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- PDB-3fof: Structural insight into the quinolone-DNA cleavage complex of typ... -

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Basic information

Entry
Database: PDB / ID: 3fof
TitleStructural insight into the quinolone-DNA cleavage complex of type IIA topoisomerases
Components
  • (DNA topoisomerase 4 subunit ...) x 2
  • DNA (5'-D(P*AP*CP*CP*AP*AP*GP*GP*TP*CP*AP*TP*GP*AP*AP*T)-3')
  • DNA (5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3')
  • DNA (5'-D(P*CP*TP*GP*TP*TP*TP*TP*AP*CP*GP*TP*GP*CP*AP*T)-3')
  • DNA (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 / quinolone / topoisomerase / DNA / protein-DNA cleavage complex / Streptococcus pneumoniae / moxifloxacin / Cell membrane / DNA-binding / Isomerase / Membrane / ATP-binding / Nucleotide-binding / 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 / Topoisomerase II; domain 5 / Topoisomerase II, domain 5 / Topoisomerase, domain 3 / Topoisomerase; domain 3 / Rossmann fold - #670 / Gyrase A; domain 2 - #40 / DNA gyrase/topoisomerase IV, subunit A, C-terminal repeat / DNA gyrase/topoisomerase IV, subunit A, C-terminal ...DNA topoisomerase IV subunit A, Gram-positive / DNA topoisomerase 4 subunit B, Firmicutes/Mollicutes / Topoisomerase II; domain 5 / Topoisomerase II, domain 5 / Topoisomerase, domain 3 / Topoisomerase; domain 3 / Rossmann fold - #670 / Gyrase A; domain 2 - #40 / 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 / Gyrase A; domain 2 / 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 / Alpha-Beta Complex / Rossmann fold / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-MFX / 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: 4 Å
AuthorsLaponogov, I. / Sohi, M.K. / Veselkov, D.A. / Pan, X.-S. / Sawhney, R. / Thompson, A.W. / McAuley, K.E. / Fisher, L.M. / Sanderson, M.R.
CitationJournal: 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
DepositionDec 30, 2008Deposition site: RCSB / Processing site: PDBJ
Revision 1.0Feb 24, 2009Provider: 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_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_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: DNA (5'-D(P*AP*CP*CP*AP*AP*GP*GP*TP*CP*AP*TP*GP*AP*AP*T)-3')
F: DNA (5'-D(P*AP*GP*TP*CP*AP*TP*TP*CP*AP*TP*GP*AP*CP*CP*TP*TP*GP*GP*T)-3')
G: DNA (5'-D(P*CP*TP*GP*TP*TP*TP*TP*AP*CP*GP*TP*GP*CP*AP*T)-3')
H: DNA (5'-D(P*GP*AP*CP*TP*AP*TP*GP*CP*AP*CP*GP*TP*AP*AP*AP*AP*CP*AP*G)-3')
F: 1-cyclopropyl-6-fluoro-8-methoxy-7-[(4aS,7aS)-octahydro-6H-pyrrolo[3,4-b]pyridin-6-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
H: 1-cyclopropyl-6-fluoro-8-methoxy-7-[(4aS,7aS)-octahydro-6H-pyrrolo[3,4-b]pyridin-6-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid
hetero molecules


Theoretical massNumber of molelcules
Total (without water)195,37110
Polymers194,5688
Non-polymers8032
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14040 Å2
ΔGint-119 kcal/mol
Surface area79350 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.601, 121.601, 178.699
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
11chain A and (resseq 5:53 or resseq 56:165 or resseq...
21chain B and (resseq 5:53 or resseq 56:165 or resseq...
12chain C and (resseq 417:421 or resseq 423:443 or resseq...
22chain D and (resseq 417:421 or resseq 423:443 or resseq...

