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- PDB-3rae: Quinolone(Levofloxacin)-DNA cleavage complex of type IV topoisome... -

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Basic information

Entry
Database: PDB / ID: 3rae
TitleQuinolone(Levofloxacin)-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 / Levofloxacin / ISOMERASE-DNA-ANTIBIOTIC 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
Chem-LFX / 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: 2.9 Å
AuthorsLaponogov, I. / Pan, X.-S. / Veselkov, D.A. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
CitationJournal: Acta Crystallogr.,Sect.D / Year: 2016
Title: Structure of a quinolone-stabilized cleavage complex of topoisomerase IV from Klebsiella pneumoniae and comparison with a related Streptococcus pneumoniae complex.
Authors: Veselkov, D.A. / Laponogov, I. / Pan, X.S. / Selvarajah, J. / Skamrova, G.B. / Branstrom, A. / Narasimhan, J. / Prasad, J.V. / 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 1.1Apr 20, 2016Group: Database references
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_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_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)185,55216
Polymers184,6848
Non-polymers8698
Water97354
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area19570 Å2
ΔGint-121 kcal/mol
Surface area57380 Å2
MethodPISA
Unit cell
Length a, b, c (Å)157.831, 157.831, 211.147
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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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, EC: 5.99.1.-
#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, EC: 5.99.1.-

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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
#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
#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
#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

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Non-polymers , 3 types, 62 molecules

#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-LFX / (3S)-9-fluoro-3-methyl-10-(4-methylpiperazin-1-yl)-7-oxo-2,3-dihydro-7H-[1,4]oxazino[2,3,4-ij]quinoline-6-carboxylic acid / Levofloxacin


Mass: 361.368 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C18H20FN3O4 / Comment: medication, antibiotic*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 54 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 4.11 Å3/Da / Density % sol: 70.08 %
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: 2.6→50 Å / Num. all: 94010 / Num. obs: 93164 / % possible obs: 99.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.5 % / Biso Wilson estimate: 71.22 Å2 / Rmerge(I) obs: 0.085 / Rsym value: 0.085 / Net I/σ(I): 13.789
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allRsym value% possible all
2.6-2.693.50.841.288380.8495.3
2.69-2.84.20.7691.7592960.76999.7
2.8-2.934.60.6242.5693280.62499.8
2.93-3.084.70.394.192720.3999.8
3.08-3.284.70.2316.6993090.23199.9
3.28-3.534.70.13710.6293610.13799.9
3.53-3.884.70.08814.593830.08899.9
3.88-4.454.60.06416.4994060.06499.9
4.45-5.64.60.06417.494920.06499.9
5.6-504.40.03622.9194790.03696.7

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Processing

Software
NameVersionClassification
GDEdata collection
PHASERphasing
PHENIX(phenix.refine: 1.6.1_357)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3K9F

