.59170.4983-0.2587-0.71771.4562-0.48271.6883-0.27720.61170.2944-0.2875-0.3523-0.27040.02770.4634-0.1069-0.05091.5689-0.11370.3569-65.441551.4409-31.4598
142.4689-0.79161.01831.5446-0.57761.923-0.23070.55410.3440.0227-0.2201-0.4057-0.03990.23970.4480.398-0.17-0.19770.73710.05410.456-34.546565.5443-16.6489
153.9395-2.57693.36041.0508-3.65715.7167-0.9875-0.65120.58270.74340.3152-0.4879-1.0342-0.70750.61051.3052-0.332-0.1150.5354-0.25510.525-38.832176.38119.963
16-0.9507-0.4259-0.5081.68510.4523-0.15860.33780.0316-0.2508-0.2776-0.3343-0.22830.22360.21090.14630.778-0.1576-0.17391.44580.8270.9344-25.047587.5756-44.7651
170.43530.22110.3598-2.0323-1.9316-0.24750.22450.09020.95880.9046-0.6969-0.187-1.3152-0.06930.46721.3614-0.151-0.34420.46380.15370.8458-38.216387.6574-8.1001
183.1467-0.0434-1.49682.6612-2.39042.062-0.04580.74360.64190.5434-0.137-0.04-0.4568-0.65660.14680.70820.1041-0.38320.74480.17550.6694-45.569785.2851-21.9563
192.8727-2.1832-1.43031.43761.26943.6106-1.1251-0.58890.69220.23690.5976-0.17570.18932.18680.50580.7185-0.278-0.12381.84990.17730.7128-8.22667.1646-13.6192
200.5472-1.6761.1750.22510.62364.05870.14370.4289-0.4096-0.1464-0.32460.0779-0.60661.2810.07890.3840.14360.27911.53890.03680.29394.231241.2574-36.7328
210.7673-0.73720.03441.04710.29141.04960.00190.54390.442-0.0431-0.2492-0.2645-0.03030.18670.22750.2267-0.19360.10431.23860.43580.5132-6.197260.9583-38.7799
222.081-0.49261.2510.5757-0.21753.1356-0.8684-0.4746-0.41130.48140.12680.1744-0.649-1.51090.73910.7091-0.20370.14721.5685-0.15450.6366-53.035838.9367-13.6112
23-0.2278-1.8283-2.94090.1563-0.63264.20930.14850.39090.5112-0.031-0.4239-0.01560.4791-1.43680.21470.40040.1796-0.28281.6096-0.04760.3811-65.498564.8339-36.7331
240.3134-0.5997-0.42591.1026-0.24470.9557-0.03360.4389-0.3742-0.0645-0.24070.30590.031-0.29980.18920.2412-0.2176-0.11651.2866-0.4120.5269-55.069345.1334-38.7726
252.18941.5686-0.99520.7255-0.6482-1.04310.12591.7923-0.4267-0.2202-0.58470.53150.1282-0.43150.43810.5331-0.00630.22391.669-0.28680.6821-20.027841.0545-37.2389
260.73321.2346-0.05861.58350.9165-1.4770.15861.67250.197-0.2543-0.4499-0.5611-0.19330.41290.27490.5468-0.0689-0.24991.61880.26190.5687-41.256365.0221-37.2328
27-2.5017-1.98040.32781.0542.36518.97270.0030.151-0.8804-0.16391.4610.6107-0.3881-0.0543-1.28550.754-0.2734-0.06141.6719-0.00550.9434-22.061551.1147-38.1228
281.97181.93370.59022.8989-2.04443.180.23121.121-0.2102-0.2760.7892-0.36630.19320.0999-0.84290.6405-0.13820.17881.87360.3810.8477-39.204254.9457-37.9926
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) and not resname HOHA0
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) and not resname HOHB0
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) and not resname HOHD0
25X-RAY DIFFRACTION25chain E or chain F and not resid 0E9 - 15
26X-RAY DIFFRACTION25chain E or chain F and not resid 0F1 - 11
27X-RAY DIFFRACTION26chain G or chain H and not resid 0G9 - 15
28X-RAY DIFFRACTION26chain G or chain H and not resid 0H1 - 11
29X-RAY DIFFRACTION27chain F and resid 0F0
30X-RAY DIFFRACTION28chain H and resid 0F0 - 20

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