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLNGLNLEULEUAA5 - 4795 - 479
21GLNGLNLEULEUBB5 - 4795 - 479
12THRTHRASNASNCC417 - 63638 - 257
22THRTHRASNASNDD417 - 63638 - 257

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) / Gene: parC, SP_0855 / 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) / Gene: parE, SP_0852 / 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 DNA (5'-D(P*AP*CP*CP*AP*AP*GP*GP*TP*CP*AP*TP*GP*AP*AP*T)-3')


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


Mass: 4565.968 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: E-site DNA / References: PDB-3FOE
#6: DNA chain DNA (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 DNA / References: PDB-3FOE

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Non-polymers , 1 types, 2 molecules FH

#7: Chemical
ChemComp-MFX / 1-cyclopropyl-6-fluoro-8-methoxy-7-[(4aS,7aS)-octahydro-6H-pyrrolo[3,4-b]pyridin-6-yl]-4-oxo-1,4-dihydroquinoline-3-carboxylic acid / moxifloxacin


Mass: 401.431 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C21H24FN3O4

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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: 3.92 Å3/Da / Density % sol: 68.63 %
Crystal growTemperature: 295 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 50mM Na cacodylate, 100mM Ammonium acetate, 15mM Magnesium acetate, 7.5% isopropanol, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 295K
Components of the solutions
IDNameCrystal-IDSol-ID
1Na cacodylate11
2Ammonium acetate11
3Magnesium acetate11
4isopropanol11
5Na cacodylate12
6Ammonium acetate12
7Magnesium acetate12

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 27, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 3.2→34.067 Å / Num. obs: 44580 / Biso Wilson estimate: 178.14 Å2

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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 ENTRIES 2NOV and 2RGR