3k9f


Resolution: 2.9→41.832 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.21 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2264 6838 10.13 %Random
Rwork0.1857 ---
obs0.1899 67471 99.45 %-
all-67471 --
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 37.674 Å2 / ksol: 0.277 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-6.8001 Å2-0 Å2-0 Å2
2--6.8001 Å20 Å2
3----13.6002 Å2
Refinement stepCycle: LAST / Resolution: 2.9→41.832 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10338 730 58 54 11180
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00811450
X-RAY DIFFRACTIONf_angle_d1.22115654
X-RAY DIFFRACTIONf_dihedral_angle_d16.8394178
X-RAY DIFFRACTIONf_chiral_restr0.0771789
X-RAY DIFFRACTIONf_plane_restr0.0061919
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 (%)
2.9-2.9330.35622180.28061992100
2.933-2.96750.32852190.26412026100
2.9675-3.00360.31912050.2472026100
3.0036-3.04170.33352170.25872011100
3.0417-3.08170.31452250.24881997100
3.0817-3.12390.29392250.23691999100
3.1239-3.16850.29112210.22872043100
3.1685-3.21580.28212250.23472029100
3.2158-3.2660.32252230.22761977100
3.266-3.31950.28172070.21322026100
3.3195-3.37670.24332320.20282018100
3.3767-3.43810.24612480.19221978100
3.4381-3.50420.24962320.18882040100
3.5042-3.57570.23782380.17541998100
3.5757-3.65340.25572030.1812038100
3.6534-3.73830.2292220.1862000100
3.7383-3.83180.24322320.1752041100
3.8318-3.93530.2112370.16252010100
3.9353-4.0510.19872210.16162038100
4.051-4.18160.2112230.15762023100
4.1816-4.33090.18582220.15262029100
4.3309-4.50410.20022500.13452012100
4.5041-4.70890.15942390.13632024100
4.7089-4.95680.17662090.152064100
4.9568-5.26680.19562330.162051100
5.2668-5.67250.20612470.17532019100
5.6725-6.24170.24422310.18722059100
6.2417-7.1410.20622500.17782057100
7.141-8.98220.16692400.155207499
8.9822-41.83680.19512440.1854193489
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)
10.81060.6757-1.120.1787-0.7380.6788-0.29080.2101-0.155-0.26140.0966-0.11530.3370.06050.07750.3193-0.0225-0.03130.2921-0.07970.1715-73.844548.7928-44.4221
22.23010.6242-0.95090.9559-1.62452.8796-0.2107-0.0241-0.7337-0.1351-0.1935-0.10420.22670.10040.35670.35830.07540.13630.2286-0.0380.418-89.813531.8663-27.1307
38.48482.3161-5.65.5679-1.65235.6109-0.42350.08850.57210.29671.1560.45370.4665-0.6233-0.60580.45620.0787-0.03030.8124-0.07860.3933-40.31355.672-39.2327
41.89170.9928-0.50781.05530.39771.9511-0.25460.23470.561-0.47410.56170.01150.37610.5508-0.1180.61620.4707-0.22180.844-0.3290.6915-24.476645.2937-35.4535
50.92960.30240.03661.0373-0.79081.28060.2003-0.21840.06460.1367-0.14480.0156-0.05020.1223-0.0370.3139-0.12780.00830.48050.00590.2213-55.902465.4226-31.0608
60.3564-0.45660.47470.7679-1.02722.1674-0.2193-0.09190.18260.55780.48480.09880.3273-0.6073-0.09770.6454-0.0435-0.08950.3649-0.08940.2612-87.178747.6201-44.347
71.59330.94330.18451.3667-0.70680.87890.22820.05260.21570.2004-0.04630.1887-0.41430.0412-0.14060.6836-0.2050.07380.40710.02380.3925-41.579296.7635-43.7879
80.76010.48890.93311.92581.58451.899-0.27720.16720.1726-0.2092-0.00610.3983-0.0541-0.33080.16160.1793-0.1239-0.01120.63570.08120.2124-67.768268.2976-52.0652
90.50980.5084-0.40951.8084-0.55051.9683-0.12270.53330.0386-0.2460.2231-0.10850.05620.4274-0.07560.2497-0.11420.02070.60890.0320.2037-51.301269.9592-53.3828
101.14810.50270.47840.3659-0.04570.7880.0026-0.31370.1519-0.0782-0.15860.105-0.4135-0.07080.00320.28080.12020.10380.38970.06810.2205-76.447849.06325.7489
111.0242-0.12230.49950.55950.29510.6938-0.15360.17650.0675-0.07850.14830.2307-0.1461-0.042-0.0050.28330.1630.01620.3360.02370.3042-96.967240.4916-13.5724
122.622-1.8399-2.57617.8327-0.88123.62180.1090.42030.2093-1.27860.22220.09610.2233-1.4618-0.33780.7409-0.09590.0260.71930.01450.5092-55.611477.3342.7725
132.76550.5782-0.07430.2290.86236.91720.1178-0.55160.04850.20070.43760.1939-1.4242-0.5274-0.66660.80650.04730.26530.54660.02530.7772-57.743395.6185-0.4725
141.32110.468-0.00280.96860.0042.1627-0.09270.1115-0.0188-0.04110.163-0.00780.0813-0.028-0.06930.2495-0.0798-0.01270.49340.03780.2286-53.151258.9264-5.7374
150.45380.02270.9321.19970.24982.30130.728-0.0652-0.2303-0.1077-0.2196-0.51860.0402-0.5012-0.12470.1640.07680.04160.41510.15630.2097-82.501437.48334.769
160.0773-0.11970.32761.88990.33982.00270.2175-0.0567-0.39430.01980.1094-0.15970.12120.1746-0.28020.24140.0198-0.07620.67760.05250.5097-19.538256.55149.1751
170.8967-0.17560.01070.13520.42821.7857-0.27110.33690.11140.31640.0155-0.02150.3177-0.03560.19980.3648-0.17-0.06870.36670.13560.1208-56.882346.312814.2409
180.9861-0.09730.19850.0699-0.41331.88580.1643-0.55420.02190.24-0.0415-0.0405-0.41360.2031-0.06750.4683-0.1086-0.05790.65050.05770.2781-48.726360.075216.7173
195.1357.04823.29099.66554.51712.10470.35460.65160.77820.3682-0.29231.28561.6390.0771-0.24260.9854-0.0289-0.12890.8499-0.20540.9571-39.988938.8791-22.7165
200.8243-0.48050.83410.8638-1.08961.61690.46231.6031-0.40770.0515-0.716-0.34710.25811.26070.15470.40040.39650.1121.6424-0.18410.4356-24.591654.3597-46.3296
210.2021-0.26660.9650.8127-0.83442.88860.27890.6239-0.09970.0522-0.3428-0.2040.26140.93590.05950.19220.2716-0.02811.0393-0.07130.3484-22.046753.6001-23.9031
223.5953.1963-2.09814.3262-0.34512.78540.63732.16860.5070.27750.3649-0.1393-0.0118-0.0768-0.62990.7548-0.05970.13941.10280.01391.0378-69.441285.2137-14.6135
232.4384-1.1501-1.11925.48023.40892.2123-0.3133-0.87220.34731.29620.3192-0.1371-0.08830.34510.08411.4032-0.32870.13190.3622-0.15340.3605-50.302191.448211.116
240.5029-0.4289-0.19750.559-0.46791.94990.05620.12150.21120.4060.02510.0616-0.7634-0.0526-0.07990.9279-0.15610.13630.3044-0.00720.5063-48.156694.6877-11.0373
253.1117-1.03281.33342.9987-0.4290.52570.16080.08120.34810.04940.2118-0.1282-0.42170.2609-0.11430.5828-0.14360.20351.0434-0.01130.2508-35.549471.1092-33.4824
261.4989-0.5078-0.35533.1634-1.17740.55220.2848-0.6119-0.0346-0.16940.4167-0.60090.00290.2342-0.3060.5692-0.1656-0.06880.7389-0.22080.3017-39.058774.4913-1.6616
271.7639-0.90623.26791.0037-2.59177.8425-0.2468-0.56910.46810.12910.3685-0.16882.0894-1.6350.05620.82440.07580.00371.622-0.4750.7788-34.238168.5347-24.0716
280.30550.35350.35381.69291.7912.4310.0176-0.04090.12130.9016-0.8495-0.22971.4215-1.28130.54881.2724-0.27220.14151.243-0.33370.9334-40.131277.4007-11.1377
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 801:823 ) )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 801:823 ) )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 801:823 ) )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 801:823 ) )A501
13X-RAY DIFFRACTION9( CHAIN A AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 501:501 OR RESID 801:823 ) )A801 - 823
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 700:700 OR RESID 801:821 ) )B155 - 238
23X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 700:700 OR RESID 801:821 ) )B323 - 342
24X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 700:700 OR RESID 801:821 ) )B483 - 484
25X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 700:700 OR RESID 801:821 ) )B700
26X-RAY DIFFRACTION18( CHAIN B AND ( RESID 155:238 OR RESID 323:342 OR RESID 483:484 OR RESID 700:700 OR RESID 801:821 ) )B801 - 821
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 801:801 ) )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 801:801 ) )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 801:801 ) )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 801:801 ) )C701
33X-RAY DIFFRACTION21( CHAIN C AND ( RESID 414:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:801 ) )C801
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 OR RESID 801:803 ) )D415 - 538
37X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:803 ) )D582 - 609
38X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:803 ) )D635 - 640
39X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:803 ) )D701
40X-RAY DIFFRACTION24( CHAIN D AND ( RESID 415:538 OR RESID 582:609 OR RESID 635:640 OR RESID 701:701 OR RESID 801:803 ) )D801 - 803
41X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:104 ) ) OR ( CHAIN F AND RESID 1:11 )E9 - 15
42X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:104 ) ) OR ( CHAIN F AND RESID 1:11 )E101 - 104
43X-RAY DIFFRACTION25( CHAIN E AND ( RESID 9:15 OR RESID 101:104 ) ) OR ( CHAIN F AND RESID 1:11 )F1 - 11
44X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 201:202 ) )H1 - 11
45X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 201:202 ) )G9 - 15
46X-RAY DIFFRACTION26( CHAIN H AND RESID 1:11 ) OR ( CHAIN G AND ( RESID 9:15 OR RESID 201:202 ) )G201 - 202
47X-RAY DIFFRACTION27( CHAIN A AND RESID 502:502 ) OR ( CHAIN F AND RESID 101:101 )A502
48X-RAY DIFFRACTION27( CHAIN A AND RESID 502:502 ) OR ( CHAIN F AND RESID 101:101 )F101
49X-RAY DIFFRACTION28( CHAIN H AND RESID 101:101 ) OR ( CHAIN G AND RESID 101:101 )H101
50X-RAY DIFFRACTION28( CHAIN H AND RESID 101:101 ) OR ( CHAIN G AND RESID 101:101 )G101

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