2nov

2rgr


Resolution: 4→34.066 Å / Occupancy max: 1 / Occupancy min: 1 / SU ML: 0.6 / Cross valid method: THROUGHOUT / σ(F): 1.98 / Phase error: 28.67 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2892 2492 10.1 %random
Rwork0.239 22193 --
obs0.2441 24685 98.92 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 150.002 Å2 / ksol: 0.185 e/Å3
Displacement parametersBiso max: 638.86 Å2 / Biso mean: 198.798 Å2 / Biso min: 44.54 Å2
Baniso -1Baniso -2Baniso -3
1--7.561 Å20 Å2-0 Å2
2---7.561 Å20 Å2
3----11.421 Å2
Refinement stepCycle: LAST / Resolution: 4→34.066 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms7020 1374 104 0 8498
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0088909
X-RAY DIFFRACTIONf_angle_d1.20812589
X-RAY DIFFRACTIONf_chiral_restr0.0511488
X-RAY DIFFRACTIONf_plane_restr0.0121471
X-RAY DIFFRACTIONf_dihedral_angle_d17.9182472
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A2427X-RAY DIFFRACTIONPOSITIONAL
12B2427X-RAY DIFFRACTIONPOSITIONAL0.047
21C980X-RAY DIFFRACTIONPOSITIONAL
22D980X-RAY DIFFRACTIONPOSITIONAL0.061
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.0001-4.07690.31081490.26871279X-RAY DIFFRACTION100
4.0769-4.160.3141600.25091202X-RAY DIFFRACTION100
4.16-4.25030.30151330.23031264X-RAY DIFFRACTION100
4.2503-4.3490.26741510.22131235X-RAY DIFFRACTION100
4.349-4.45750.27871330.22051246X-RAY DIFFRACTION100
4.4575-4.57780.28211360.21081246X-RAY DIFFRACTION100
4.5778-4.71210.25941420.21321261X-RAY DIFFRACTION100
4.7121-4.86380.2341150.19761276X-RAY DIFFRACTION100
4.8638-5.03710.26171530.21721235X-RAY DIFFRACTION100
5.0371-5.23810.28931400.23461221X-RAY DIFFRACTION100
5.2381-5.47560.2981390.25081235X-RAY DIFFRACTION100
5.4756-5.7630.36131320.26991272X-RAY DIFFRACTION100
5.763-6.12210.37741520.2871225X-RAY DIFFRACTION100
6.1221-6.59160.31951510.28961239X-RAY DIFFRACTION100
6.5916-7.24920.31291310.24721260X-RAY DIFFRACTION100
7.2492-8.2850.23181270.21681233X-RAY DIFFRACTION100
8.285-10.38880.23511370.17821253X-RAY DIFFRACTION99
10.3888-34.06680.29861110.26321011X-RAY DIFFRACTION81
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)
10.80330.9231-1.34583.1989-0.84371.86360.022-0.0211-0.58280.3214-0.9026-0.49130.00150.35590.92880.5972-0.25930.83220.22350.96380.6875-15.610231.8828.4771
2-0.3350.11020.7114-0.04071.2406-2.3992-0.44790.28430.2572-0.26190.003-0.026-1.02471.46190.26140.1699-1.1675-0.29331.54280.07430.0321-21.688150.619830.8215
3-4.9397-1.51730.57752.554-1.42140.7405-0.50910.5922-0.26140.17950.76690.8655-0.1395-1.3321-0.35520.5780.87590.58592.11271.13411.1187-4.926443.3251-25.2525
4-8.0854-4.33652.0456.05881.62520.5729-0.8233-0.48620.08220.1201-0.85682.21310.04090.49791.70110.68090.22020.34450.98170.20451.59186.528856.057-31.3621
53.2395-1.1508-0.68751.22391.90492.7451-1.13880.7135-1.07190.2174-0.32051.18460.0101-0.05181.39670.3452-0.23350.27030.3674-0.06051.0421-25.987440.3513-15.8728
6-2.58880.4584-0.64590.7676-1.16764.63540.36480.07890.1680.0993-2.0814-1.3393-0.112.23721.67430.9142-0.02320.07382.26811.51141.2812-20.369128.570620.0143
78.44775.36383.95499.76463.96082.56661.2791-1.4191.0327-1.3694-0.3472-1.2282-0.4275-0.3452-0.88081.2415-0.26260.83621.2641-0.14061.6177-34.993616.5435-44.3997
80.49914.4890.42762.01966.39640.27050.219-0.0901-0.52761.63360.0210.25950.81860.0162-0.2661.7913-0.19830.60770.86530.30431.9433-23.69618.4326-5.075
90.604-1.1132-0.4112.147-0.99411.9452-0.54440.1487-0.61221.6113-0.54460.76740.47250.10781.11771.6231-0.06681.02420.51820.01920.7526-15.87518.6774-20.0404
10-0.13970.44670.37894.15490.53380.9942-0.2144-0.2505-0.0940.6569-0.45460.33310.1016-0.28180.43670.29310.0513-0.8214-0.5741-1.52420.3778-45.158173.41288.4778
110.51040.6183-1.71020.3209-1.804-0.0747-0.77690.6019-0.2604-0.46130.28190.05931.1395-1.61380.25630.4552-1.00950.32061.27580.1525-0.3208-39.151954.564930.521
120.0101-0.39410.55-0.2772-0.15240.3804-0.3127-0.54010.4955-0.0392-0.0762-0.0148-0.0148-0.18180.33120.38821.187-1.01381.8492-1.39031.2251-55.941361.7837-25.7459
131.1376-4.04671.28654.2143-0.40921.7037-1.2483-1.14260.7782-0.0941-0.4316-0.7156-0.1593-0.79011.63120.96410.269-0.32311.0698-0.34361.2757-67.329749.2469-31.351
140.78060.01320.11851.3339-1.54522.4366-0.96170.51690.53050.0829-0.3952-1.0750.0352-0.12421.18180.2612-0.2217-0.38840.38660.08451.0593-34.84164.9615-15.8228
15-0.96610.098-1.96542.81082.57420.55590.59340.1256-0.13310.4052-1.63030.80310.1128-1.66331.05170.8085-0.0463-0.0782.084-1.26060.8187-40.393776.729920.0119
16-3.1113-1.4970.58683.0086-1.482.56560.8817-0.6164-1.0364-0.2237-0.8113-0.854-0.20560.30350.03781.2156-0.3738-0.77981.51060.32332.167-25.569288.7202-44.7324
174.2743-0.9535-3.70693.88830.36142.99640.503-0.02130.06932.89430.057-0.9095-0.3058-0.1106-0.5792.0144-0.1522-0.25910.8377-0.44611.5002-37.09486.8614-5.0839
180.5822-0.98750.96433.4740.50040.514-0.37950.16340.63082.1059-0.6095-1.0919-0.9766-0.15231.04631.59310.0059-0.99860.4065-0.0220.7493-44.93986.586-19.7203
19-2.41231.16448.36514.1504-1.02392.9236-0.28060.84390.1161.06041.14730.264-0.67353.4775-0.79161.5555-0.1560.83072.2794-0.07491.1992-7.095965.6835-12.5935
20-0.02380.5461-0.33190.22120.31640.5845-0.26351.4143-0.3197-0.1280.30750.07820.0923-0.6845-0.05670.03830.34171.00712.02540.27710.28053.83139.51-36.0933
210.25120.23360.55780.6065-0.18040.42350.13620.8043-0.099-0.0508-0.03160.566-0.24680.77920.01130.383-0.17480.14061.58820.51510.6121-6.05759.0369-38.6769
226.56820.0201-1.1124-0.80230.7658-0.6489-0.15742.183-0.83330.09421.0078-0.22210.0070.918-0.80821.2851-0.3634-0.32571.9331-0.34491.4592-53.774939.6894-12.7049
237.30212.29336.3246-0.0131.56674.879-0.35412.8160.4651-0.05030.4066-0.20890.01313.1272-0.0068-0.33260.4339-1.02171.8945-0.18-0.0693-64.663265.8147-35.9947
24-0.4860.1034-0.21081.5016-0.03060.39690.09060.62620.1714-0.0213-0.0262-0.85820.223-0.6789-0.00090.3968-0.18370.03391.5491-0.49730.686-54.639945.7493-38.3653
251.29660.46341.5041-1.7797-0.54977.15670.38631.19350.5147-0.63660.30740.07992.6711.2203-0.57841.5753-0.62970.09921.62510.00290.5355-16.883833.4132-45.5821
263.00561.8862-0.2004-0.16080.21966.47370.37891.1098-0.6838-0.7368-0.0343-0.1952-2.3712-1.0876-0.31911.689-0.1893-0.0181.6263-0.16310.5203-43.865771.8259-45.6433
271.40360.91282.25140.07180.19150.5534-0.31450.14260.10240.0178-0.52570.35440.0027-1.15250.8331.5404-0.1442-0.62333.183-1.71914.1381-38.029655.5254-33.8058
28-3.5325-1.89493.69990.1301-0.29531.0518-0.17060.27530.01860.00480.35650.5232-0.01440.1997-0.18551.7909-0.3601-0.12293.93671.8772.8075-22.624849.8571-34.3225
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resseq 343:382
2X-RAY DIFFRACTION2chain A and resseq 383:429
3X-RAY DIFFRACTION3chain A and resseq 18:30
4X-RAY DIFFRACTION4chain A and resseq 5:17
5X-RAY DIFFRACTION5chain A and resseq 31:154
6X-RAY DIFFRACTION6chain A and resseq 430:455
7X-RAY DIFFRACTION7chain A and resseq 239:322
8X-RAY DIFFRACTION8chain A and resseq 456:479
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 5:17 or resseq 18:30 or resseq 456:479)
10X-RAY DIFFRACTION10chain B and resseq 343:382
11X-RAY DIFFRACTION11chain B and resseq 383:429
12X-RAY DIFFRACTION12chain B and resseq 18:30
13X-RAY DIFFRACTION13chain B and resseq 5:17
14X-RAY DIFFRACTION14chain B and resseq 31:154
15X-RAY DIFFRACTION15chain B and resseq 430:455
16X-RAY DIFFRACTION16chain B and resseq 239:322
17X-RAY DIFFRACTION17chain B and resseq 456:479
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 5:17 or resseq 18:30 or resseq 456:479)
19X-RAY DIFFRACTION19chain C and resseq 539:581
20X-RAY DIFFRACTION20chain C and resseq 610:634
21X-RAY DIFFRACTION21chain C and not (resseq 539:581 or resseq 610:634)
22X-RAY DIFFRACTION22chain D and resseq 539:581
23X-RAY DIFFRACTION23chain D and resseq 610:634
24X-RAY DIFFRACTION24chain D and not (resseq 539:581 or resseq 610:634)
25X-RAY DIFFRACTION25chain E or chain F
26X-RAY DIFFRACTION26chain G or chain H
27X-RAY DIFFRACTION27chain F and resid 0
28X-RAY DIFFRACTION28chain H and resid 0

+
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